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Secretory Leukocyte Protease Inhibitor (SLPI): Oxidation of SLPI Does Not Explain Its Variable Anti-HIV Activity

Department of Microbiology, School of Dentistry, University of the Pacific, 2155 Webster Street, San Francisco, California 941 15.2399), USA

N. Shine

Department of Microbiology, School of Dentistry, University of the Pacific, 2155 Webster Street, San Francisco, California 941 15.2399), USA

E. Pretzer

Department of Microbiology, School of Dentistry, University of the Pacific, 2155 Webster Street, San Francisco, California 941 15.2399), USA, Lynx Thera peutics, 3832 Bay Center Place, Hayward, California 94545, USA

N. Düzgünes

Department of Microbiology, School of Dentistry, University of the Pacific, 2155 Webster Street, San Francisco, California 941 15.2399), USA

Secretory leuhocyte protease inhibitor (SLPI) has been proposed as a potential inhibitor of HIV-1 infection in human saliva. Although the ability of recombinant (r) SLPI to inhibit HIV-1 infection of macrophages and primary T-cells has been demonstrated by two independent laboratories, evidence to the contrary has also been reported. This study re-examines the anti-HIV effect of rSLPI and investigates the effects of repeated freeze-thawing and oxidation on the anti-HIV activity of rSLPI. rSLPI inhibited HIV-1 _BaL infection of human macrophages in a highly variable manner. HPLC and electrospray ionization mass spectrometry (ESI) analyses indicated that variability in our inhibition data could not be attributed to the degradation or oxidation of rSLPI. These results suggest that the variable anti-HIV effect of rSLPI may be due to differential expression of the cell-surface molecule(s) to which SLPI binds rather than to changes in the rSLPI molecule.

Key Words: HIV-1 • saliva • SLPI • macrophages.

Journal of Dental Research, Vol. 78, No. 12, 1773-1776 (1999)
DOI: 10.1177/00220345990780120201


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