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J Exp Med. 2004 Nov 15;200(10):1337-46.

Secretory leukocyte protease inhibitor binds to annexin II, a cofactor for macrophage HIV-1 infection.

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Oral Infection and Immunity Branch, NIDCR, NIH, 30 Convent Dr., MSC4352, Building 30, Room 320, Bethesda, MD 20892, USA.


The distribution of secretory leukocyte protease inhibitor (SLPI) at entry portals indicates its involvement in defending the host from pathogens, consistent with the ability of SLPI to inhibit human immunodeficiency virus (HIV)-1 infection by an unknown mechanism. We now demonstrate that SLPI binds to the membrane of human macrophages through the phospholipid-binding protein, annexin II. Based on the recent identification of human cell membrane phosphatidylserine (PS) in the outer coat of HIV-1, we define a novel role for annexin II, a PS-binding moiety, as a cellular cofactor supporting macrophage HIV-1 infection. Moreover, this HIV-1 PS interaction with annexin II can be disrupted by SLPI or other annexin II-specific inhibitors. The PS-annexin II connection may represent a new target to prevent HIV-1 infection.

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