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

• Published in: Nature communications Vol. 5; no. 1; p. 3508
• Main Authors: Usmani, Shariq M, Zirafi, Onofrio, Müller, Janis A, Sandi-Monroy, Nathallie L, Yadav, Jay K, Meier, Christoph, Weil, Tanja, Roan, Nadia R, Greene, Warner C, Walther, Paul, Nilsson, K Peter R, Hammarström, Per, Wetzel, Ronald, Pilcher, Christopher D, Gagsteiger, Friedrich, Fändrich, Marcus, Kirchhoff, Frank, Münch, Jan
• Format: Journal Article
• Language: English
• Published: England Nature Publishing Group 01.04.2014
• Subjects: Acid Phosphatase; Amyloid - metabolism; Amyloid - ultrastructure; HIV Infections - metabolism; HIV Infections - virology; HIV-1 - physiology; Humans; Male; Microscopy, Confocal; Microscopy, Electron, Transmission; Protein Tyrosine Phosphatases - metabolism; Semen - metabolism; Semen - virology; Seminal Vesicle Secretory Proteins - metabolism; TECHNOLOGY; TEKNIKVETENSKAP
• ISSN: 2041-1723; 2041-1723
• DOI: 10.1038/ncomms4508

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.