Phage Display on the Base of Filamentous Bacteriophages: Application for Recombinant Antibodies Selection

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Abstract

The display of peptides and proteins on the surface of filamentous bacteriophage is a powerful methodology for selection of peptides and protein domains, including antibodies. An advantage of this methodology is the direct physical link between the phenotype and the genotype, as an analyzed polypeptide and its encoding DNA fragment exist in one phage particle. Development of phage display antibody libraries provides repertoires of phage particles exposing antibody fragments of great diversity. The biopanning procedure facilitates selection of antibodies with high affinity and specificity for almost any target. This review is an introduction to phage display methodology. It presents recombinant antibodies display in more details:, construction of phage libraries of antibody fragments and different strategies for the biopanning procedure.

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Most cited references 81

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Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface.

G. Smith (1985)

Foreign DNA fragments can be inserted into filamentous phage gene III to create a fusion protein with the foreign sequence in the middle. The fusion protein is incorporated into the virion, which retains infectivity and displays the foreign amino acids in immunologically accessible form. These "fusion phage" can be enriched more than 1000-fold over ordinary phage by affinity for antibody directed against the foreign sequence. Fusion phage may provide a simple way of cloning a gene when an antibody against the product of that gene is available.

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Diversity in the CDR3 region of V(H) is sufficient for most antibody specificities.

J. Xu, M Davis (2000)

All rearranging antigen receptor genes have one or two highly diverse complementarity determining regions (CDRs) among the six that typically form the ligand binding surface. We report here that, in the case of antibodies, diversity at one of these regions, CDR3 of the V(H) domain, is sufficient to permit otherwise identical IgM molecules to distinguish between a variety of hapten and protein antigens. Furthermore, we find that somatic mutation can allow such antibodies to achieve surprisingly high affinities. These results are consistent with a model in which the highly diverse CDR3 loops are the key determinant of specificity in antigen recognition in both T cell receptors (TCR) and antibodies, whereas the germline-encoded CDR1 and CDR2 sequences are much more cross-reactive.

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Organ targeting in vivo using phage display peptide libraries.

R Pasqualini, E Ruoslahti (1996)

Preferential homing of tumour cells and leukocytes to specific organs indicates that tissues carry unique marker molecules accessible to circulating cells. Organ-selective address molecules on endothelial surfaces have been identified for lymphocyte homing to various lymphoid organs and to tissues undergoing inflammation, and an endothelial marker responsible for tumour homing to the lungs has also been identified. Here we report a new approach to studying organ-selective targeting based on in vivo screening of random peptide sequences. Peptides capable of mediating selective localization of phage to brain and kidney blood vessels were identified, and showed up to 13-fold selectivity for these organs. One of the peptides displayed by the brain-localizing phage was synthesized and shown to specifically inhibit the localization of the homologous phage into the brain. When coated onto glutaraldehyde-fixed red blood cells, the peptide caused selective localization of intravenously injected cells into the brain. These peptide sequences represent the first step towards identifying selective endothelial markers, which may be useful in targeting cells, drugs and genes into selected tissues.

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Journal

Journal ID (nlm-ta): Acta Naturae

Journal ID (iso-abbrev): Acta Naturae

Journal ID (publisher-id): Acta Naturae

Title: Acta Naturae

Publisher: A.I. Gordeyev

ISSN (Print): 2075-8251

Publication date (Print): October 2009

Volume: 1

Issue: 3

Pages: 20-28

Affiliations

[1 ]Institute of Chemical Biology and Fundamental Medicine, Siberian Branch, Russian Academy of Science

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tikunova@ 123456niboch.nsc.ru

Article

DOI: 10.32607/20758251-2009-1-3-20-28

PMC ID: 3347532

PubMed ID: 22649612

SO-VID: c6b7cd70-2376-4934-9b55-85f84a29ce7c

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This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Phage Display on the Base of Filamentous Bacteriophages: Application for Recombinant Antibodies Selection

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Abstract

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Network and Systems Medicine

Most cited references 81

Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface.

Diversity in the CDR3 region of V(H) is sufficient for most antibody specificities.

Organ targeting in vivo using phage display peptide libraries.

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