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 Blood, 15 December 2003, Vol. 102, No. 13, pp. 4479-4486.
Prepublished online as a Blood First Edition Paper on August 21, 2003; DOI 10.1182/blood-2003-05-1635.

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IMMUNOBIOLOGY

HIV-1 preferentially binds receptors copatched with cell-surface elastase

Cynthia L. Bristow, Danielle R. Mercatante, and Ryszard Kole

From the Laboratory of Cellular Physiology and Immunology, The Rockefeller University and Population Council, New York, NY, and the Department of Pharmacology and Lineberger Comprehensive Cancer Center, University of North Carolina-Chapel Hill.

Human leukocyte elastase (HLE) interacts with HIV-1 glycoprotein (gp)41, suggesting a nonenzymatic receptor function for HLE in the context of HIV-1. HLE is found localized to the cell surface, but not granules in HIV permissive clones, and to granules, but not the cell surface of HIV nonpermissive clones. Inducing cell-surface HLE expression on HLE null, HIV nonpermissive clones permits HIV infectivity. HIV binding and infectivity diminish in proportion to HLE RNA subtraction. HIV binding and infectivity show dose dependence for the natural HLE ligand {alpha}1 proteinase inhibitor ({alpha}1antitrypsin, {alpha}1PI). Chemokines prevent, whereas {alpha}1PI promotes, copatching of HLE with the canonical HIV receptors. Recent demonstration that decreased viral RNA is significantly correlated with decreased circulating {alpha}1PI in HIV seropositive individuals is consistent with a model in which HLE and {alpha}1PI can serve as HIV coreceptor and cofactor, respectively, and potentially participate in the pathophysiology of HIV disease progression. (Blood. 2003;102:4479-4486)


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