Direct visualization of HIV-enhancing endogenous amyloid fibrils in human semen

Shariq M. Usmani, Onofrio Zirafi, Janis A. Müller, Nathallie L. Sandi-Monroy, Jay K. Yadav, Christoph Meier, Tanja Weil, Nadia R. Roan, Warner C. Greene, Paul Walther, K. Peter R. Nilsson, Per Hammarström, Ronald Wetzel, Christopher D. Pilcher, Friedrich Gagsteiger, Marcus Fändrich, Frank Kirchhoff and Jan Münch ()
Additional contact information
Shariq M. Usmani: Institute of Molecular Virology, Ulm University Medical Center
Onofrio Zirafi: Institute of Molecular Virology, Ulm University Medical Center
Janis A. Müller: Institute of Molecular Virology, Ulm University Medical Center
Nathallie L. Sandi-Monroy: Institute of Molecular Virology, Ulm University Medical Center
Jay K. Yadav: Institute of Pharmaceutical Biotechnology, Ulm University
Christoph Meier: Institute of Organic Chemistry III/Macromolecular Chemistry, Ulm University
Tanja Weil: Institute of Organic Chemistry III/Macromolecular Chemistry, Ulm University
Nadia R. Roan: University of California
Warner C. Greene: Gladstone Institute of Virology and Immunology, University of California at San Francisco
Paul Walther: Central Electron Microscopy Facility, Ulm University
K. Peter R. Nilsson: Linköping University
Per Hammarström: Linköping University
Ronald Wetzel: University of Pittsburgh School of Medicine
Christopher D. Pilcher: San Francisco General Hospital, University of California
Friedrich Gagsteiger: Kinderwunsch-Zentrum Ulm
Marcus Fändrich: Institute of Pharmaceutical Biotechnology, Ulm University
Frank Kirchhoff: Institute of Molecular Virology, Ulm University Medical Center
Jan Münch: Institute of Molecular Virology, Ulm University Medical Center

Nature Communications, 2014, vol. 5, issue 1, 1-8

Abstract: Abstract Naturally occurring fragments of the abundant semen proteins prostatic acid phosphatase (PAP) and semenogelins form amyloid fibrils in vitro. These fibrils boost HIV infection and may play a key role in the spread of the AIDS pandemic. However, the presence of amyloid fibrils in semen remained to be demonstrated. Here, we use state of the art confocal and electron microscopy techniques for direct imaging of amyloid fibrils in human ejaculates. We detect amyloid aggregates in all semen samples and find that they partially consist of PAP fragments, interact with HIV particles and increase viral infectivity. Our results establish semen as a body fluid that naturally contains amyloid fibrils that are exploited by HIV to promote its sexual transmission.

Date: 2014
References: Add references at CitEc
Citations: View citations in EconPapers (2)

Downloads: (external link)
https://www.nature.com/articles/ncomms4508 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms4508

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms4508

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().