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Journal of Virology, May 2001, p. 4402-4406, Vol. 75, No. 9
Laboratory of Experimental
Chemotherapy1 and Laboratory of
Molecular Immunology,2 Department of
Microbiology and Immunology, Rega Institute for Medical Research,
Katholieke Universiteit Leuven, Leuven, Belgium
Received 14 September 2000/Accepted 29 January 2001
The CC-chemokines RANTES, macrophage inflammatory protein 1
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.75.9.4402-4406.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
The LD78
Isoform of MIP-1
Is the Most Potent
CC-Chemokine in Inhibiting CCR5-Dependent Human Immunodeficiency Virus
Type 1 Replication in Human Macrophages
(MIP-1
), and MIP-1
are natural ligands for the CC-chemokine receptor CCR5. MIP-1
, also known as LD78
, has an isoform,
LD78
, which was identified as the product of a nonallelic gene. The two isoforms differ in only 3 amino acids. LD78
was recently reported to be a much more potent CCR5 agonist than LD78
and RANTES
in inducing intracellular Ca2+ signaling and chemotaxis.
CCR5 is expressed by human monocytes/macrophages (M/M) and represents
an important coreceptor for macrophage-tropic, CCR5-using (R5) human
immunodeficiency virus type 1 (HIV-1) strains to infect the cells. We
compared the antiviral activities of LD78
and the other
CC-chemokines in M/M. LD78
at 100 ng/ml almost completely blocked
HIV-1 replication, while at the same concentration LD78
had only
weak antiviral activity. Moreover, when HIV-1 infection in M/M was
monitored by a flow cytometric analysis using p24 antigen intracellular
staining, LD78
proved to be the most antivirally active of the
chemokines. RANTES, once described as the most potent chemokine in
inhibiting R5 HIV-1 infection, was found to be considerably less active
than LD78
. LD78
strongly downregulated CCR5 expression in M/M,
thereby explaining its potent antiviral activity.
*
Corresponding author. Mailing address: Department of
Experimental Medicine, University of Rome "Tor Vergata," Rome,
Italy. Phone: 39 06 7259 6553. Fax: 39 06 72596552. E-mail:
aquaro{at}uniroma2.it.
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