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PMID: 6310587 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

One of two Epstein-Barr virus nuclear antigens contains a glycine-alanine copolymer domain.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 80 ·No. 18 ·1983-09-00 ·Pages 5665-9

Hennessy K, Kieff E

Abstract

A gene fusion between an Epstein-Barr virus (EBV) triplet nucleotide repeat array (IR3), which has homology to host DNA, and lacZ was used to demonstrate that this EBV sequence encodes part of the Epstein-Barr nuclear antigen (EBNA). The IR3 sequence is translated into a glycine-alanine copolymer that reacts with anti-EBNA human sera. Some EBV-immune human antisera recognize a second intranuclear protein that is also specific for latently infected cells and is designated EBNA2. EBNA2 is not related to EBNA1 because the molecular mass of EBNA2 is 82 kilodaltons, whereas that of EBNA1 varies from 68 to 85 kilodaltons among cells transformed by different EBV isolates; also EBNA2 does not contain the copolymer domain of EBNA1.

MeSH Terms
Animals Antigens, Viral/analysis,genetics Base Sequence DNA, Viral/metabolism Epstein-Barr Virus Nuclear Antigens Herpesvirus 4, Human/immunology Peptides/analysis Polymers Protein Biosynthesis Rabbits beta-Galactosidase/genetics
Chemicals
Antigens, Viral DNA, Viral Epstein-Barr Virus Nuclear Antigens Peptides Polymers poly(alanylglycine) beta-Galactosidase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Hennessy K
Kieff E
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35 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.80.18.5665
Published
1983-09-00
Pages
5665-9
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC384319
Subset
IM
Grants
NCI NIH HHS · CA 17281 · United States
NCI NIH HHS · CA 19264 · United States
NIGMS NIH HHS · GM 07183 · United States
Databases
GENBANK
K00106
External Links
PubMed source DOI: 10.1073/pnas.80.18.5665 PMC Full Text View journal details
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