PMID- 19098488
OWN - NLM
STAT- MEDLINE
DCOM- 20090306
LR  - 20211028
IS  - 1473-5571 (Electronic)
IS  - 0269-9370 (Linking)
VI  - 23
IP  - 2
DP  - 2009 Jan 14
TI  - Reciprocal recognition of an HLA-Cw4-restricted HIV-1 gp120 epitope by CD8+ T 
      cells and NK cells.
PG  - 189-93
LID - 10.1097/QAD.0b013e32831fb55a [doi]
AB  - OBJECTIVES: The HIV-1 Nef protein selectively downregulates human leukocyte 
      antigen (HLA)-A and HLA-B but not HLA-C molecules on the surface of infected 
      cells. This allows HIV-infected cells to evade recognition by most cytotoxic T 
      lymphocytes (CTLs) and natural killer (NK) cells. We investigated the recognition 
      of an HLA-Cw4-restricted HIV-1 gp120 epitope SFNCGGEFF (SF9) and its variant 
      SFNCGGEFL (SL9) by T cells and NK receptors. DESIGN AND METHOD: Recognition of 
      HIV-1 gp120 peptides (SF9 and SL9) by T-cell clones was measured by staining with 
      HLA-Cw4-peptide tetrameric complexes and cytolytic assays using target cell 
      pulsed with either peptides. KIR2DL1 binding to these two peptides was measured 
      using surface plasmon resonance and tetramer staining of an NK cell line. RESULT: 
      : CTLs could recognize SF9 better than the variant SL9, as shown by both tetramer 
      staining and cytolytic assays. Intriguingly, an HLA-Cw4 tetramer folded with the 
      'escape' variant SL9 could bind to KIR2DL1 on NK cell lines with higher affinity 
      than HLA-Cw4-SF9. The binding of KIR2DL1 to its ligand results in inhibition of 
      NK cell function. Our results indicate that the HIV-1 gp120 variant peptide SL9 
      could potentially escape both from NK cell and CTL recognition by increasing its 
      affinity for KIR2DL1 binding. CONCLUSION: These data suggest that HIV-1 can 
      acquire mutations that are capable of escaping from both CTL and NK cell 
      recognition, a phenomenon we have termed 'double escape'.
FAU - Thananchai, Hathairat
AU  - Thananchai H
AD  - Department of Microbiology, Faculty of Medicine, Chiang Mai University, Chiang 
      Mai, Thailand.
FAU - Makadzange, Tariro
AU  - Makadzange T
FAU - Maenaka, Katsumi
AU  - Maenaka K
FAU - Kuroki, Kimiko
AU  - Kuroki K
FAU - Peng, Yanchun
AU  - Peng Y
FAU - Conlon, Chris
AU  - Conlon C
FAU - Rowland-Jones, Sarah
AU  - Rowland-Jones S
FAU - Dong, Tao
AU  - Dong T
LA  - eng
GR  - G0600520/MRC_/Medical Research Council/United Kingdom
GR  - MC_U137884180/MRC_/Medical Research Council/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 (HIV Envelope Protein gp120)
RN  - 0 (HLA-C Antigens)
RN  - 0 (HLA-C*04 antigen)
RN  - 0 (KIR2DL1 protein, human)
RN  - 0 (Receptors, KIR2DL1)
SB  - IM
MH  - Antibody Affinity/immunology
MH  - Antigen-Antibody Reactions/immunology
MH  - Cell Line
MH  - Cytotoxicity Tests, Immunologic/methods
MH  - Cytotoxicity, Immunologic/immunology
MH  - HIV Envelope Protein gp120/*immunology
MH  - HIV-1/genetics/*immunology
MH  - HLA-C Antigens/*immunology
MH  - Humans
MH  - Immune Tolerance
MH  - Killer Cells, Natural/*immunology
MH  - Receptors, KIR2DL1/immunology
MH  - T-Lymphocytes, Cytotoxic/*immunology
EDAT- 2008/12/23 09:00
MHDA- 2009/03/07 09:00
CRDT- 2008/12/23 09:00
PHST- 2008/12/23 09:00 [entrez]
PHST- 2008/12/23 09:00 [pubmed]
PHST- 2009/03/07 09:00 [medline]
AID - 00002030-200901140-00005 [pii]
AID - 10.1097/QAD.0b013e32831fb55a [doi]
PST - ppublish
SO  - AIDS. 2009 Jan 14;23(2):189-93. doi: 10.1097/QAD.0b013e32831fb55a.