PMID- 10089882
OWN - NLM
STAT- MEDLINE
DCOM- 19990422
LR  - 20190705
IS  - 0092-8674 (Print)
IS  - 0092-8674 (Linking)
VI  - 96
IP  - 5
DP  - 1999 Mar 5
TI  - Tyrosine sulfation of the amino terminus of CCR5 facilitates HIV-1 entry.
PG  - 667-76
AB  - Chemokine receptors and related seven-transmembrane-segment (7TMS) receptors
      serve as coreceptors for entry of human and simian immunodeficiency viruses
      (HIV-1, HIV-2, and SIV) into target cells. Each of these otherwise diverse
      coreceptors contains an N-terminal region that is acidic and tyrosine rich. Here,
      we show that the chemokine receptor CCR5, a principal HIV-1 coreceptor, is
      posttranslationally modified by O-linked glycosylation and by sulfation of its
      N-terminal tyrosines. Sulfated tyrosines contribute to the binding of CCR5 to
      MIP-1 alpha, MIP-1 beta, and HIV-1 gp120/CD4 complexes and to the ability of
      HIV-1 to enter cells expressing CCR5 and CD4. CXCR4, another important HIV-1
      coreceptor, is also sulfated. Tyrosine sulfation may contribute to the natural
      function of many 7TMS receptors and may be a modification common to primate
      immunodeficiency virus coreceptors.
FAU - Farzan, M
AU  - Farzan M
AD  - Dana-Farber Cancer Institute, Department of Pathology, Harvard Medical School,
      Boston, Massachusetts 02115, USA. farzan@mbcrr.harvard.edu
FAU - Mirzabekov, T
AU  - Mirzabekov T
FAU - Kolchinsky, P
AU  - Kolchinsky P
FAU - Wyatt, R
AU  - Wyatt R
FAU - Cayabyab, M
AU  - Cayabyab M
FAU - Gerard, N P
AU  - Gerard NP
FAU - Gerard, C
AU  - Gerard C
FAU - Sodroski, J
AU  - Sodroski J
FAU - Choe, H
AU  - Choe H
LA  - eng
GR  - AI 24755/AI/NIAID NIH HHS/United States
GR  - AI 28691/AI/NIAID NIH HHS/United States
GR  - AI 41851/AI/NIAID NIH HHS/United States
GR  - etc.
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cell
JT  - Cell
JID - 0413066
RN  - 0 (CD4 Antigens)
RN  - 0 (Chemokine CCL4)
RN  - 0 (Chlorates)
RN  - 0 (HIV Envelope Protein gp120)
RN  - 0 (Macrophage Inflammatory Proteins)
RN  - 0 (Receptors, CCR5)
RN  - 0 (Receptors, CXCR4)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 29166358BF (tyrosine O-sulfate)
RN  - 42HK56048U (Tyrosine)
RN  - EC 2.8.2.- (Sulfotransferases)
SB  - IM
SB  - X
MH  - Amino Acid Sequence
MH  - Animals
MH  - CD4 Antigens/metabolism
MH  - Carbohydrate Conformation
MH  - Cells, Cultured
MH  - Chemokine CCL4
MH  - Chlorates/pharmacology
MH  - Dogs
MH  - Glycosylation
MH  - HIV Envelope Protein gp120/metabolism
MH  - HIV-1/*physiology
MH  - HeLa Cells
MH  - Humans
MH  - Macrophage Inflammatory Proteins/metabolism
MH  - Molecular Sequence Data
MH  - *Protein Processing, Post-Translational/drug effects
MH  - Receptors, CCR5/*chemistry/physiology
MH  - Receptors, CXCR4/chemistry/physiology
MH  - Recombinant Fusion Proteins/metabolism
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - Sulfotransferases/metabolism
MH  - Tumor Cells, Cultured
MH  - Tyrosine/*analogs & derivatives/biosynthesis/physiology
EDAT- 1999/03/25 00:00
MHDA- 1999/03/25 00:01
CRDT- 1999/03/25 00:00
PHST- 1999/03/25 00:00 [pubmed]
PHST- 1999/03/25 00:01 [medline]
PHST- 1999/03/25 00:00 [entrez]
AID - S0092-8674(00)80577-2 [pii]
AID - 10.1016/s0092-8674(00)80577-2 [doi]
PST - ppublish
SO  - Cell. 1999 Mar 5;96(5):667-76. doi: 10.1016/s0092-8674(00)80577-2.