Abstract
Host defense peptides (HDPs) constitute a large group of natural broad-spectrum antimicrobials and an important first line of immunity in virtually all forms of life. Specific augmentation of synthesis of endogenous HDPs may represent a promising antibiotic-alternative approach to disease control. Previously, we purified and identificated a Novel Antimicrobial Host Defense Peptide from a histone of Rabbit sacculus rotundus, and termed this Peptide RSRAH, which could promoted cellular immune function in immunosuppressed mice and protected mice from E. coli challenge (Chen in Int J Pept Res Ther 2015, 2018). In the present study, we further revealed that RSRAH expression in the sacculus rotundus is significantly higher in adult rabbits than in aging rabbits. And RSRAH is highly expressed in immune-related tissues. Furthermore, feed supplementation with 0.1% and 0.2% Atractylodes macrocephala polysaccharide, recognized as an ideal immunopotentiator, led to a significant increase in RSRAH gene expression in the Rabbit sacculus rotundus. Collectively, it was hypothesized that RSRAH may play an important role in the immune system of rabbits.
Similar content being viewed by others
References
Brogden KA, Ackermann M, McCray PB, Tack BF (2003) Antimicrobial peptides in animals and their role in host defences. Int J Antimicrob Agents 22:465–478. https://doi.org/10.1016/S0924-8579(03)00180-8
Chen H, Li Y, Wu J, Liu J, Huang Q, Wei S, Zhao G, Zhang Z, Hua L (2015) Purification and identification of a novel antimicrobial protein from the rabbit sacculus rotundus and its effect on cellular immune function in mice. Int J Pept Res Ther 21:443–450. https://doi.org/10.1007/s10989-015-9472-x
Chen H, Wu J, Wang Y, Yu X, Feng T, Dai D, Xiang M, Chen L (2018) Rabbit’s host defense peptide (RSRAH) protects mice from Escherichia coli challenge. Int J Pept Res Ther. https://doi.org/10.1007/s10989-018-9694-9
Fjell CD, Hiss JA, Hancock RE, Schneider G (2011) Designing antimicrobial peptides: form follows function. Nat Rev Drug Discov 11:37–51. https://doi.org/10.1038/nrd3591
Hancock RE, Sahl H-G (2006) Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat Biotechnol 24:1551–1557. https://doi.org/10.1038/nbt1267
Hancock RE, Haney EF, Gill EE (2016) The immunology of host defence peptides: beyond antimicrobial activity. Nat Rev Immunol 16:321–334. https://doi.org/10.1038/nri.2016.29
Haney EF, Mansour SC, Hancock RE (2017) Antimicrobial peptides: an introduction. Antimicrob Pept Methods Protoc. https://doi.org/10.1007/978-1-4939-6737-7_1
Hirata M, Shimomura Y, Yoshida M, Morgan JG, Palings I, Wilson D, Yen MH, Wright SC, Larrick JW (1994) Characterization of a rabbit cationic protein (CAP18) with lipopolysaccharide-inhibitory activity. Infect Immun 62:1421–1426
Kawasaki H, Isaacson T, Iwamuro S, Conlon JM (2003) A protein with antimicrobial activity in the skin of Schlegel’s green tree frog Rhacophorus schlegelii (Rhacophoridae) identified as histone H2B. Biochem Biophys Res Commun 312:1082–1086. https://doi.org/10.1016/j.bbrc.2003.11.052
Kawasaki H, Koyama T, Conlon JM, Yamakura F, Iwamuro S (2008) Antimicrobial action of histone H2B in Escherichia coli: evidence for membrane translocation and DNA-binding of a histone H2B fragment after proteolytic cleavage by outer membrane proteinase T. Biochimie 90:1693–1702. https://doi.org/10.1016/j.biochi.2008.07.003
Lehrer RI, Daher K, Ganz T, Selsted M (1985) Direct inactivation of viruses by MCP-1 and MCP-2, natural peptide antibiotics from rabbit leukocytes. J Virol 54:467–472
Li X, Lin J, Han W, Mai W, Wang L, Li Q, Lin M, Bai M, Zhang L, Chen D (2012) Antioxidant ability and mechanism of rhizoma Atractylodes macrocephala. Molecules 17:13457–13472. https://doi.org/10.3390/molecules171113457
Liu T, She R, Wang K, Bao H, Zhang Y, Luo D, Hu Y, Ding Y, Wang D, Peng K (2008) Effects of rabbit sacculus rotundus antimicrobial peptides on the intestinal mucosal immunity in chickens. Poult Sci 87:250–254. https://doi.org/10.3382/ps.2007-00353
Liu J, Chen X, Yue C, Hou R, Chen J, Lu Y, Li X, Li R, Liu C, Gao Z (2015) Effect of selenylation modification on immune-enhancing activity of Atractylodes macrocephala polysaccharide. Int J Biol Macromol 72:1435–1440. https://doi.org/10.1016/j.ijbiomac.2014.10.022
Lüders T, Birkemo GA, Nissen-Meyer J, Andersen Ø, Nes IF (2005) Proline conformation-dependent antimicrobial activity of a proline-rich histone H1N-terminal peptide fragment isolated from the skin mucus of Atlantic salmon. Antimicrob Agents Chemother 49:2399–2406. https://doi.org/10.1128/AAC.49.6.2399-2406.2005
Ooi CE, Weiss J, Levy O, Elsbach P (1990) Isolation of two isoforms of a novel 15-kDa protein from rabbit polymorphonuclear leukocytes that modulate the antibacterial actions of other leukocyte proteins. J Biol Chem 265:15956–15962
Park CB, Kim MS, Kim SC (1996) A novel antimicrobial peptide from Bufo bufo gargarizans. Biochem Biophys Res Commun 218:408–413
Pfaffl MW (2001) A new mathematical model for relative quantification in real-time RT–PCR. Nucleic Acids Res 29:e45–e45. https://doi.org/10.1093/nar/29.9.e45
Pletzer D, Coleman SR, Hancock RE (2016) Anti-biofilm peptides as a new weapon in antimicrobial warfare. Curr Opin Microbiol 33:35–40. https://doi.org/10.1016/j.mib.2016.05.016
Sinha S, Cheshenko N, Lehrer RI, Herold BC (2003) NP-1, a rabbit α-defensin, prevents the entry and intercellular spread of herpes simplex virus type 2. Antimicrob Agents Chemother 47:494–500. https://doi.org/10.1128/AAC.47.2.494-500.2003
Steiner H, Hultmark D, Engström Å, Bennich H, Boman HG (1981) Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 292:246–248
Strominger JL (2009) Animal antimicrobial peptides: ancient players in innate immunity. J Immunol 182:6633–6634. https://doi.org/10.4049/jimmunol.0990038
Sunkara LT, Jiang W, Zhang G (2012) Modulation of antimicrobial host defense peptide gene expression by free fatty acids. PLoS ONE 7:e49558. https://doi.org/10.1371/journal.pone.0049558
Trimble MJ, Hancock RE (2017) An alternative approach to treating antibiotic-resistant infections. Future Microbiol 12:201–204. https://doi.org/10.2217/fmb-2016-0222
Tu Y, Wang Y, Xu C, Yao G, Shan T (2006) Effect of astragalus and astragalus polysaccharide on antimicrobial peptides PR-39 and protegrin-1 gene expression in pigs. Turk J Vet Anim Sci 30:325–330
Xie F, Sakwiwatkul K, Zhang C, Wang Y, Zhai L, Hu S (2013) Atractylodis macrocephalae Koidz. Polysaccharides enhance both serum IgG response and gut mucosal immunity. Carbohydr Polym 91:68–73. https://doi.org/10.1016/j.carbpol.2012.07.083
Xu D, Li W, Huang Y, He J, Tian Y (2014) The effect of selenium and polysaccharide of Atractylodes macrocephala Koidz. (PAMK) on immune response in chicken spleen under heat stress. Biol Trace Elem Res 160:232–237. https://doi.org/10.1007/s12011-014-0056-y
Yang D, Biragyn A, Hoover DM, Lubkowski J, Oppenheim JJ (2004) Multiple roles of antimicrobial defensins, cathelicidins, and eosinophil-derived neurotoxin in host defense. Annu Rev Immunol 22:181–215. https://doi.org/10.1146/annurev.immunol.22.012703.104603
Zasloff M (2002) Antimicrobial peptides of multicellular organisms. Nature 415:389–395. https://doi.org/10.1038/415389a
Zhao YR, Chen QH, He JH, Fan ZY, Zhou C, Liu ZY (2008) The effect of Achyranthes bidentata polysaccharides on Protegrin-1mRNA expression in weaned piglets. Chin J Anim Nutr 20:80–84 (In Chinese.)
Acknowledgements
This work was supported by grants from the “Fundamental Research Funds for the Central Universities” (XDJK2019B040), and the “Chongqing basic research and frontier exploration project”(cstc2018jcyjAX0466, cstc2017jcyjAX0040).
Author information
Authors and Affiliations
Corresponding author
Ethics declarations
Conflict of interest
All the authors declare they have no conflicts of interest.
Ethical Approval
The authors declare that the experiments on animals were conducted in accordance with local Ethical Committee laws and regulations as regards care and use of laboratory animals.
Additional information
Publisher's Note
Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
Electronic supplementary material
Below is the link to the electronic supplementary material.
Rights and permissions
About this article
Cite this article
Fu, G., Zhang, Y., Li, Y. et al. The Effect of Atractylodes macrocephala Polysaccharides on Rabbit’s Host Defense Peptide (RSRAH) mRNA Expression. Int J Pept Res Ther 26, 1871–1877 (2020). https://doi.org/10.1007/s10989-019-09988-z
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s10989-019-09988-z