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

Shariq M Usmani1, Onofrio Zirafi1, Janis A Müller1

  • 1Institute of Molecular Virology, Ulm University Medical Center, 89081 Ulm, Germany.

Nature Communications
|April 3, 2014
PubMed

Insights

Naturally occurring amyloid fibrils in semen, including prostatic acid phosphatase (PAP) fragments, were visualized for the first time. These fibrils enhance HIV infection, aiding its sexual transmission.

Area of Science:

  • * Virology and Biochemistry
  • * Human Reproductive Health

Background:

  • * Naturally occurring semen proteins, prostatic acid phosphatase (PAP) and semenogelins, can form amyloid fibrils in vitro.
  • * These amyloid fibrils are known to enhance HIV infection.
  • * The in vivo presence and role of amyloid fibrils in human semen were previously unconfirmed.

Purpose of the Study:

  • * To directly visualize and characterize amyloid fibrils in human ejaculates.
  • * To determine if naturally occurring amyloid fibrils in semen interact with HIV.
  • * To assess the impact of these fibrils on HIV infectivity.

Main Methods:

  • * Advanced confocal and electron microscopy techniques were employed for direct imaging.
  • * Human semen samples were analyzed for the presence of amyloid aggregates.
  • * Interactions between detected fibrils and HIV particles were investigated.

Main Results:

  • * Amyloid aggregates were detected in all analyzed human semen samples.
  • * These aggregates were found to partially comprise prostatic acid phosphatase (PAP) fragments.
  • * The identified amyloid fibrils interact with HIV particles and significantly increase viral infectivity.

Conclusions:

  • * Human semen naturally contains amyloid fibrils.
  • * These naturally occurring amyloid fibrils, including PAP fragments, play a role in promoting HIV sexual transmission.
  • * The findings highlight a novel mechanism exploited by HIV for propagation.