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PMID: 2434608 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Epitope mapping of the major Epstein-Barr virus outer envelope glycoprotein gp350/220.

The Journal of general virology ·Vol. 68 ( Pt 2) ·1987-02-00 ·Pages 535-43

Qualtiere LF, Decoteau JF, Hassan Nasr-el-Din M

Abstract

To understand the complete immunochemical structure of the Epstein-Barr virus (EBV) major membrane glycoprotein gp350/220, monoclonal antibodies (MAbs) reacting with this important viral antigen were isolated. Through competitive inhibition binding studies, it was determined that a group of 18 IgG MAbs recognized seven distinct epitopes on the gp350/220 molecule. Eight of these MAbs fell into a single epitope group with four of those MAbs, as well as a single MAb from another epitope group, being capable of neutralizing EBV strain B95-8 transformation of umbilical cord lymphocytes.

MeSH Terms
Antibodies, Monoclonal/immunology Antibodies, Viral/immunology Antigens, Viral/immunology Binding, Competitive Cell Transformation, Viral Epitopes/immunology Herpesvirus 4, Human/immunology Humans Infant, Newborn Lymphocytes/microbiology Neutralization Tests Umbilical Cord/cytology Viral Matrix Proteins
Chemicals
Antibodies, Monoclonal Antibodies, Viral Antigens, Viral EBV-associated membrane antigen, Epstein-Barr virus Epitopes Viral Matrix Proteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Qualtiere L F
Decoteau J F
Hassan Nasr-el-Din M
Article Info
Journal
The Journal of general virology
Abbr.
J Gen Virol
ISSN
0022-1317
Published
1987-02-00
Pages
535-43
Language
English
Region
England
NLM ID
0077340
Subset
IM
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