HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Lesner, A. Articles by Simm, M. Search for Related Content PubMed PubMed Citation Articles by Lesner, A. Articles by Simm, M. Pubmed/NCBI databases Compound via MeSH Substance via MeSH Medline Plus Health Information AIDS Medicines

A Soluble Factor Secreted by an HIV-1-Resistant Cell Line Blocks Transcription through Inactivating the DNA-Binding Capacity of the NF-B p65/p50 Dimer¹

Molecular Virology Division, St. Luke’s-Roosevelt Hospital Center, Columbia University Medical Center, New York, NY 10019

The identity and activity of several anti-HIV soluble factor(s) secreted by CD8 and CD4 T lymphocytes have been determined; however, some of them still await definition. We have established an HIV-1-resistant, transformed CD4 T cell line that secretes HIV-1 resistance protein(s). Our studies indicate that this protein(s), called HIV-1 resistance factor (HRF), inhibits transcription of the virus by interfering with the activity of NF-B. In the present report we identified the site at which HRF exerts this inhibition by evaluating a set of discrete events in NF-B action. We tested the B oligonucleotide binding activity in nuclei of resistant cells, nuclear translocation and binding to the HIV-1 long terminal repeat of p65 and p50 proteins from susceptible cells after exposure to HRF, and the binding of recombinant p50 to the B oligonucleotide in vitro as affected by prior or simultaneous exposure to HRF. The results of this experimental schema indicate that HRF interacts with p50 after it enters the nucleus, but before its binding to DNA and that this interaction impedes the formation of an NF-B-DNA complex required for the promotion of transcription. These findings suggest that HRF mediates a novel innate immune response to virus infection.