Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 549565
Title Monoclonal antibodies to the E2 protein of a new genotype (type 2) of bovine viral diarrhea virus define three antigenic domains involved in neutralization
Author(s) Deregt, Dirk; Rijn, Piet A. van; Wiens, Tania Y.; ven Hurk, Jan van
Source Virus Research 57 (1998)2. - ISSN 0168-1702 - p. 171 - 182.
DOI https://doi.org/10.1016/S0168-1702(98)00095-1
Department(s) Virology
Publication type Refereed Article in a scientific journal
Publication year 1998
Keyword(s) Epitopes - Monoclonal antibodies - Neutralization - Type 2 bovine viral diarrhea virus
Abstract

Bovine viral diarrhea virus (BVDV) has recently been segregated into two genotypes, namely, BVDV 1 and BVDV 2. Viruses of the BVDV 2 genotype are a cause of hemorrhagic and acute fatal disease in cattle in the US and Canada. In this study, monoclonal antibodies (mAbs) to the newly described BVDV 2 were produced after immunization with virus or a combination of virus and E2 peptide. From an original panel of 17 mAbs, 13 mAbs were identified as E2-specific by reactivity with a BVDV 2 recombinant E2 protein expressed in insect cells. Nine E2 mAbs were observed to be virus-neutralizing. The E2 epitopes represented by the mAbs were found to be highly conserved among BVDV 2 isolates associated with hemorrhagic or severe disease in cattle. Except for one virus-neutralizing E2 mAb, the mAbs showed few or relatively weak cross-reactions with BVDV 1. Two non-neutralizing E2 mAbs were BVDV 2-specific. In contrast to BVDV 1 for which conserved neutralizing epitopes have been mapped in one immunodominant domain, the virus-neutralizing E2 mAbs produced to BVDV 2 were found to bind to highly conserved epitopes in three antigenic domains. Copyright (C) 1998 Elsevier Science B.V.

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