A Broad-Spectrum Chemokine Antagonist Encoded by Kaposi's Sarcoma-Associated Herpesvirus-Reference-Cited by-同舟云学术

A Broad-Spectrum Chemokine Antagonist Encoded by Kaposi's Sarcoma-Associated Herpesvirus

Published:1997-09-12 Issue:5332 Volume:277 Page:1656-1659
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Kledal Thomas N.¹²³⁴⁵,Rosenkilde Mette M.¹²³⁴⁵,Coulin Florence¹²³⁴⁵,Simmons Graham¹²³⁴⁵,Johnsen Anders H.¹²³⁴⁵,Alouani Sami¹²³⁴⁵,Power Christine A.¹²³⁴⁵,Lüttichau Hans R.¹²³⁴⁵,Gerstoft Jan¹²³⁴⁵,Clapham Paul R.¹²³⁴⁵,Clark-Lewis Ian¹²³⁴⁵,Wells Timothy N. C.¹²³⁴⁵,Schwartz Thue W.¹²³⁴⁵

Affiliation:

1. T. N. Kledal, M. M. Rosenkilde, T. W. Schwartz, Laboratory for Molecular Pharmacology, Institute of Pharmacology, Panum Institute, University of Copenhagen, DK-2200 Copenhagen, Denmark.

2. A. H. Johnsen, Department of Clinical Biochemistry; H. R. Lüttichau and J. Gerstoft, Department of Infectious Diseases, Rigshospitalet, DK-2100 Copenhagen, Denmark.

3. G. Simmons and P. R. Clapham, Section of Virology, Chester Beatty Laboratories, The Institute of Cancer Research, Fulham Road, London, SW3 6JB, UK.

4. I. Clark-Lewis, Biomedical Research Center, University of British Columbia, Vancouver, B.C., V6T 1Z3, Canada.

5. F. Coulin, S. Alouani, C. A. Power, T. N. C. Wells, Geneva Biomedical Research Institute, Glaxo Wellcome Research and Development S.A., 1228 Plan-les-Ouates, Geneva, Switzerland.

Abstract

Kaposi's sarcoma–associated herpesvirus encodes a chemokine called vMIP-II. This protein displayed a broader spectrum of receptor activities than any mammalian chemokine as it bound with high affinity to a number of both CC and CXC chemokine receptors. Binding of vMIP-II, however, was not associated with the normal, rapid mobilization of calcium from intracellular stores; instead, it blocked calcium mobilization induced by endogenous chemokines. In freshly isolated human monocytes the virally encoded vMIP-II acted as a potent and efficient antagonist of chemotaxis induced by chemokines. Because vMIP-II could inhibit cell entry of human immunodeficiency virus (HIV) mediated through CCR3 and CCR5 as well as CXCR4, this protein may serve as a lead for development of broad-spectrum anti-HIV agents.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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