You are not currently logged in.
Access your personal account or get JSTOR access through your library or other institution:
If You Use a Screen ReaderThis content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
One of Two Epstein--Barr Virus Nuclear Antigens Contains a Glycinealanine Copolymer Domain
Kevin Hennessy and Elliott Kieff
Proceedings of the National Academy of Sciences of the United States of America
Vol. 80, No. 18, [Part 1: Biological Sciences] (Sep. 15, 1983), pp. 5665-5669
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/14400
Page Count: 5
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Preview not available
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.
Proceedings of the National Academy of Sciences of the United States of America © 1983 National Academy of Sciences