Construction of Antibody Phage Libraries and Their Application in Veterinary Immunovirology

Overview

Journal Antibodies (Basel)

Date 2020 Jun 7

PMID 32503103

Citations 9

Authors

Shahbaz Bashir

Jan Paeshuyse

Affiliations

Soon will be listed here.

Abstract

Antibody phage display (APD) technology has revolutionized the field of immunovirology with its application in viral disease diagnostics and antiviral therapy. This robust and versatile technology allows the expression of an antibody fused to a phage coat protein on the surface of a filamentous phage. The DNA sequence coding for the antibody is packaged within the phage, linking the phenotype to genotype. Antibody phage display inherits the ability to rapidly generate and modify or improve high-affinity monoclonal antibodies, rendering it indispensable in immunology. In the last two decades, phage-display-derived antibodies have been extensively used in human medicine as diagnostic and therapeutic modalities. Recently, they are also gaining significant ground in veterinary medicine. Even though these advancements are mainly biased towards economically important animals such as chicken, cattle, and pigs, they are laying the foundation of fulfilling the unmet needs of veterinary medicine as antibody-based biologics in viral diagnostics, therapeutics, and immunoprophylaxis. This review provides a brief overview of the construction of antibody phage libraries and their application in diagnosis, prevention, and control of infectious viral diseases in veterinary medicine in detail.

Citing Articles

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Single-Stranded Variable Fragment Gene Libraries Built for Phage Display: An Updated Review of Design, Selection and Application.

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References

Shimazaki K, Lepin E, Wei B, Nagy A, Coulam C, Mareninov S . Diabodies targeting epithelial membrane protein 2 reduce tumorigenicity of human endometrial cancer cell lines. Clin Cancer Res. 2008; 14(22):7367-77. PMC: 3109074. DOI: 10.1158/1078-0432.CCR-08-1016. View

Hoogenboom H, Lutgerink J, Pelsers M, Rousch M, Coote J, van Neer N . Selection-dominant and nonaccessible epitopes on cell-surface receptors revealed by cell-panning with a large phage antibody library. Eur J Biochem. 1999; 260(3):774-84. DOI: 10.1046/j.1432-1327.1999.00214.x. View

Blazek D, Celer V, Navratilova I, Skladal P . Generation and characterization of single-chain antibody fragments specific against transmembrane envelope glycoprotein gp46 of maedi-visna virus. J Virol Methods. 2003; 115(1):83-92. DOI: 10.1016/j.jviromet.2003.09.020. View

Meli G, Visintin M, Cannistraci I, Cattaneo A . Direct in vivo intracellular selection of conformation-sensitive antibody domains targeting Alzheimer's amyloid-beta oligomers. J Mol Biol. 2009; 387(3):584-606. DOI: 10.1016/j.jmb.2009.01.061. View

Li T, Huang M, Xiao H, Zhang G, Ding J, Wu P . Selection and characterization of specific nanobody against bovine virus diarrhea virus (BVDV) E2 protein. PLoS One. 2017; 12(6):e0178469. PMC: 5459339. DOI: 10.1371/journal.pone.0178469. View

Boruah B, Liu D, Ye D, Gu T, Jiang C, Qu M . Single domain antibody multimers confer protection against rabies infection. PLoS One. 2013; 8(8):e71383. PMC: 3748109. DOI: 10.1371/journal.pone.0071383. View

Carlsson F, Trilling M, Perez F, Ohlin M . A dimerized single-chain variable fragment system for the assessment of neutralizing activity of phage display-selected antibody fragments specific for cytomegalovirus. J Immunol Methods. 2011; 376(1-2):69-78. DOI: 10.1016/j.jim.2011.11.010. View

Sapats S, Gould G, Trinidad L, Parede L, David C, Ignjatovic J . An ELISA for detection of infectious bursal disease virus and differentiation of very virulent strains based on single chain recombinant chicken antibodies. Avian Pathol. 2006; 34(6):449-55. DOI: 10.1080/03079450500367765. View

Liu H, Liang C, Duan H, Zhang X, Wang X, Xiao S . Intracellularly expressed nanobodies against non-structural protein 4 of porcine reproductive and respiratory syndrome virus inhibit virus replication. Biotechnol Lett. 2016; 38(7):1081-8. DOI: 10.1007/s10529-016-2086-3. View

10.

Hoogenboom H, de Bruine A, Hufton S, Hoet R, Arends J, Roovers R . Antibody phage display technology and its applications. Immunotechnology. 1998; 4(1):1-20. DOI: 10.1016/s1380-2933(98)00007-4. View

11.

Dominik P, Borowska M, Dalmas O, Kim S, Perozo E, Keenan R . Conformational Chaperones for Structural Studies of Membrane Proteins Using Antibody Phage Display with Nanodiscs. Structure. 2016; 24(2):300-9. PMC: 4740257. DOI: 10.1016/j.str.2015.11.014. View

12.

Molinkova D, Skladal P, Celer V . In vitro neutralization of equid herpesvirus 1 mediated by recombinant antibodies. J Immunol Methods. 2008; 333(1-2):186-91. DOI: 10.1016/j.jim.2008.01.019. View

13.

. Surface display and peptide libraries. Cold Spring Harbor Laboratory, April 4-7, 1992. Proceedings. Gene. 1993; 128(1):1-144. View

14.

Bao F, Wang L, Zhao X, Lu T, Na A, Wang X . Preparation and characterization of a single-domain antibody specific for the porcine epidemic diarrhea virus spike protein. AMB Express. 2019; 9(1):104. PMC: 6626092. DOI: 10.1186/s13568-019-0834-1. View

15.

McWhirter J, Kretz-Rommel A, Saven A, Maruyama T, Potter K, Mockridge C . Antibodies selected from combinatorial libraries block a tumor antigen that plays a key role in immunomodulation. Proc Natl Acad Sci U S A. 2006; 103(4):1041-6. PMC: 1327729. DOI: 10.1073/pnas.0510081103. View

16.

Duggan J, COATES D, Ulaeto D . Isolation of single-chain antibody fragments against Venezuelan equine encephalomyelitis virus from two different immune sources. Viral Immunol. 2001; 14(3):263-73. DOI: 10.1089/088282401753266774. View

17.

Tanaka T, Rabbitts T . Protocol for the selection of single-domain antibody fragments by third generation intracellular antibody capture. Nat Protoc. 2010; 5(1):67-92. DOI: 10.1038/nprot.2009.199. View

18.

Tutykhina I, Sedova E, Gribova I, Ivanova T, Vasilev L, Rutovskaya M . Passive immunization with a recombinant adenovirus expressing an HA (H5)-specific single-domain antibody protects mice from lethal influenza infection. Antiviral Res. 2013; 97(3):318-28. DOI: 10.1016/j.antiviral.2012.12.021. View

19.

Foord A, Muller J, Yu M, Wang L, Heine H . Production and application of recombinant antibodies to foot-and-mouth disease virus non-structural protein 3ABC. J Immunol Methods. 2007; 321(1-2):142-51. DOI: 10.1016/j.jim.2007.01.014. View

20.

Fantini M, Pandolfini L, Lisi S, Chirichella M, Arisi I, Terrigno M . Assessment of antibody library diversity through next generation sequencing and technical error compensation. PLoS One. 2017; 12(5):e0177574. PMC: 5432181. DOI: 10.1371/journal.pone.0177574. View