Abstract
Filamentous bacteriophages (Ff) are a group of related viruses which infect only gram-negative bacteria They are flexible filaments of about 900 nm long and 6−10 nm thick, similar to amyloid fibrils The similarity in characteristics and conformation between amyloids that are composed of different proteins without any sequence homology raised the hypothesis that filamentous phages may affect protein amyloids regardless of the protein from which they are composed. Indeed the filamentous phages may bind to a certain conformation or region which is common for several types of amyloids and effect their aggregation similar to conformational antibodies.
Moreover the filamentous bacteriophage proved to be an efficient and non-toxic viral delivery vector of antibodies to the brain, following the olfactory tract and an efficient immunocarrier for raising antibodies. The therapeutic potential of phages in amyloidogenic diseases, stems from their unprecedented ability to access the CNS, to induce a potent anti-aggregating effect, and from their lack of tropism to mammalian cells.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Banks WA, Terrell B, Farr SA, Robinson S, Nonaka N, Morley E (2002) Passage of amyloid beta protein antibody across the blood-brain barrier in a mouse model of Alzheimer’s disease. Peptides 23:2223–2226
Bard F, Barbour R, Cannon C, Carretto R, Games D, Guido T, Hoenow K, Hu K, Johnson-Wood K, Khan K, Kholodenko LC, Lee M, Motter R, Nguyen M, Reed A, Schenk D, Tang P, Vasquez N, Seubert P, Yednock T (2000) Epitope and isotype specificities of antibodies to β-amyloid peptide for protection against Alzheimer’s disease-like neuropathology. Proc Natl Acad Sci U S A 100:2023–2028
Dabrowska K, Switala-Jelen K, Opolski A, Weber-Dabrowska B, Gorski A (2005) Bacteriophage penetration in vertebrates. J Appl Microbiol 98:7–13
Delmastro P, Meola A, Monaci P, Cortese R, Galfre G (1997) Immunogenicity of filamentous phage displaying peptide mimotopes after oral administration. Vaccine 15:1276–1285
Dickerson TJ, Janda KD (2005) Recent advances for the treatment of cocaine abuse: central nervous system Immunopharmacotherapy. AAPS J 7:E579–E586
Dimant H, Solomon B (2010) Filamentous phages reduce α-Synuclein Oligomerization in the membrane fraction of SH-SY5Y cells. Neurodegener Dis 7:203–205
Dimant H, Sharon N, Solomon B (2009) Modulation effect of filamentous phage on a-synuclein aggregation Biochem. Biophys Res Comm 383:491–496
Dobson CM (1999) Protein misfolding, evolution and disease. Trends Biochem Sci 24:329–332
El-Agnaf SA, Salem KE, Paleologou MD, Curran MJ, Gibson JA, Court MG, Schlossmacher MG, Allsop D (2006) Detection of oligomeric forms of {alpha}-synuclein protein in human plasma as a potential biomarker for Parkinson’s disease. FASEB J 20:419–425
Frenkel D, Solomon B (2002) Filamentous phage as vector-mediated antibody delivery to the brain. Proc Natl Acad Sci U S A 99:5675–5679
Frenkel D, Balass M, Solomon B (1998) N-Terminal EFRH sequence of Alzheimer’s β-amyloid peptide represents the epitope of its anti-aggregating antibodies. J Neuroimmunol 88:85–90
Frenkel D, Dewachter I, Van Leuven F, Solomon B (2003) Reduction of beta-amyloid plaques in brain of transgenic mouse model of Alzheimer’s disease by EFRH-phage immunization. Vaccine 7:1060–1065
Frey WI (2002) Bypassing the blood-brain barrier to deliver therapeutic agents to the brain and spinal cord. Drug Delivery Technol 2:46–49
Games D, Adams D, Alessandrini R, Barbour R, Berthelette P, Blackwell C, Carr T, Clemens J, Donaldson T et al (1995) Alzheimer-type neuropathology in transgenic mice overexpressing V717F beta-amyloid precursor protein. Nature 373:523–527
Goedert M (2001) Alpha-synuclein and neurodegenerative diseases. Nat Rev Neurosci 2:492–501
Goren O (2008) PhD thesis Submitted to Tel Aviv University
Griffith J, Manning M, Dunn K (1981) Filamentous bacteriophage contract into hollow spherical particles upon exposure to a chloroform-water interface. Cell 23:747–753
Hart AM, Knight RP, Harbottle A, Mistry HD, Hunger DF, Cutler R, Williamson R, Coutelle C (1994) Cell binding and internalization by filamentous phage displaying a cyclic Arg-Gly-Asp-containing peptide. J Biol Chem 269:12468–12474
Hartman RE, Izumi Y, Bales KR, Paul SM, Wozniak DF, Holtzman DM (2005) Treatment with an amyloid-beta antibody ameliorates plaque load, learning deficits, and hippocampal long-term potentiation in a mouse model of Alzheimer’s disease. J Neurosci 25:6213–6220
Illum L (2000) Transport of drugs from the nasal cavity to the central nervous system. Eur J Pharm Sci 11:1–18
Illum L (2002) Nasal drug delivery: new developments and strategies. Drug Discov Today 7:1184–1189
Jin K, Xie L, Childs J, Sun Y, Mao XO, Logvinova A, Greenberg DA (2003) Cerebral neurogenesis is induced by intranasal administration of growth factors. Ann Neurol 53:405–409
Kayed R, Canto I, Breydo L, Rasool S, Lukacsovich T, Wu J, Albay R 3rd, Pensalfini A, Yeung S, Head E, March JL, Glabe CG (2010) Conformation dependent monoclonal antibodies distinguish different replicating strains or conformers of prefibrillar Abeta oligomers. Mol Neurodegener 5:57. https://doi.org/10.1186/1750-1326-5-57
Krag DN, Fuller SP, Oligino L, Pero SC, Weaver D, Soden AL, Hebert C, Mills LC, Peterson D (2002) Phage-displayed random peptide libraries in mice: toxicity after serial panning. Cancer Chemother Pharmacol 50:325–332
Krishnan R, Tsubery H, Proschitsky MY, Asp E, Lulu M, Gilead S, Gartner M, Waltho JP, Davis PJ, Hounslow AM, Kirschner DA, Inouye H, Myszka DG, Wright J, Solomon B, Fisher RA (2014) A bacteriophage capsid protein provides a general amyloid interaction motif (GAIM) that binds and remodels misfolded protein assemblies. J Mol Biol 426:2500–2519
Manoutcharian K, Gevorkian G, Cano A, Almagro JC (2001) Phage displated biomolecules as preventive and therapeutics agents. Curr Pharm Biotechnol 2:217–223
Marvin DA (1998) Filamentous phage structure, infection and assembly. Curr Opin Struct Biol 8:150–158
Marvin D, Hohn B (1969) Filamentous bacterial viruses. Bacteriol Rev 33:172–209
Marvin D, Pigram W, Wiseman R, Wachtel E, Marvin F (1974) Filamentous bacterial viruses. XII. Molecular architecture of the class I (fd, Ifi, Ike) virion. J Mol Biol 88:581–598
McCafferty J, Griffiths AD, Winter G, Chiswell D (1990) Phage antibodies: filamentous phage displaying antibody variable domains. Nature 348:552–554
Meola A, Delmastro P, Monaci P, Luzzago A, Nicosia A, Felici F, Cortese R, Galfre G (1995) Derivation of vaccines from mimotopes. Immunological properties of human hepatitis virus surface antigen mimotopes displayed on filamentous phage. J Immunol 154:3162–3172
Molenaar TJ, Michon T, de Haas SA, van Berkel TJ, Kuiper J, Biessen EA (2002) Uptake and processing of modified bacteriophage M13 in mice: implications for phage display. Virology 293:182–191
Newman J, Swinney H, Day L (1977) Hydrodynamic properties and structure of fd virus. J Mol Biol 116:593–606
Opella SJ, Cross T, Di Verdi J, Sturm C (1980) Nuclear magnetic resonance of the filamentous bacteriophage fd. Biophys J 32:531–548
Pasqualini R, Ruoslahti E (1996) Organ targeting in vivo using phage display peptide libraries. Nature 380:364–366
Peters JM, Hummel T, Kratzsch T, Lotsch J, Skarke C, Frolich L (2003) Olfactory function in mild cognitive impairment and Alzheimer’s disease: an investigation using psychophysical and electrophysiological techniques. Am J Psychiatry 160:1995–2002
Rodi DJ, Makowski L (1998) Phage-display technology finding a needle I in a vast molecular haystack. Curr Opin Biotechnol 10:87–93
Rossomando E, Zinder N (1968) Studies on the bacteriophage flI. Alkali-induced disassembly of the phage into DNA and protein. J Mol Biol 36:387–399
Schenk D, Barbour R, Dunn W, Gordon G, Grajeda H, Guido T, Hu K, Huang J, Johnson-Wood K, Khon K, Kholodenko D, Lee M, Liao Z, Lieberburg I, Motter R, Mutter L, Soriano F, Shopp G, Vasquez N, Vandevert C, Walker S, Wogulis M, Yednock T, Games D, Seubert P (1999) Immunization with amyloid-beta attenuates Alzheimer-disease-like pathology in the PDAPP mouse. Nature 400:173–177
Scott JK, Smith GP (1990) Searching for peptide ligands with an epitope library. Science 249:386–390
Selkoe DJ (1991) The molecular pathology of Alzheimer’s disease. Neuron 6:487–498
Sigurdsson P, Thorvaldsson T, Gizurarson S, Gunnarsson E (1997) Olfactory absorption of insulin to the brain. Drug Deliv 4:195–200
Smith GP (1985) Filamentous fusion phage; novel expression vectors that display cloned antigens on the virion surface. Science 228:1315–1317
Smith HW, Huggins RB (1982) Successful treatment of experimental E coli infections in mice using phage: its general superiority over antibiotics. J Gen Microbiol 128:307–318
Solomon B, Koppel R, Hanan E, Katzav T (1996) Monoclonal antibodies inhibit in vitro fibrillar aggregation of the Alzheimer beta-amyloid peptide. Proc Natl Acad Sci U S A 93:452–455
Solomon B, Koppel R, Frankel D, Hanan-Aharon E (1997) Disaggregation of Alzheimer beta-amyloid by site-directed mAb. Proc Natl Acad Sci U S A 94:4109–4112
Soto C, Estrada L, Castilla J (2006) Amyloids, prions and the inherent infectious nature of misfolded protein aggregates. Trends Biochem Sci 31:150–155
Stone R (2002) Stalin’s forgotten cure. Science 298:728–731
Thorne RG, Frey WH (2001) Delivery of neurotrophic factors to the central nervous system: pharmacokinetic considerations. Clin Pharmacokinet 40:907–946
Vasilevko V, Cribbs DH (2006) Novel approaches for immunotherapeutic intervention in Alzheimer’s disease. Neurochem Int 49:113–126
Weksler ME, Gouras G, Relkin NR, Szabo P (2005) The immune system, amyloid-β peptide, and Alzheimer’s disease. Immunol Rev 205:244–256
Willis EA, Perham NR, Wraaith D (1993) Immunological properties of foreign peptides in multiple display on a filamentous bacteriophage. Gene 128:79–83
Zou J, Dickerson MT, Owen NK, Landon LA, Deutscher SL (2004) Distribution of filamentous phage peptide libraries in mice Mol. Biol Reprod 31:121–129
Zuercher AW, Miescher SM, Vogel M, Rudolf MR, Stadler MB, Stadler BM (2000) Oral anti-IgE immunization with epitope-displaying phage. Eur J Immunol 30:128–135
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2020 Springer Nature Switzerland AG
About this chapter
Cite this chapter
Solomon, B. (2020). Bacteriophage Therapies Targets Multiple Diseases Caused by Protein Misfolding. In: Witzany, G. (eds) Biocommunication of Phages. Springer, Cham. https://doi.org/10.1007/978-3-030-45885-0_19
Download citation
DOI: https://doi.org/10.1007/978-3-030-45885-0_19
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-030-45884-3
Online ISBN: 978-3-030-45885-0
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)