Biotechnologies from Marine Bivalves

  • Paola VenierEmail author
  • Marco Gerdol
  • Stefania Domeneghetti
  • Nidhi Sharma
  • Alberto Pallavicini
  • Umberto Rosani
Open Access


Bivalve molluscs comprise more than 9000 extant species. A number of them are traditionally farmed worldwide and are fundamental in the functioning of benthic ecosystems. The peculiarities of marine bivalves have inspired versatile biotechnological tools for coastal pollution monitoring and several new biomimetic materials. Moreover, large amounts of sequence data available for some farmed bivalve species can be used to unveil the organism’s responses to environmental factors (e.g. global climate change, emergence of new infectious agents and other production problems). In bivalves, data from genomics and transcriptomics increases more quickly than data from other omics, and permit new bioinformatics inferences, real comparative genomics and the study of molecules suitable for biotechnological innovations. Bivalves (and their microorganism communities) produce a variety of bioactive peptides, proteins and metabolites. Among them, the numerous families of antimicrobial peptides identified in the Mediterranean mussel likely contribute to its vigour and could assist with the identification of molecular scaffolds for innovative pharmaceuticals, nutraceuticals and constructs suitable for other applications.


Marine bivalve molluscs Biotechnology Mytilus Crassostrea Ruditapes DNA microarray High-throughput sequencing Byssus Biomimetic Antimicrobial 


双壳类软体动物由9,000多种现存物种组成。其中一些全球分布物种有着比较悠久的养殖历史,并且是底栖生态系统的基础物种。海水双壳贝类的生长及生理学特性为海岸污染监测和创新仿生物材料研发提供了多种多样的生物技术工具。受到海水双壳贝类生物学特性的启发,研究人员研发了一些用于沿海污染监测的通用生物技术工具及数种新仿生材料。此外,大量的养殖双壳贝类的测序数据可以用来揭示生物体对环境因素变化的响应(如全球气候变化,新型传染病和其他养殖问题)。双壳贝类的转录组学和基因组资源比其它组学数据的增长要快得多,从而使针对这一动物类群的新的生物信息学预测、真正的比较基因组学和适用于生物技术创新的分子研究成为可行。双壳贝类(及其微生物群落)会产生多种生物活性肽、蛋白质和代谢物。其中,在地中海贻贝中鉴别出多种可能有助于增强贻贝活力的抗菌肽家族成员,为开发新型药物、营养制品等提供了分子骨架模 板.


软体双壳贝类 · 生物技术, 贻贝 · 牡蛎;蛤 · DNA微阵列 · 高通量测序 · 足丝 · 仿生 · 抗菌剂 

6.1 Introduction

Technologies based on the peculiarities of marine bivalves not only provide services and products of current use but are expected to grow in the future, owing to the great exploration power of current omics strategies (high-throughput production of different sorts of molecular data aimed at the complete interpretation of biological structures, functions, and dynamics) and to the surprising advances of life sciences, material and nanomaterial sciences and microelectronics engineering. Undeniably, the growing number of bivalve-inspired innovations add value to animal species already identified as fundamental components of marine benthic ecosystems and regarded as a strategic food resource for the future (the European aquaculture production of marine molluscs reached 572,957 tons, nearly 3.5% of the global amount, with an estimated value of 972,987 USD in 2016) (FAO 2018).

6.2 Living Monitors and Source of Versatile Biotechnological Tools

Since the mid ‘70s, filter-feeding bivalves such as mussels and clams started to be used as pollution sentinels because they integrate in space and time the contaminant mixtures present in the surrounding water and sediments, respectively (Goldberg and Bertine 2000). Complementary to the analysis of toxicants in the soft tissues (Guéguen et al. 2011; Melwani et al. 2014), various pollution biomarkers have been developed and a number of them has been validated (Moore et al. 2006; Banni et al. 2007; Bolognesi and Hayashi 2011) and combined (Pytharopoulou et al. 2008; Okay et al. 2016) to rank coastal sites according to the intensity of toxicant-induced adverse effects.

Over time, the increasing availability of nucleotide sequence data inspired the production of DNA microarrays, adaptable biotechnological tools made of spotted DNA/cDNA or in situ synthesized oligonucleotides (Table 6.1). Such predefined assemblies of molecular probes allow the multiple and quantitative assessment of gene expression levels, among other purposes.
Table 6.1

Gene expression datasets and DNA microarray platforms available for selected marine bivalves




Crassostrea gigas



Crassostrea virginica



Mytilus galloprovincialis



Ruditapes philippinarum



Mytilus californianus



Mytilus edulis



Ruditapes decussatus



Mytilus trossulus



Pinctada maxima



Pinctada fucata



Mercenaria mercenaria



Chamelea gallina



Pinctada martensii



From Gene Expression Omnibus at Aug 2018 (

aGPL22172 probes from Crassostrea angulata, Crassostrea ariakensis, C. gigas, C. virginica, M. californianus, Mytilus chilensis, Mytilus coruscus, M. edulis, M. galloprovincialis, M. trossulus and Venerupis (Ruditapes) philippinarum

bGPL3994 probes from C. gigas and C. virginica

The hybridization of processed RNA samples on DNA microarray slides could discriminate Mytilus mussels and Ruditapes clams sampled at different distance from a petro-chemical district in the Venice lagoon area (Venier et al. 2006; Milan et al. 2015), supporting the use of transcriptional profiles in environmental monitoring and suggesting an innovative way to assess quality and the possible illegal origin of traded stocks.

Tissue- stage- and sex-specific transcript profiles obtained by DNA microarrays can assist management actions and sustainability plans in the farming of bivalves. For instance, they have been used to understand the partial sterility of triploid oysters and genes related to growth and reproduction (Dheilly et al. 2014; Guan et al. 2017; Tong et al. 2015) or the oyster response to pathogens and stress factors negatively impacting the production rates (Venier et al. 2011; Anderson et al. 2015; Romero et al. 2015; Pardo et al. 2016). Relevant to the growth of the pearl oyster Pinctada fucata, gene expression profiles obtained during larval development highlighted new aspects of shell formation mechanisms (Liu et al. 2015).

Both high-throughput sequencing and a DNA microarray were used to investigate the early mussel response to algal toxins with the aim of developing new monitoring tools for okadaic acid, a heat-stable phosphatase inhibitor causing diarrhetic shellfish poisoning (Suarez-Ulloa et al. 2015). A total of “1,066,985” nucleotide sequences (at 10.08.2018) and “3,478” GEO datasets (at 10.08.2018) are available at NCBI for Bivalvia (10 Aug 2018) and the genomes of nine marine bivalves (oysters: C. gigas, C. virginica, P. fucata martensii; mussels: Bathymodiolus platifrons, M. galloprovincialis, Modiolus philippinarum, Limnoperna fortunei; scallops: Mizuhopecten yessoensis; clam Ruditapes philippinarum) have been completed or drafted (Zhang et al. 2012; Takeuchi et al. 2012; Murgarella et al. 2016; Mun et al. 2017; Sun et al. 2017; Wang et al. 2017a, b; Du et al. 2017).

Different from the DNA microarray analysis, high-throughput sequencing can lead to gene discovery and to the validation of population genetics markers for breeding programmes. The identification of single nucleotide polymorphisms (SNPs, codominant-inherited molecular features very abundant in animal genomes) in bivalves is just a preliminary step, before starting to validate their association with valuable quantitatively inherited traits or with stress-responsive genes, and to proceed with fine linkage mapping and population genetics analyses (Coppe et al. 2012; Ge et al. 2015; Nie et al. 2015; Dong et al. 2016; Fan et al. 2016; Wang et al. 2016a, b; Qi et al. 2017; Gutierrez et al. 2017; Azéma et al. 2017).

Although proteomics, metabolomics and epigenetics studies in marine bivalves are at their onset (Gómez-Chiarri et al. 2015; Digilio et al. 2016; Dineshram et al. 2016; Vincenzetti et al. 2017), in the near future they could reinforce and widen the existing assortment of bivalve services and products. In essence, the comprehensive knowledge of the vital processes in marine bivalves is a fundamental research strategy, consistent with the growth of a sustainable and innovative blue economy for the future. To confirm the continuous attention to marine bivalves and their expanding roles, they have been proposed in Northern Europe as living monitors of multidrug-resistant Escherichia coli and other Enterobacteriaceae spp. (Grevskott et al. 2017).

In the following section, we present a paradigmatic case which illustrates how the natural properties of bivalve byssus has guided the development of new materials of practical use.

6.3 Byssal Threads and Adhesive Plaques as Archetypes for New Biomimetics

Some freshwater and marine bivalves such as Dreissena polymorpha, Perna viridis and Mytilus spp. anchor themselves to hard substrates by means of silk-like byssus threads, having remarkable mechanical properties, and adhesive plaque proteins, functioning as an underwater superglue.

Descriptions of the general structure and microscopical anatomy of mussel byssus date back to 1711 and 1877, respectively, but only in the early 1950s investigations based on mechanical, chemical and enzymatic assays, histological and histochemical techniques, polarized light and X-ray diffraction, paved the way to bivalve-inspired materials for medical and non-medical applications (Fig. 6.1) (Brown 1952; Smyth 1954; Deming 1999; Lee et al. 2011; Kord Forooshani and Lee 2017).
Fig. 6.1

Graphical representations of mussel byssus threads (left, as reported in Deming 1999) and anatomy of the byssus production in Mytilus (right, as reported in Smyth 1954). Gland tissue cells, detectable in precise zones of the mussel foot, emit a thread-like protein secretion along the foot groove whereas cells coating the foot groove secrete the protein components of the terminal adhesive plaque (disk). The byssus thread is released when it occupies the whole groove length

The proteinaceous byssus fibers comprise a proximal stem region, a mid-thread region and the terminal adhesive plaque. Mussel byssogenesis occurs in the post-larval stages within minutes by coordinated secretion and extracellular solidification of a composite fluid released by three pedal glands into the distal depression and ventral groove of the foot organ (Silverman and Roberto 2010; Priemel et al. 2017). More than ten types of secreted proteins compose the mussel byssus, including fibrillar collagens, non-collagenous thread matrix proteins and polyphenolic proteins of the thin cuticle surrounding the stretchy fibrous core and the adhesive plaque. As a result of post-translational hydroxylation of tyrosine, L-3,4-dihydroxyphenylalanine (L-DOPA) is a main component of the latter proteins, commonly named mussel foot proteins (Mfp, not to be confused with other proteins with the same acronym) or mussel adhesive proteins.

The unusual resistance of such fibrous and adhesive structure against predators and the mechanical force of waves and currents has considerably stimulated multidisciplinary investigations aimed to develop innovative biomimetic materials (Degtyar et al. 2014; Reinecke et al. 2016; Priemel et al. 2017). In the byssus thread, non-covalent protein–metal interactions stabilize the main constituent proteins and contribute to their tensile strength and self-healing properties. In detail, the thread core is made by bundles of collagenous proteins (preCols) having a central collagen domain with a typical Gly-X-Y triple helical repeat and flanking domains. Among other features, all preCols have N- and C-termini enriched in histidine, the amino acid most likely involved in coordination bonds with transition metal ions such as Zn and Cu. In essence, highly directional and dynamic protein–metal coordination bonds generate cross-linking and hierarchical structuring of byssal protein blocks, with the metal site geometry and activity governed by local charges, helical dipoles and other conformational protein elements. Rupture and rapid restructuring of coordination bonds between histidine residues and Zn2+ sustain the self-healing of byssus and, as expected, such self-healing can be inhibited by removing metal ions with ethylenediaminotetraacetic acid or by lowering the pH, a condition known to hamper histidine–metal bonding (Degtyar et al. 2014; Reinecke et al. 2016).

In the byssus plaque of Mytilus species, at least six Mfp rich in DOPA and cationic amino acids contribute with specialized roles to the adhesion in wet conditions to hard substrates (Table 6.2). The catechol moiety of L-DOPA permits the formation of hydrogen bonds and the interactions with other aromatic rings and with positively charged ions such as Cu2+, Zn2+, Mn2+ and Fe3+ among others. At sea water pH (mildly basic), these chemical events result in stable coordination complexes (e.g. DOPA oxidation coupled with the reduction of coordinated Fe3+ ions) and cross-linking (e.g. catechols oxidized to quinones can react with various nucleophilic groups and produce intermolecular/interfacial covalent bonds). After secretion, the spontaneous DOPA-Fe cross-linking in the byssus coating acts like a protective varnish as a result of attained hardness and extensibility. The local distribution of different Mfp and the significant presence of positively charged ions in the byssus plaque additionally stabilize its foamy structure and boost cohesive interactions and, hence, enhance the strong (wet) adhesion to hard surfaces (Lee et al. 2011; Reinecke et al. 2016; Kord Forooshani and Lee 2017; Priemel et al. 2017).
Table 6.2

Some data on the mussel foot proteins (from Kord Foreooshani and Lee 2017)








Molecular weight (Kda)







Isoelectric pointc







Secondary structure

Very little

Highly repetitive motifs; 6 mol % Cys

No repeats; 30–35 variants rich in DOPA (>20 to 28 mol %): MFP-3f and Mfp-3s are rich in Gly (25–29 mol %), MFP-3f is highly hydrophililic; MFP-3s is polar but hydrophobic

His-rich decapeptide tandeml y repeated more than 36 times

Just 2 closely related variants; rich in DOPA (30 mol%), cationic ami no acids (27.7 mol %) and phosphoserine (≈4.8 mol%); hydrophilic

Rich in Tyr (20 mol %) mostly not converted in DOPA (3 mol %) and in Cys (11 mol%); the richest in charged aminoacids (23 mol% cationic, 16 mol% anionic)

Proposed role

Protective coating

It is the most abundant protein (≈25 wt %); its disulphide bonds support plaque integrity

It contributes to adhesion at the plaque-surface interphase

Exceptional binding to transition metal ions, functional bridge between thread (PreCol) and plaque proteins

It contributes to adhesion at the plaque-surface interphase

It contributes to adhesion at the plaque-surface interphase; it likely controls the redox chemistry of DOPA in the other plaque proteins

ain Mytilus edulis

bin Mytilus californianus

cfrom Lee et al. (2011)

Using Mf3 as an example, the multiple alignment of 36 protein sequences available in GenBank highlights fully conserved amino acid residues and variable sequence traits (Fig. 6.2).
Fig. 6.2

Multiple alignment of amino acid sequences of 36 mussel foot proteins (Mfp 3). GenBank accession number, consensus sequence and sequence logo (i.e. graphical representation of the conservation extent of each protein residue) are reported

In essence, the byssus threads and their terminal plaques have emerged as a model for the development of self-healing polymers and water-resistant adhesive materials (Holten-Andersen et al. 2011; Danner et al. 2012; Guerette et al. 2013; Park et al. 2013; Liu et al. 2014; Fullenkamp et al. 2014; Schmidt et al. 2014; Wu et al. 2014; Nichols 2015; Ryu et al. 2015; Grindy et al. 2015; Miller et al. 2015; Tian et al. 2015; Krogsgaard et al. 2016; Liu et al. 2016; Xu et al. 2016; Zhang et al. 2017b; Waite 2017). In both cases, the coordination of metal ions plays a fundamental role; however, the occurring chemical events and final material properties depend on metals and ligands, their molar ratio, pH and redox reactions. Actually, catechols are regarded as suitable anchoring groups for surface modification, although their metal-binding strength depends on the oxidation status. Other byssogenic bivalves produce somewhat different foot proteins yet capable of strong adhesion, e.g. pvfp-1 from Perna viridis contains C(2)-mannosyl-7-hydroxytryptophan, Man7OHTrp, instead of DOPA, and trimerized chains instead of monomeric chains (Hwang et al. 2012). Deep understanding of the complex chemico-physical processes underlying the byssus formation as well as comparative data deriving from the omics technologies (Schultz and Adema 2017) should provide additional hints for a step-by-step development of useful novelties. As long as the new materials mimic natural substances and processes, they should have a great chance to be efficiently produced in environmentally friendly conditions and to be biodegradable. The development of wet adhesive materials using molluscan models could enable the development of new surgical adhesives, artificial joints, contact lenses, dental sealants and hair and skin conditioners (Wu et al. 2014; Nichols 2015; Ryu et al. 2015; Grindy et al. 2015; Miller et al. 2015; Tian et al. 2015). Moreover, byssus-inspired bioadhesive polymers, polymer blends and micro- or nano-structures have been proposed to fabricate new drug delivery or diagnostic systems including the encapsulation of therapeutic, prophylactic, diagnostic agents to deliver bioactive components expected to be released upon contact with mucosal tissues of aquatic organisms. One could also imagine the development of biodegradable and nutritionally attractive feed formulations containing biocidal or antibiotic compounds and/or microbes, for the prevention and control of invasive non-indigenous species or for selective nutritional feed ingredients for more efficient growth of farmed species (Ma et al. 2016; Wang et al. 2016a, b, 2017a, b; Li et al. 2017; Luo and Liu 2017; Zhang et al. 2017a). Patents describing byssus-inspired inventions are exemplified in Table 6.3.
Table 6.3

Examples of patents describing byssus-inspired inventions (from Google patents)


Registration date

Pubblication date

Candidate Appointee





Genex Corporation

Bioadhesive coding sequences




Enzon Labs Inc.

Method of producing bioadhesive protein




Battelle Energy Alliance, Llc.

Cloning and expression of recombinant adhesive protein Mefp-1 of the blue mussel, Mytilus edulis




Spherics, Inc.

Bioadhesive polymers with catechol functionality




Spherics, Inc.

Bioadhesive polymers

CA 2864891A1



Advanced Bionutrition Corporation and others

Compositions and methods for target delivering a bioactive agent to aquatic organisms




Ramot At Tel-Aviv University Ltd.

Self-assembled micro-and nanostructures

Reversing the scope, new lubricant-infused coatings are now suggested as an effective strategy to prevent the mussel adhesion and, hence, to mitigate marine biofouling (Amini et al. 2017).

6.4 Antimicrobials and Other Bioactive Molecules from Marine Bivalves Are Valuable Assets

The search of bioactive molecules of marine origin dates back to the past century but continues to generate pharmaceutics of human use and new compounds (1340 in 2015) (Liu et al. 2009; Mayer et al. 2010; García-Fernández et al. 2016; Kwon et al. 2016; Anjum et al. 2017; Blunt et al. 2017; Kang et al. 2017).

Marine species including plants, animals and microorganisms (mostly unculturable and unknown) are a rich source of gene-encoded products and metabolites whose molecular moieties mediate biological activities potentially exploitable for new inventions or for the repositioning/reinvention of known bioactive components (pharmaceuticals and nutraceuticals, among others). For instance, inhibitors of proteases and voltage-gated ion channels have been isolated from marine venomous animals such as sea anemones and Conus snails and are currently studied for their therapeutical and biotechnological potential (Liu et al. 2009; García-Fernández et al. 2016; Kwon et al. 2016). In the ‘90s, the cloning of the green florescent protein from the jellyfish Aequoria victoria and production of mutants opened the way to use these chromo proteins as probes in cell and tissue imaging (Prasher et al. 1992; Verkhusha and Lukyanov 2004; Chen et al. 2013). Both discoveries have driven significant advancements in the field of life sciences. In the discovery phase, the bioactivity is often claimed following in vitro demonstration of antibacterial/ antifungal/ antiviral, anti-proliferative and anti-tumor properties, although the latter must be demonstrated in vivo with adequate study design and high costs. It should be noted that different human ethnic groups have traditionally used molluscs and mollusc extracts for their anti-inflammatory, immune-modulatory and wound healing properties. Molluscan species were estimated to be the source of more than 1145 products by 2014. Liprinol® and Biolane Seatone from the green-lipped mussel Perna canaliculus exemplify marketed products of current use, the potent analgesic ziconotide from Conus snails has been clinically tested and approved by the Food and Drug Administration whereas other compounds are under trial (Ahmad et al. 2018).

Owing to their filtering activity, marine bivalves interact with putative pathogens including bacteria and viruses, and, thus, are expected to possess effective defence mechanisms. Nowadays, bioinformatic approaches accelerate the identification and guide the functional characterization of bioactive molecules from non-model bivalve species. In Mytilus galloprovincialis, the Mediterranean mussel, many families of putative cysteine-stabilized antimicrobials have been described. Mytilins, defensins, myticins and mytimycins were reported in the ‘90s (Hubert et al. 1996; Charlet et al. 1996) whereas big defensins, mytimacins, CRP I and the linear myticalin peptides were more recently discovered (Gerdol et al. 2012; Gerdol et al. 2015; Leoni et al. 2017). Among all of them, myticin C displayed high gene transcript polymorphism, constitutive and microbe-inducible expression, chemokine-like and antiviral activities. Although the action mode of myticin C is still unclear, an engineered construct with superior antiviral activity has been developed (Pallavicini et al. 2008; Novoa et al. 2016). As additional example, Mytichitin CB from Mytilus coruscus is a chitotriosidase-like antimicrobial which displays antifungal activity whose recombinant production should permit its full characterization (Qin et al. 2014; Meng et al. 2016).

While no mussel antimicrobial peptide (AMP) has been commercially exploited yet, some pilot studies have been carried out over the years, demonstrating the potential biotechnological applications of engineered peptides. Indeed, synthetic mytilin-derived peptides were capable or reducing mortality in virus-infected shrimp (white-spot syndrome) (Dupuy et al. 2004). Interesting antiviral, antibacterial and antiprotozoan activities also have been demonstrated for engineered defensin and mytilin variants (Dupuy et al. 2004; Liu et al. 2010).

Additional bivalve molecules could be regarded as having therapeutic potential. For instance, the mussel MytiLec-1 is a galactose-binding lectin able to inhibit the growth of both Gram-positive and Gram-negative bacteria (Hasan et al. 2016) and, at the same time, able to bind Burkitt’s lymphoma and breast cancer cells expressing globotriose on their surface, significantly inducing apoptosis (Hasan et al. 2015; Liao et al. 2016; Chernikov et al. 2017). These remarkable properties have led to the computational design of an artificial β-trefoil lectin, named Mitsuba, capable of recognizing globotriose-expressing cancer cells, as an initial step for the development of effective MytiLec-1-based cancer treatment or diagnostics tools (Terada et al. 2017).

Other molluscan lectins with biotechnological potential are two C-type lectins from C. gigas (CgCLec-4, CgCLec-5), which exhibited anti-microbial (agglutinating) activity against bacteria and fungi (Jia et al. 2016). One extrapallial protein (C1Q-domain containing protein) of the mussel hemolymph serum (MgEP) was also demonstrated to act as an opsonin and to promote interactions between a suspected Vibrio pathogen and Mytilus hemocytes (Canesi et al. 2016).

In addition to ethanolic extracts, hydrolysates obtained by enzymatic digestion from bivalves and other marine invertebrates, revealed tens of antioxidant peptides which could benefit health or be used to produce novel food products (Chai et al. 2017; Odeleye et al. 2016; Wu and Huang 2017). Almost certainly, there are many more bioactive mollusc/bivalve components yet to be investigated. Regardless of the current state of knowledge of molluscan bioactives, we should never forget the possibility of toxic substances co-occurring in the same biological matrix.

6.5 Conclusions and Perspectives

This paper has presented a historical and conceptual timeline of the products and services provided by marine bivalve molluscs, focusing the attention to biotechnological innovations for a sustainable future. Marine bivalves with their associated microorganisms are central in the marine trophic networks, from the shoreline to the deep ocean. Bivalve species are traditionally fished and farmed worldwide as seafood since ancient times whereas their use as water pollution sentinels was established far more recently. Our time testifies great progresses in life sciences and, accordingly, further research on marine bivalves will likely confirm them as rich source of bioactive compounds and as interesting models for technological innovations (Imhoff et al. 2011; Desriac et al. 2014; Newman 2016). Today, the CRISP/CAS genome editing biotechnology represents a new revolutionary strategy also to engineer and implement bivalve-inspired products (Mojica and Montoliu 2016; Singh et al. 2018). As our knowledge base expands based on a multifaceted blue economy, there is little doubt that discoveries in this field will lead to societal and economic benefit in the near future.



We thank the Editor of this Springer book for his attention to the author’s work. This work was partially funded by the University of Padova-Department of Biology (BIRD168432-2016 to U. Rosani) and by the University of Trieste (Finanziamento di Ateneo per la Ricerca Scientifica 2015 to M. Gerdol). The affiliation institutions had no role in the chapter contents. The authors acknowledge prof. A. Alfaro for the review and her valuable comments.


  1. Ahmad TB, Liu L, Kotiw M, Benkendorff K (2018) Review of anti-inflammatory, immune-modulatory and wound healing properties of molluscs. J Ethnopharmacol 210:156–178. CrossRefPubMedGoogle Scholar
  2. Amini S, Kolle S, Petrone L, Ahanotu O, Sunny S, Sutanto CN, Hoon S, Cohen L, Weaver JC, Aizenberg J, Vogel N, Miserez A (2017) Preventing mussel adhesion using lubricant-infused materials. Science 357(6352):668–673. CrossRefPubMedGoogle Scholar
  3. Anderson K, Taylor DA, Thompson EL, Melwani AR, Nair SV, Raftos DA (2015) Meta-analysis of studies using suppression subtractive hybridization and microarrays to investigate the effects of environmental stress on gene transcription in oysters. PLoS One 10(3):e0118839. CrossRefPubMedPubMedCentralGoogle Scholar
  4. Anjum K, Abbas SQ, Akhter N, Shagufta BI, Shah SAA, Hassan SSU (2017) Emerging biopharmaceuticals from bioactive peptides derived from marine organisms. Chem Biol Drug Des 90(1):12–30. CrossRefPubMedGoogle Scholar
  5. Azéma P, Lamy JB, Boudry P, Renault T, Travers MA, Dégremont L (2017) Genetic parameters of resistance to Vibrio aestuarianus, and OsHV-1 infections in the Pacific oyster, Crassostrea gigas, at three different life stages. Genet Sel Evol 49(1):23. CrossRefPubMedPubMedCentralGoogle Scholar
  6. Banni M, Dondero F, Jebali J, Guerbej H, Boussetta H, Viarengo A (2007) Assessment of heavy metal contamination using real-time PCR analysis of mussel metallothionein mt10 and mt20 expression: a validation along the Tunisian coast. Biomarkers 12(4):369–383. CrossRefPubMedGoogle Scholar
  7. Blunt JW, Copp BR, Keyzers RA, Munro MHG, Prinsep MR (2017) Marine natural products. Nat Prod Rep 34(3):235–294. CrossRefPubMedGoogle Scholar
  8. Bolognesi C, Hayashi M (2011) Micronucleus assay in aquatic animals. Mutagenesis 26(1):205–213. CrossRefPubMedGoogle Scholar
  9. Brown CH (1952) Some structural proteins of Mytilus edulis. J Cell Sci s3–93:487–502Google Scholar
  10. Canesi L, Grande C, Pezzati E, Balbi T, Vezzulli L, Pruzzo C (2016) Killing of Vibrio cholerae and Escherichia coli strains carrying D-mannose-sensitive ligands by Mytilus hemocytes is promoted by a multifunctional hemolymph serum protein. Microb Ecol 72(4):759–762. CrossRefPubMedGoogle Scholar
  11. Chai TT, Law YC, Wong FC, Kim SK (2017) Enzyme-assisted discovery of antioxidant peptides from edible marine invertebrates: a review. Mar Drugs 15(2). CrossRefGoogle Scholar
  12. Charlet M, Chernysh S, Philippe H, Hetru C, Hoffmann JA, Bulet P (1996) Innate immunity. Isolation of several cysteine-rich antimicrobial peptides from the blood of a mollusc Mytilus edulis. J Biol Chem 271:21808–21813CrossRefGoogle Scholar
  13. Chen SF, Ferré N, Liu YJ (2013) QM/MM study on the light emitters of aequorin chemiluminescence, bioluminescence, and fluorescence: a general understanding of the bioluminescence of several marine organisms. Chemistry 19(26):8466–8472. CrossRefPubMedGoogle Scholar
  14. Chernikov O, Kuzmich A, Chikalovets I, Molchanova V, Hua KF (2017) Lectin CGL from the sea mussel Crenomytilus grayanus induces Burkitt’s lymphoma cells death via interaction with surface glycan. Int J Biol Macromol 104(Pt A):508–514. CrossRefPubMedGoogle Scholar
  15. Coppe A, Bortoluzzi S, Murari G, Marino IA, Zane L, Papetti C (2012) Sequencing and characterization of striped venus transcriptome expand resources for clam fishery genetics. PLoS One 7(9):e44185. CrossRefPubMedPubMedCentralGoogle Scholar
  16. Danner EW, Kan Y, Hammer MU, Israelachvili JN, Waite JH (2012) Adhesion of mussel foot protein Mefp-5 to mica: an underwater superglue. Biochemistry 51(33):6511–6518. CrossRefPubMedPubMedCentralGoogle Scholar
  17. Degtyar E, Harrington MJ, Politi Y, Fratzl P (2014) The mechanical role of metal ions in biogenic protein-based materials. Angew Chem Int Ed Engl 53(45):12026–12044. CrossRefPubMedGoogle Scholar
  18. Deming T (1999) Mussel byssus and biomolecular materials. Curr Opin Chem Biol 3(1):100–105CrossRefGoogle Scholar
  19. Desriac F, Le Chevalier P, Brillet B, Leguerinel I, Thuillier B, Paillard C, Fleury Y (2014) Exploring the hologenome concept in marine bivalvia: haemolymph microbiota as a pertinent source of probiotics for aquaculture. FEMS Microbiol Lett 350(1):107–116. CrossRefPubMedGoogle Scholar
  20. Dheilly NM, Jouaux A, Boudry P, Favrel P, Lelong C (2014) Transcriptomic profiling of gametogenesis in triploid Pacific oysters Crassostrea gigas: towards an understanding of partial sterility associated with triploidy. PLoS One 9(11):e112094. CrossRefPubMedPubMedCentralGoogle Scholar
  21. Digilio G, Sforzini S, Cassino C, Robotti E, Oliveri C, Marengo E, Musso D, Osella D, Viarengo A (2016) Haemolymph from Mytilus galloprovincialis: response to copper and temperature challenges studied by (1)H-NMR metabonomics. Comp Biochem Physiol C Toxicol Pharmacol 183–184:61–71. CrossRefPubMedGoogle Scholar
  22. Dineshram R, Chandramouli K, Ko GW, Zhang H, Qian PY, Ravasi T, Thiyagarajan V (2016) Quantitative analysis of oyster larval proteome provides new insights into the effects of multiple climate change stressors. Glob Chang Biol 22(6):2054–2068. CrossRefPubMedGoogle Scholar
  23. Dong YH, Yao HH, Sun CS, Lv DM, Li MQ, Lin ZH (2016) Development of polymorphic SSR markers in the razor clam (Sinonovacula constricta) and cross-species amplification. Genet Mol Res 15(1).
  24. Du X, Fan G, Jiao Y, Zhang H, Guo X, Huang R, Zheng Z, Bian C, Deng Y, Wang Q, Wang Z, Liang X, Liang H, Shi C, Zhao X, Sun F, Hao R, Bai J, Liu J, Chen W, Liang J, Liu W, Xu Z, Shi Q, Xu X, Zhang G, Liu X (2017) The pearl oyster Pinctada fucata martensii genome and multi-omic analyses provide insights into biomineralization. Gigascience 6(8):1–12. CrossRefPubMedPubMedCentralGoogle Scholar
  25. Dupuy JW, Bonami JR, Roch P (2004) A synthetic antibacterial peptide from Mytilus galloprovincialis reduces mortality due to white spot syndrome virus in palaemonid shrimp. J Fish Dis 27(1):57–64CrossRefGoogle Scholar
  26. Fan SG, Wei JF, Guo YH, Huang GJ, Yu DH (2016) Development of coding single nucleotide polymorphic markers in the pearl oyster Pinctada fucata based on next-generation sequencing and high-resolution melting analysis. Genet Mol Res 15(4).
  27. FAO (2018) Fisheries and Aquaculture Information and Statistics Branch., accessed on line 08/2018
  28. Fullenkamp DE, Barrett DG, Miller DR, Kurutz JW, Messersmith PB (2014) pH-dependent cross-linking of catechols through oxidation via Fe3+ and potential implications for mussel adhesion. RSC Adv 4(48):25127–25134. CrossRefPubMedPubMedCentralGoogle Scholar
  29. García-Fernández R, Peigneur S, Pons T, Alvarez C, González L, Chávez MA, Tytgat J (2016) The Kunitz-type protein ShPI-1 inhibits serine proteases and voltage-gated potassium channels. Toxins (Basel) 8(4):110. CrossRefGoogle Scholar
  30. Ge J, Li Q, Yu H, Kong L (2015) Identification of single-locus PCR-based markers linked to shell background color in the pacific oyster (Crassostrea gigas). Mar Biotechnol (NY) 17(5):655–662. CrossRefGoogle Scholar
  31. Gerdol M, De Moro G, Manfrin C, Venier P, Pallavicini A (2012) Big defensins and mytimacins, new AMP families of the Mediterranean mussel Mytilus galloprovincialis. Dev Comp Immunol 36(2):390–399. CrossRefPubMedGoogle Scholar
  32. Gerdol M, Puillandre N, De Moro G, Guarnaccia C, Lucafò M, Benincasa M, Zlatev V, Manfrin C, Torboli V, Giulianini PG, Sava G, Venier P, Pallavicini A (2015) Identification and characterization of a novel family of cysteine-rich peptides (MgCRP-I) from Mytilus galloprovincialis. Genome Biol Evol 7(8):2203–2219. CrossRefPubMedPubMedCentralGoogle Scholar
  33. Goldberg ED, Bertine KK (2000) Beyond the mussel watch – new directions for monitoring marine pollution. Sci Total Environ 247(2-3):165–174CrossRefGoogle Scholar
  34. Gómez-Chiarri M, Guo X, Tanguy A, He Y, Proestou D (2015) The use of -omic tools in the study of disease processes in marine bivalve mollusks. J Invertebr Pathol 131:137–154. CrossRefPubMedGoogle Scholar
  35. Grevskott DH, Svanevik CS, Sunde M, Wester AL, Lunestad BT (2017) Marine bivalve mollusks as possible indicators of multidrug-resistant Escherichia coli and other species of the Enterobacteriaceae family. Front Microbiol 8:24. CrossRefPubMedPubMedCentralGoogle Scholar
  36. Grindy SC, Learsch R, Mozhdehi D, Cheng J, Barrett DG, Guan Z, Messersmith PB, Holten-Andersen N (2015) Control of hierarchical polymer mechanics with bioinspired metal-coordination dynamics. Nat Mater 14(12):1210–1216. CrossRefPubMedPubMedCentralGoogle Scholar
  37. Guan Y, He M, Wu H (2017) Differential mantle transcriptomics and characterization of growth-related genes in the diploid and triploid pearl oyster Pinctada fucata. Mar Genomics 33:31–38. CrossRefPubMedGoogle Scholar
  38. Guéguen M, Amiard JC, Arnich N, Badot PM, Claisse D, Guérin T, Vernoux JP (2011) Shellfish and residual chemical contaminants: hazards, monitoring, and health risk assessment along French coasts. Rev Environ Contam Toxicol 213:55–111. CrossRefPubMedGoogle Scholar
  39. Guerette PA, Hoon S, Seow Y, Raida M, Masic A, Wong FT, Ho VH, Kong KW, Demirel MC, Pena-Francesch A, Amini S, Tay GZ, Ding D, Miserez A (2013) Accelerating the design of biomimetic materials by integrating RNA-seq with proteomics and materials science. Nat Biotechnol 31(10):908–915. CrossRefPubMedGoogle Scholar
  40. Gutierrez AP, Turner F, Gharbi K, Talbot R, Lowe NR, Peñaloza C, McCullough M, Prodöhl PA, Bean TP, Houston RD (2017) Development of a medium density combined-species SNP array for pacific and european oysters Crassostrea gigas and Ostrea edulis. G3 (Bethesda) 7(7):2209–2218. CrossRefGoogle Scholar
  41. Hasan I, Sugawara S, Fujii Y, Koide Y, Terada D, Iimura N, Fujiwara T, Takahashi KG, Kojima N, Rajia S, Kawsar SM, Kanaly RA, Uchiyama H, Hosono M, Ogawa Y, Fujita H, Hamako J, Matsui T, Ozeki Y (2015) MytiLec, a mussel R-type lectin, interacts with surface glycan Gb3 on Burkitt’s lymphoma cells to trigger apoptosis through multiple pathways. Mar Drugs 13(12):7377–7389. CrossRefPubMedPubMedCentralGoogle Scholar
  42. Hasan I, Gerdol M, Fujii Y, Rajia S, Koide Y, Yamamoto D, Kawsar SM, Ozeki Y (2016) cDNA and gene structure of MytiLec-1, A bacteriostatic R-Type Lectin from the Mediterranean mussel (Mytilus galloprovincialis). Mar Drugs 14(5). CrossRefGoogle Scholar
  43. Holten-Andersen N, Harrington MJ, Birkedal H, Lee BP, Messersmith PB, Lee KY, Waite JH (2011) pH-induced metal-ligand cross-links inspired by mussel yield self-healing polymer networks with near-covalent elastic moduli. Proc Natl Acad Sci USA 108(7):2651–2655. CrossRefPubMedGoogle Scholar
  44. Hubert F, Noel T, Roch P (1996) A member of the arthropod defensin family from edible Mediterranean mussels (Mytilus galloprovincialis). Eur J Biochem 240(1):302–306 Erratum in (1996) Eur J Biochem 240:815CrossRefGoogle Scholar
  45. Hwang DS, Zeng H, Lu Q, Israelachvili J, Waite JH (2012) Adhesion mechanism in a DOPA-deficient foot protein from green mussels. Soft Matter 8(20):5640–5648. CrossRefPubMedPubMedCentralGoogle Scholar
  46. Imhoff JF, Labes A, Wiese J (2011) Bio-mining the microbial treasures of the ocean: new natural products. Biotechnol Adv 29(5):468–482. CrossRefPubMedGoogle Scholar
  47. Jia Z, Zhang H, Jiang S, Wang M, Wang L, Song L (2016) Comparative study of two single CRD C-type lectins, CgCLec-4 and CgCLec-5, from pacific oyster Crassostrea gigas. Fish Shellfish Immunol 59:220–232. CrossRefPubMedGoogle Scholar
  48. Kang HK, Kim C, Seo CH, Park Y (2017) The therapeutic applications of antimicrobial peptides (AMPs): a patent review. J Microbiol 55(1):1–12. CrossRefPubMedGoogle Scholar
  49. Kord Forooshani P, Lee BP (2017) Recent approaches in designing bioadhesive materials inspired by mussel adhesive protein. J Polym Sci A Polym Chem 55(1):9–33. CrossRefPubMedGoogle Scholar
  50. Krogsgaard M, Nue V, Birkedal H (2016) Mussel-inspired materials: self-healing through coordination chemistry. Chemistry 22(3):844–857. CrossRefPubMedGoogle Scholar
  51. Kwon S, Bosmans F, Kaas Q, Cheneval O, Conibear AC, Rosengren KJ, Wang CK, Schroeder CI, Craik DJ (2016) Efficient enzymatic cyclization of an inhibitory cystine knot-containing peptide. Biotechnol Bioeng 113(10):2202–2212. CrossRefPubMedPubMedCentralGoogle Scholar
  52. Lee BP, Messersmith PB, Israelachvili JN, Waite JH (2011) Mussel-inspired adhesives and coatings. Annu Rev Mater Res 41:99–132. CrossRefPubMedPubMedCentralGoogle Scholar
  53. Leoni G, De Poli A, Mardirossian M, Gambato S, Florian F, Venier P, Wilson DN, Tossi A, Pallavicini A, Gerdol M (2017) Myticalins: a novel multigenic family of linear, cationic antimicrobial peptides from marine mussels (Mytilus spp.). Mar Drugs 15(8). CrossRefGoogle Scholar
  54. Li L, Yan B, Yang J, Huang W, Chen L, Zeng H (2017) Injectable self-healing hydrogel with antimicrobial and antifouling properties. ACS Appl Mater Interfaces 9(11):9221–9225. CrossRefPubMedGoogle Scholar
  55. Liao JH, Chien CT, Wu HY, Huang KF, Wang I, Ho MR, Tu IF, Lee IM, Li W, Shih YL, Wu CY, Lukyanov PA, Hsu ST, Wu SH (2016) A multivalent marine Lectin from Crenomytilus grayanus possesses anti-cancer activity through recognizing Globotriose Gb3. J Am Chem Soc 138(14):4787–4795. CrossRefPubMedGoogle Scholar
  56. Liu Z, Xu N, Hu J, Zhao C, Yu Z, Dai Q (2009) Identification of novel I-superfamily conopeptides from several clades of Conus species found in the South China Sea. Peptides 30(10):1782–1787. CrossRefPubMedGoogle Scholar
  57. Liu M, Wu M, Zhou S, Gao P, Lu T, Wang R, Shi G, Liao Z (2010) Designation, solid-phase synthesis and antimicrobial activity of Mytilin derived peptides based on Mytilin-1 from Mytiluscoruscus. Sheng Wu Gong Cheng Xue Bao 26(4):550–556. In ChineseGoogle Scholar
  58. Liu Z, Qu S, Zheng X, Xiong X, Fu R, Tang K, Zhong Z, Weng J (2014) Effect of polydopamine on the biomimetic mineralization of mussel-inspired calcium phosphate cement in vitro. Mater Sci Eng C Mater Biol Appl 44:44–51. CrossRefPubMedGoogle Scholar
  59. Liu J, Yang D, Liu S, Li S, Xu G, Zheng G, Xie L, Zhang R (2015) Microarray: a global analysis of biomineralization-related gene expression profiles during larval development in the pearl oyster, Pinctada fucata. BMC Genomics 16:325. CrossRefPubMedPubMedCentralGoogle Scholar
  60. Liu M, Zeng G, Wang K, Wan Q, Tao L, Zhang X, Wei Y (2016) Recent developments in polydopamine: an emerging soft matter for surface modification and biomedical applications. Nanoscale 8(38):16819–16840. CrossRefPubMedGoogle Scholar
  61. Luo C, Liu Q (2017) Oxidant-induced high-efficient mussel-inspired modification on PVDF membrane with superhydrophilicity and underwater superoleophobicity characteristics for oil/water separation. ACS Appl Mater Interfaces 9(9):8297–8307. CrossRefPubMedGoogle Scholar
  62. Ma H, Luo J, Sun Z, Xia L, Shi M, Liu M, Chang J, Wu C (2016) 3D printing of biomaterials with mussel-inspired nanostructures for tumor therapy and tissue regeneration. Biomaterials 111:138–148. CrossRefPubMedGoogle Scholar
  63. Mayer AMS, Glaser KB, Cuevas C, Jacobs RS, Kem W, Little RD, McIntosh JM, Newman DJ, Potts BC, Shuster DE (2010) The odyssey of marine pharmaceuticals: a current pipeline perspective. Trends Pharmacol Sci 31(6):255–265. CrossRefPubMedGoogle Scholar
  64. Melwani AR, Gregorio D, Jin Y, Stephenson M, Ichikawa G, Siegel E, Crane D, Lauenstein G, Davis JA (2014) Mussel Watch update: long-term trends in selected contaminants from coastal California, 1977-2010. Mar Pollut Bull 81(2):291–302. CrossRefPubMedGoogle Scholar
  65. Meng DM, Dai HX, Gao XF, Zhao JF, Guo YJ, Ling X, Dong B, Zhang ZQ, Fan ZC (2016) Expression, purification and initial characterization of a novel recombinant antimicrobial peptide Mytichitin-A in Pichia pastoris. Protein Expr Purif 127:35–43. CrossRefPubMedGoogle Scholar
  66. Milan M, Pauletto M, Boffo L, Carrer C, Sorrentino F, Ferrari G, Pavan L, Patarnello T, Bargelloni L (2015) Transcriptomic resources for environmental risk assessment: a case study in the Venice lagoon. Environ Pollut 197:90–98. CrossRefPubMedGoogle Scholar
  67. Miller DR, Das S, Huang KY, Han S, Israelachvili JN, Waite JH (2015) Mussel coating protein-derived complex coacervates mitigate frictional surface damage. ACS BiomaterSci Eng 1(11):1121–1128. CrossRefGoogle Scholar
  68. Mojica FJ, Montoliu L (2016) On the origin of CRISPR-Cas technology: from prokaryotes to mammals. Trends Microbiol 24(10):811–820. CrossRefPubMedGoogle Scholar
  69. Moore MN, Allen JI, McVeigh A, Shaw J (2006) Lysosomal and autophagic reactions as predictive indicators of environmental impact in aquatic animals. Autophagy 2(3):217–220CrossRefGoogle Scholar
  70. Mun S, Kim YJ, Markkandan K, Shin W, Oh S, Woo J, Yoo J, An H, Han K (2017) The whole-genome and transcriptome of the manila clam (Ruditapes philippinarum). Genome Biol Evol 9(6):1487–1498. CrossRefPubMedPubMedCentralGoogle Scholar
  71. Murgarella M, Puiu D, Novoa B, Figueras A, Posada D, Canchaya C (2016) A first insight into the genome of the Filter-Feeder Mussel Mytilus galloprovincialis. PLoS One 11(3):e0151561. Correction in (2016) PLoS One 11(7):e0160081.
  72. Newman DJ (2016) Predominately uncultured microbes as sources of bioactive agents. Front Microbiol 7:1832. CrossRefPubMedPubMedCentralGoogle Scholar
  73. Nichols WT (2015) Designing biomimetic materials from marine organisms. J Nanosci Nanotechnol 15(1):189–191CrossRefGoogle Scholar
  74. Nie Q, Yue X, Liu B (2015) Development of Vibrio spp. infection resistance related SNP markers using multiplex SNaPshot genotyping method in the clam Meretrix meretrix. Fish Shellfish Immunol 43(2):469–476. CrossRefPubMedGoogle Scholar
  75. Novoa B, Romero A, Álvarez ÁL, Moreira R, Pereiro P, Costa MM, Dios S, Estepa A, Parra F, Figueras A (2016) Antiviral activity of myticin C peptide from Mussel: an ancient defense against Herpesviruses. J Virol 90(17):7692–7702. CrossRefPubMedPubMedCentralGoogle Scholar
  76. Odeleye T, Li Y, White WL, Nie S, Chen S, Wang J, Lu J (2016) The antioxidant potential of the New Zealand surf clams. Food Chem 204:141–149. CrossRefPubMedGoogle Scholar
  77. Okay OS, Ozmen M, Güngördü A, Yılmaz A, Yakan SD, Karacık B, Tutak B, Schramm KW (2016) Heavy metal pollution in sediments and mussels: assessment by using pollution indices and metallothionein levels. Environ Monit Assess 188(6):352. CrossRefPubMedGoogle Scholar
  78. Pallavicini A, Costa Mdel M, Gestal C, Dreos R, Figueras A, Venier P, Novoa B (2008) High sequence variability of myticin transcripts in hemocytes of immune-stimulated mussels suggests ancient host-pathogen interactions. Dev Comp Immunol 32(3):213–226. CrossRefPubMedGoogle Scholar
  79. Pardo BG, Álvarez-Dios JA, Cao A, Ramilo A, Gómez-Tato A, Planas JV, Villalba A, Martínez P (2016) Construction of an Ostrea edulis database from genomic and expressed sequence tags (ESTs) obtained from Bonamia ostreae infected haemocytes: development of an immune-enriched oligo-microarray. Fish Shellfish Immunol 59:331–344. CrossRefPubMedGoogle Scholar
  80. Park JY, Yeom J, Kim JS, Lee M, Lee H, Nam YS (2013) Cell-repellant dextran coatings of porous titania using mussel adhesion chemistry. Macromol Biosci 13(11):1511–1519. CrossRefPubMedGoogle Scholar
  81. Prasher DC, Eckenrode VK, Ward WW, Prendergast FG, Cormier MJ (1992) Primary structure of the Aequorea victoria green-fluorescent protein. Gene 111(2):229–233CrossRefGoogle Scholar
  82. Priemel T, Degtyar E, Dean MN, Harrington MJ (2017) Rapid self-assembly of complex biomolecular architectures during mussel byssus biofabrication. Nat Commun 8:14539. CrossRefPubMedPubMedCentralGoogle Scholar
  83. Pytharopoulou S, Sazakli E, Grintzalis K, Georgiou CD, Leotsinidis M, Kalpaxis DL (2008) Translational responses of Mytilus galloprovincialis to environmental pollution: integrating the responses to oxidative stress and other biomarker responses into a general stress index. Aquat Toxicol 89(1):18–27. CrossRefPubMedGoogle Scholar
  84. Qi H, Song K, Li C, Wang W, Li B, Li L, Zhang G (2017) Construction and evaluation of a high-density SNP array for the Pacific oyster (Crassostrea gigas). PLoS One 12(3):e0174007. CrossRefPubMedPubMedCentralGoogle Scholar
  85. Qin CL, Huang W, Zhou SQ, Wang XC, Liu HH, Fan MH, Wang RX, Gao P, Liao Z (2014) Characterization of a novel antimicrobial peptide with chitin-biding domain from Mytilus coruscus. Fish Shellfish Immunol 41(2):362–370. CrossRefPubMedGoogle Scholar
  86. Reinecke A, Bertinetti L, Fratzl P, Harrington MJ (2016) Cooperative behaviour of a sacrificial bond network and elastic framework in providing self-healing capacity in mussel byssal threads. J Struct Biol 196(3):329–339. CrossRefPubMedGoogle Scholar
  87. Romero A, Forn-Cuní G, Moreira R, Milan M, Bargelloni L, Figueras A, Novoa B (2015) An immune-enriched oligo-microarrayanalysis of gene expression in Manila clam (Venerupis philippinarum) haemocytes after a Perkinsus olseni challenge. Fish Shellfish Immunol 43(1):275–286. CrossRefPubMedGoogle Scholar
  88. Ryu JH, Hong S, Lee H (2015) Bio-inspired adhesive catechol-conjugated chitosan for biomedical applications: a mini review. Acta Biomater 27:101–115. CrossRefPubMedGoogle Scholar
  89. Schmidt S, Reinecke A, Wojcik F, Pussak D, Hartmann L, Harrington MJ (2014) Metal-mediated molecular self-healing in histidine-rich mussel peptides. Biomacromolecules 15(5):1644–1652. CrossRefPubMedGoogle Scholar
  90. Schultz JH, Adema CM (2017) Comparative immunogenomics of molluscs. Dev Comp Immunol 75:3–15. CrossRefPubMedPubMedCentralGoogle Scholar
  91. Silverman HG, Roberto FF (2010) Byssus formation in mussel. In: von Byern J, Grunwald I (eds) Biological adhesive systems: from nature to technical and medical application, ch 18. Springer, Wien/New York, pp 273–285, ISBN 978-3-8091-1041-4Google Scholar
  92. Singh RK, Lee JK, Selvaraj C, Singh R, Li J, Kim SY, Kalia VC (2018) Protein engineering approaches in the post-genomic era. Curr Protein Pept Sci 19(1):5–15. CrossRefPubMedGoogle Scholar
  93. Smyth A (1954) Technique for the histochemical demonstration of polyphenol oxidase and its application to egg-shell formation in helminths and byssus formation in Mytilus. J Cell Sci 95(2):139–152Google Scholar
  94. Suarez-Ulloa V, Fernandez-Tajes J, Aguiar-Pulido V, Prego-Faraldo MV, Florez-Barros F, Sexto-Iglesias A, Mendez J, Eirin-Lopez JM (2015) Unbiased high-throughput characterization of mussel transcriptomic responses to sublethal concentrations of the biotoxin okadaic acid. PeerJ 3:e1429. CrossRefPubMedPubMedCentralGoogle Scholar
  95. Sun J, Zhang Y, Xu T, Zhang Y, Mu H, Zhang Y, Lan Y, Fields CJ, Hui JHL, Zhang W, Li R, Nong W, Cheung FKM, Qiu JW, Qian PY (2017) Adaptation to deep-sea chemosynthetic environments as revealed by mussel genomes. Nat Ecol Evol 1(5):121. CrossRefPubMedGoogle Scholar
  96. Takeuchi T, Kawashima T, Koyanagi R, Gyoja F, Tanaka M, Ikuta T, Shoguchi E, Fujiwara M, Shinzato C, Hisata K, Fujie M, Usami T, Nagai K, Maeyama K, Okamoto K, Aoki H, Ishikawa T, Masaoka T, Fujiwara A, Endo K, Endo H, Nagasawa H, Kinoshita S, Asakawa S, Watabe S, Satoh N (2012) Draft genome of the pearl oyster Pinctada fucata: a platform for understanding bivalve biology. DNA Res 19(2):117–130. CrossRefPubMedPubMedCentralGoogle Scholar
  97. Terada D, Voet ARD, Noguchi H, Kamata K, Ohki M, Addy C, Fujii Y, Yamamoto D, Ozeki Y, Tame JRH, Zhang KYJ (2017) Computational design of a symmetrical β-trefoil lectin with cancer cell binding activity. Sci Rep 7(1):5943. CrossRefPubMedPubMedCentralGoogle Scholar
  98. Tian Y, Shen S, Feng J, Jiang X, Yang W (2015) Mussel-inspired gold hollow superparticles for photothermal therapy. Adv Healthc Mater 4(7):1009–1014. CrossRefPubMedGoogle Scholar
  99. Tong Y, Zhang Y, Huang J, Xiao S, Zhang Y, Li J, Chen J, Yu Z (2015) Transcriptomics analysis of Crassostrea hongkongensis for the discovery of reproduction-related genes. PLoS One 10(8):e0134280. CrossRefPubMedPubMedCentralGoogle Scholar
  100. Venier P, De Pittà C, Pallavicini A, Marsano F, Varotto L, Romualdi C, Dondero F, Viarengo A, Lanfranchi G (2006) Development of mussel mRNA profiling: can gene expression trends reveal coastal water pollution? Mutat Res 602(1–2):121–134. CrossRefPubMedGoogle Scholar
  101. Venier P, Varotto L, Rosani U, Millino C, Celegato B, Bernante F, Lanfranchi G, Novoa B, Roch P, Figueras A, Pallavicini A (2011) Insights into the innate immunity of the Mediterranean mussel Mytilus galloprovincialis. BMC Genomics 12:69. CrossRefPubMedPubMedCentralGoogle Scholar
  102. Verkhusha VV, Lukyanov KA (2004) The molecular properties and applications of Anthozoa fluorescent proteins and chromoproteins. Nat Biotechnol 22(3):289–296. CrossRefPubMedGoogle Scholar
  103. Vincenzetti S, Felici A, Ciarrocchi G, Pucciarelli S, Ricciutelli M, Ariani A, Polzonetti V, Polidori P (2017) Comparative proteomic analysis of two clam species: Chamelea gallina and Tapes philippinarum. Food Chem 219:223–229. CrossRefPubMedGoogle Scholar
  104. Waite JH (2017) Mussel adhesion – essential footwork. J Exp Biol 220(Pt 4):517–530. CrossRefPubMedPubMedCentralGoogle Scholar
  105. Wang J, Li L, Zhang G (2016a) A high-density SNP genetic linkage map and QTL analysis of growth-related traits in a hybrid family of oysters (Crassostrea gigas × Crassostrea angulata) using genotyping-by-sequencing. G3 (Bethesda) 6(5):1417–1426. CrossRefGoogle Scholar
  106. Wang Y, Chen Z, Luo G, He W, Xu K, Xu R, Lei Q, Tan J, Wu J, Xing M (2016b) In-Situ-generated vasoactive intestinal peptide loaded microspheres in mussel-inspired polycaprolactone nanosheets creating spatiotemporal releasing microenvironment to promote wound healing and angiogenesis. ACS Appl Mater Interfaces 8(11):7411–7421. CrossRefPubMedGoogle Scholar
  107. Wang R, Song X, Xiang T, Liu Q, Su B, Zhao W, Zhao C (2017a) Mussel-inspired chitosan-polyurethane coatings for improving the antifouling and antibacterial properties of polyethersulfone membranes. CarbohydrPolym 168:310–319. CrossRefGoogle Scholar
  108. Wang S, Zhang J, Jiao W, Li J, Xun X, Sun Y, Guo X, Huan P, Dong B, Zhang L, Hu X, Sun X, Wang J, Zhao C, Wang Y, Wang D, Huang X, Wang R, Lv J, Li Y, Zhang Z, Liu B, Lu W, Hui Y, Liang J, Zhou Z, Hou R, Li X, Liu Y, Li H, Ning X, Lin Y, Zhao L, Xing Q, Dou J, Li Y, Mao J, Guo H, Dou H, Li T, Mu C, Jiang W, Fu Q, Fu X, Miao Y, Liu J, Yu Q, Li R, Liao H, Li X, Kong Y, Jiang Z, Chourrout D, Li R, Bao Z (2017b) Scallop genome provides insights into evolution of bilaterian karyotype and development. Nat Ecol Evol 1(5):120. CrossRefPubMedGoogle Scholar
  109. Wu S, Huang X (2017) Preparation and antioxidant activities of oligosaccharides from Crassostrea gigas. Food Chem 216:243–246. CrossRefPubMedGoogle Scholar
  110. Wu C, Han P, Liu X, Xu M, Tian T, Chang J, Xiao Y (2014) Mussel-inspired bioceramics with self-assembled Ca-P/polydopamine composite nanolayer: preparation, formation mechanism, improved cellular bioactivity and osteogenic differentiation of bone marrow stromal cells. Acta Biomater 10(1):428–438. CrossRefPubMedGoogle Scholar
  111. Xu M, Zhai D, Xia L, Li H, Chen S, Fang B, Chang J, Wu C (2016) Hierarchical bioceramic scaffolds with 3D-plotted macropores and mussel-inspired surface nanolayers for stimulating osteogenesis. Nanoscale 8(28):13790–13803. CrossRefPubMedGoogle Scholar
  112. Zhang G, Fang X, Guo X, Li L, Luo R, Xu F, Yang P, Zhang L, Wang X, Qi H, Xiong Z, Que H, Xie Y, Holland PW, Paps J, Zhu Y, Wu F, Chen Y, Wang J, Peng C, Meng J, Yang L, Liu J, Wen B, Zhang N, Huang Z, Zhu Q, Feng Y, Mount A, Hedgecock D, Xu Z, Liu Y, Domazet-Lošo T, Du Y, Sun X, Zhang S, Liu B, Cheng P, Jiang X, Li J, Fan D, Wang W, Fu W, Wang T, Wang B, Zhang J, Peng Z, Li Y, Li N, Wang J, Chen M, He Y, Tan F, Song X, Zheng Q, Huang R, Yang H, Du X, Chen L, Yang M, Gaffney PM, Wang S, Luo L, She Z, Ming Y, Huang W, Zhang S, Huang B, Zhang Y, Qu T, Ni P, Miao G, Wang J, Wang Q, Steinberg CE, Wang H, Li N, Qian L, Zhang G, Li Y, Yang H, Liu X, Wang J, Yin Y, Wang J (2012) The oyster genome reveals stress adaptation and complexity of shell formation. Nature 490(7418):49–54. CrossRefGoogle Scholar
  113. Zhang C, Li HN, Du Y, Ma MQ, Xu ZK (2017a) CuSO4H2O2-triggered polydopamine/poly(sulfobetaine methacrylate) coatings for antifouling membrane surfaces. Langmuir 33(5):1210–1216. CrossRefPubMedGoogle Scholar
  114. Zhang C, Lv Y, Qiu WZ, He A, Xu ZK (2017b) Polydopamine coatings with nanopores for versatile molecular separation. ACS Appl Mater Interfaces 9(16):14437–14444. CrossRefPubMedGoogle Scholar

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Authors and Affiliations

  • Paola Venier
    • 1
    Email author
  • Marco Gerdol
    • 2
  • Stefania Domeneghetti
    • 1
  • Nidhi Sharma
    • 3
  • Alberto Pallavicini
    • 2
  • Umberto Rosani
    • 1
  1. 1.Department of BiologyUniversity of PadovaPadovaItaly
  2. 2.Department of Life SciencesUniversity of TriesteTriesteItaly
  3. 3.Regional Centre for BiotechnologyNCR Biotech Science ClusterFaridabadIndia

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