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Cationic polypeptides contribute to the anti-HIV-1 activity of human seminal plasma

Julie A. Martellini^*, Amy L. Cole^*, Nitya Venkataraman^*, Gerry A. Quinn^*, Pavel Svoboda, Bhushan K. Gangrade, Jan Pohl, Ole E. Sørensen^,1 and Alexander M. Cole^*,1

^* Department of Molecular Biology and Microbiology, Biomolecular Science Center, Burnett School of Biomedical Sciences at University of Central Florida, Orlando, Florida, USA;

Biotechnology Core Facility Branch, Division of Safety Research, Centers for Disease Control and Prevention, Atlanta, Georgia, USA;

Center for Reproductive Medicine, Orlando, Florida, USA; and

Division of Infection Medicine, Department of Clinical Sciences, Lund University, Lund, Sweden

¹ Correspondence: A.M.C., 4000 Central Florida Blvd, Bldg 20, Rm. 236, Orlando, FL 32816, USA. E-mail: acole{at}mail.ucf.edu; O.E.S., BMC, B14, Tornavagen 10, SE-221 84, Lund, Sweden. E-mail: ole_e.sorensen{at}med.lu.se

Mucosal surfaces of the reproductive tract as well as their secretions have important roles in preventing sexual transmission of HIV-1. In the current study, the majority of the intrinsic anti-HIV-1 activity of human seminal plasma (SP) was determined to reside in the cationic polypeptide fraction. Antiviral assays utilizing luciferase reporter cells and lymphocytic cells revealed the ability of whole SP to prevent HIV-1 infection, even when SP was diluted 3200-fold. Subsequent fractionation by continuous flow acid-urea (AU)-PAGE and antiviral testing revealed that cationic polypeptides within SP were responsible for the majority of anti-HIV-1 activity. A proteomic approach was utilized to resolve and identify 52 individual cationic polypeptides that contribute to the aggregate anti-HIV-1 activity of SP. One peptide fragment of semenogelin I, termed SG-1, was purified from SP by a multistep chromatographic approach, protein sequenced, and determined to exhibit anti-HIV-1 activity against HIV-1. Anti-HIV-1 activity was transient, as whole SP incubated for prolonged time intervals exhibited a proportional decrease in anti-HIV-1 activity that was directly attributed to the degradation of semenogelin I peptides. Collectively, these results indicate that the cationic polypeptide fraction of SP is active against HIV-1, and that semenogelin-derived peptides contribute to the intrinsic anti-HIV-1 activity of SP.—Martellini, J. A., Cole, A. C., Venkataraman, N., Quinn, G. A., Svoboda, P., Gangrade, B. K., Pohl, J., Sørensen, O. E., Cole, A. M. Cationic polypeptides contribute to the anti-HIV-1 activity of human seminal plasma.

Key Words: antigens • epitopes • AIDS • reproductive immunology • viral • antimicrobial