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

Martellini, Julie A; Cole, Amy L; Venkataraman, Nitya; Quinn, Gerry A; Svoboda, Pavel; Gangrade, Bhushan K; Pohl, Jan; Sørensen, Ole E LU and Cole, Alexander M (2009) In The FASEB journal : official publication of the Federation of American Societies for Experimental Biology 23(10). p.3609-3618
Abstract
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... (More)
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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
The FASEB journal : official publication of the Federation of American Societies for Experimental Biology
volume
23
issue
10
pages
3609 - 3618
publisher
The Federation of American Societies for Experimental Biology
external identifiers
  • WOS:000270354300037
  • PMID:19487309
  • Scopus:70349672703
ISSN
1530-6860
DOI
10.1096/fj.09-131961
language
English
LU publication?
yes
id
79aae19b-a6b4-4e96-b541-aebf8c8642c6 (old id 1434642)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/19487309?dopt=Abstract
date added to LUP
2009-07-02 12:44:39
date last changed
2017-01-01 07:54:08
@article{79aae19b-a6b4-4e96-b541-aebf8c8642c6,
  abstract     = {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.},
  author       = {Martellini, Julie A and Cole, Amy L and Venkataraman, Nitya and Quinn, Gerry A and Svoboda, Pavel and Gangrade, Bhushan K and Pohl, Jan and Sørensen, Ole E and Cole, Alexander M},
  issn         = {1530-6860},
  language     = {eng},
  number       = {10},
  pages        = {3609--3618},
  publisher    = {The Federation of American Societies for Experimental Biology},
  series       = {The FASEB journal : official publication of the Federation of American Societies for Experimental Biology},
  title        = {Cationic polypeptides contribute to the anti-HIV-1 activity of human seminal plasma.},
  url          = {http://dx.doi.org/10.1096/fj.09-131961},
  volume       = {23},
  year         = {2009},
}