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Blood, Vol. 94 No. 6 (September 15), 1999:
pp. 1899-1905
CCR5 Binds Multiple CC-Chemokines: MCP-3 Acts as a Natural Antagonist
Cédric Blanpain,
Isabelle Migeotte,
Benhur Lee,
Jalal Vakili,
Benjamin J. Doranz,
Cédric Govaerts,
Gilbert Vassart,
Robert W. Doms, and
Marc Parmentier
From IRIBHN and Service de Génétique Médicale,
Université Libre de Bruxelles, Campus Erasme, Bruxelles, Belgium;
and the Department of Pathology and Laboratory Medicine, University of
Pennsylvania, Philadelphia, PA.
CCR5 was first characterized as a receptor for MIP-1 , MIP-1 ,
and RANTES, and was rapidly shown to be the main coreceptor for
M-tropic human immunodeficiency virus (HIV)-1 strains and simian
immunodeficiency virus (SIV). Chemokines constitute a rapidly growing
family of proteins and receptor-chemokine interactions are known to be
promiscuous and redundant. We have therefore tested whether other
CC-chemokines could bind to and activate CCR5. All CC-chemokines
currently available were tested for their ability to compete with
[125I]-MIP-1 binding on a stable cell line expressing
recombinant CCR5, and/or to induce a functional response in these
cells. We found that in addition to MIP-1, MIP-1, and RANTES,
five other CC-chemokines could compete for
[125I]-MIP-1 binding: MCP-2, MCP-3, MCP-4, MCP-1, and
eotaxin binding was characterized by IC50 values of 0.22, 2.14, 5.89, 29.9, and 21.7 nmol/L, respectively. Among these ligands,
MCP-3 had the remarkable property of binding CCR5 with high affinity
without eliciting a functional response, MCP-3 could also inhibit the activation of CCR5 by MIP-1 and may therefore be considered as a
natural antagonist for CCR5. It was unable to induce significant endocytosis of the receptor. Chemokines that could compete with high
affinity for MIP-1 binding could also compete for monomeric gp120
binding, although with variable potencies; maximal gp120 binding
inhibition was 80% for MCP-2, but only 30% for MIP-1. MCP-3 could
compete efficiently for gp120 binding but was, however, found to be a
weak inhibitor of HIV infection, probably as a consequence of its
inability to downregulate the receptor.
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Y. Percherancier, T. Planchenault, A. Valenzuela-Fernandez, J.-L. Virelizier, F. Arenzana-Seisdedos, and F. Bachelerie
Palmitoylation-dependent Control of Degradation, Life Span, and Membrane Expression of the CCR5 Receptor
J. Biol. Chem.,
August 17, 2001;
276(34):
31936 - 31944.
[Abstract]
[Full Text]
[PDF]
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