Characterization of epitopes for virus-neutralizing monoclonal antibodies to Ross River virus E2 using phage-displayed random peptide libraries

Davies, J.M., Cai, Y. P., Weir, R. C., & Rowley, M. J. (2000) Characterization of epitopes for virus-neutralizing monoclonal antibodies to Ross River virus E2 using phage-displayed random peptide libraries. Virology, 275(1), pp. 67-76.

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Ross River virus (RRV) is the predominant cause of epidemic polyarthritis in Australia, yet the antigenic determinants are not well defined. We aimed to characterize epitope(s) on RRV-E2 for a panel of monoclonal antibodies (MAbs) that recognize overlapping conformational epitopes on the E2 envelope protein of RRV and that neutralize virus infection of cells in vitro. Phage-displayed random peptide libraries were probed with the MAbs T1E7, NB3C4, and T10C9 using solution-phase and solid-phase biopanning methods. The peptides VSIFPPA and KTAISPT were selected 15 and 6 times, respectively, by all three of the MAbs using solution-phase biopanning. The peptide LRLPPAP was selected 8 times by NB3C4 using solid-phase biopanning; this peptide shares a trio of amino acids with the peptide VSIFPPA. Phage that expressed the peptides VSIFPPA and LRLPPAP were reactive with T1E7 and/or NB3C4, and phage that expressed the peptides VSIFPPA, LRLPPAP, and KTAISPT partially inhibited the reactivity of T1E7 with RRV. The selected peptides resemble regions of RRV-E2 adjacent to sites mutated in neutralization escape variants of RRV derived by culture in the presence of these MAbs (E2 210-219 and 238-245) and an additional region of E2 172-182. Together these sites represent a conformational epitope of E2 that is informative of cellular contact sites on RRV.

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ID Code: 87926
Item Type: Journal Article
Refereed: Yes
Additional Information: No file attached.
Keywords: envelope protein, epitope, monoclonal antibody, neutralizing antibody, peptide library, antigen recognition, article, binding site, controlled study, mouse, nonhuman, phage display, polyarthritis, priority journal, protein expression, Ross River alpha virus, virus infection, virus neutralization, Amino Acid Sequence, Antibodies, Monoclonal, Antibodies, Viral, Antibody Specificity, Capsid, Capsid Proteins, Cloning, Molecular, Epitope Mapping, Epitopes, Molecular Sequence Data, Neutralization Tests, Peptide Fragments, Phylogeny, Ross River virus, Sequence Alignment, Sequence Analysis, Protein, Solubility, Viral Envelope Proteins, Alphavirus, RNA viruses
DOI: 10.1006/viro.2000.0474
ISSN: 0042-6822
Divisions: Current > Schools > School of Biomedical Sciences
Current > QUT Faculties and Divisions > Faculty of Health
Deposited On: 30 Sep 2015 23:29
Last Modified: 01 Oct 2015 00:50

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