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PMID: 6287039 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Identification and isolation of the main component (gp350-gp220) of Epstein-Barr virus responsible for generating neutralizing antibodies in vivo.

Journal of virology ·Vol. 43 ·No. 2 ·1982-08-00 ·Pages 730-6

Thorley-Lawson DA, Poodry CA

Abstract

The majority of hybridomas we have characterized against Epstein-Barr virions react with the major glycoproteins gp350 and gp220 (gp350/220). One of these antibodies, ID4C-1, neutralizes virus infection in vitro. The presence of gp350/220 on the viral envelope could be confirmed directly by immunoelectron microscopy. We used lectin affinity (ricin) and immunoaffinity (ID4C-1) to purify gp350/220 and show that this material is able to induce potent virus-neutralizing antibodies. Absorption of four human and one rabbit anti-Epstein-Barr virus sera with purified gp350/220 suggests that this is the primary component responsible for generating neutralizing antibodies in vivo.

MeSH Terms
Animals Antibodies, Viral/biosynthesis Burkitt Lymphoma/immunology Glycoproteins/immunology,isolation & purification Herpesvirus 4, Human/immunology Humans Immunoenzyme Techniques Microscopy, Electron Neutralization Tests Rabbits Viral Envelope Proteins Viral Proteins/immunology,isolation & purification
Chemicals
Antibodies, Viral Glycoproteins Viral Envelope Proteins Viral Proteins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Thorley-Lawson D A
Poodry C A
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23 references, click to expand
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
DOI
10.1128/JVI.43.2.730-736.1982
Published
1982-08-00
Pages
730-6
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC256176
Subset
IM
Grants
NIAID NIH HHS · AI 15310 · United States
NCI NIH HHS · CA 28737 · United States
External Links
PubMed source DOI: 10.1128/JVI.43.2.730-736.1982 PMC Full Text View journal details
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