Title

HIV-1 Enhancing Effect of Prostatic Acid Phosphatase Peptides Is Reduced in Human Seminal Plasma

Authors

Authors

J. A. Martellini; A. L. Cole; P. Svoboda; O. Stuchlik; L. M. Chen; K. X. Chai; B. K. Gangrade; O. E. Sorensen; J. Pohl;A. M. Cole

Comments

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Abbreviated Journal Title

PLoS One

Keywords

SEMEN-MEDIATED ENHANCEMENT; ANTIMICROBIAL PEPTIDES; SEMENOGELIN-I; INFECTION; DEFENSINS; ANTIGEN; INHIBITOR; SUBSTRATE; FLUID; SEVI; Multidisciplinary Sciences

Abstract

We recently reported that HIV-1 infection can be inhibited by innate antimicrobial components of human seminal plasma (SP). Conversely, naturally occurring peptidic fragments from the SP-derived prostatic acid phosphatase ( PAP) have been reported to form amyloid fibrils called "SEVI'' and enhance HIV-1 infection in vitro. In order to understand the biological consequence of this proviral effect, we extended these studies in the presence of human SP. PAP-derived peptides were agitated to form SEVI and incubated in the presence or absence of SP. While PAP-derived peptides and SEVI alone were proviral, the presence of 1% SP ablated their proviral activity in several different anti-HIV-1 assays. The anti-HIV-1 activity of SP was concentration dependent and was reduced following filtration. Supraphysiological concentrations of PAP peptides and SEVI incubated with diluted SP were degraded within hours, with SP exhibiting proteolytic activity at dilutions as high as 1:200. Sub-physiological concentrations of two prominent proteases of SP, prostate-specific antigen (PSA) and matriptase, could degrade physiological and supraphysiological concentrations of PAP peptides and SEVI. While human SP is a complex biological fluid, containing both antiviral and proviral factors, our results suggest that PAP peptides and SEVI may be subject to naturally occurring proteolytic components capable of reducing their proviral activity.

Journal Title

Plos One

Volume

6

Issue/Number

1

Publication Date

1-1-2011

Document Type

Article

Language

English

First Page

11

WOS Identifier

WOS:000286522200047

ISSN

1932-6203

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