PMID- 8561975
OWN - NLM
STAT- MEDLINE
DCOM- 19960305
LR  - 20190718
IS  - 0269-9370 (Print)
IS  - 0269-9370 (Linking)
VI  - 9
IP  - 11
DP  - 1995 Nov
TI  - The gp120 envelope of HIV-1 binds peptides in a similar manner to human leukocyte 
      antigens.
PG  - 1229-35
AB  - OBJECTIVE: All the conserved regions of HIV gp120 have at least some partial 
      homology with human leukocyte antigen (HLA) class I or class II. One functional 
      similarity is the ability of gp120 and HLA class II to bind CD4. Given the close 
      association between HIV-induced disease and the amount of immune activation and 
      anergy, features closely associated with chronic allogenic stimulation, we asked 
      whether gp120 shared any other properties of HLA, in this case the ability to 
      bind peptides. DESIGN: T-cell epitope peptides known to bind to soluble HLA class 
      I or class II were photolabelled and made radioactive. Cross-linking of modified 
      peptides to soluble HLA class I, II and gp120 was activated by ultraviolet light 
      and analysed by sodium dodecylsulphate-polyacrylamide gel electrophoresis. 
      RESULTS: A signal peptide binding to HLA class I and a haemagglutinin peptide 
      that binds to HLA class II were found to bind soluble gp120 specifically; binding 
      and cross-linking could be competed out with excess of the unmodified peptides 
      but not unrelated control peptides. Molecular modelling of gp120 suggests shared 
      anchor sites for peptides binding to both HLA and gp120 soluble molecules. 
      CONCLUSIONS: The ability to bind these two peptides suggests that gp120 has a 
      peptide-binding site of broad specificity, which if functional in vivo, could 
      compete with normal peptide loading of major histocompatibility complex (MHC) 
      class I and/or class II peptides, as well as aberrantly stimulate the T-cell 
      receptor (by virtue of its potential to be mistaken for an allogenic MHC/peptide 
      complex), resulting in immune activation, anergy and apoptosis in susceptible 
      hosts.
FAU - Sheikh, M J
AU  - Sheikh MJ
AD  - Department of Cellular and Molecular Sciences, St George's Hospital Medical 
      School, London, UK.
FAU - Ongradi, J
AU  - Ongradi J
FAU - Austen, B M
AU  - Austen BM
FAU - Dalgleish, A G
AU  - Dalgleish AG
LA  - eng
GR  - Wellcome Trust/United Kingdom
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - AIDS
JT  - AIDS (London, England)
JID - 8710219
RN  - 0 (Epitopes)
RN  - 0 (HIV Envelope Protein gp120)
RN  - 0 (HLA Antigens)
RN  - 0 (Peptides)
SB  - IM
CIN - AIDS. 1999 Sep 10;13(13):1799-801. PMID: 10509594
MH  - Amino Acid Sequence
MH  - Binding, Competitive
MH  - Epitopes/metabolism
MH  - HIV Envelope Protein gp120/*metabolism
MH  - *HIV-1
MH  - HLA Antigens/*metabolism
MH  - Humans
MH  - Molecular Sequence Data
MH  - Peptides/chemical synthesis/*metabolism
MH  - T-Lymphocytes/immunology/*metabolism
EDAT- 1995/11/01 00:00
MHDA- 2000/03/29 09:00
CRDT- 1995/11/01 00:00
PHST- 1995/11/01 00:00 [pubmed]
PHST- 2000/03/29 09:00 [medline]
PHST- 1995/11/01 00:00 [entrez]
AID - 10.1097/00002030-199511000-00003 [doi]
PST - ppublish
SO  - AIDS. 1995 Nov;9(11):1229-35. doi: 10.1097/00002030-199511000-00003.