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Human monoclonal antibodies to West Nile virus identify epitopes on the prM protein.

Virology.. 2011-12; 410(1):30-7

Calvert AE, Kalantarov GF, Chang GJ, Trakht I, Blair CD, Roehrig JT. a Arboviral Diseases Branch, Division of Vector-Borne Infectious Diseases, Centers for Disease Control and Prevention, Public Health Service, U.S. Department of Health and Human Services, 3150 Rampart Rd., Fort Collins, CO 80521, USAb Department of Medicine, College of Physicians and Surgeons of Columbia University, New York, NY 10032, USAc Department of Microbiology, Immunology, and Pathology, Colorado State University, For Collins, CO 80523, USA

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摘要

Hybridoma cell lines (2E8, 8G8 and 5G12) producing fully human monoclonal antibodies (hMAbs) specific for the pre-membrane (prM) protein of West Nile virus (WNV) were prepared using a human fusion partner cell line, MFP-2, and human peripheral blood lymphocytes from a blood donor diagnosed with WNV fever in 2004. Using site-directed mutagenesis of a WNV-like particle (VLP) we identified 4 amino acid residues in the prM protein unique to WNV and important in the binding of these hMAbs to the VLP. Residues V19 and L33 are important epitopes for the binding of all three hMAbs. Mutations at residue, T20 and T24 affected the binding of hMAbs, 8G8 and 5G12 only. These hMAbs did not significantly protect AG129 interfe... More