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Updated: Feb 9, 2026
12:06
Collection of Post-mating Semen from the Female Reproductive Tract and Measurement of Semen Liquefaction in Mice
Published on: November 18, 2017
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Structure, function and antagonism of semen amyloids
Annika Röcker1, Nadia R Roan, Jay Kant Yadav
1Institute of Molecular Virology, Ulm University Medical Center, 89081 Ulm, Germany. jan.muench@uni-ulm.de.
Chemical Communications (Cambridge, England)
|June 7, 2018
Summary
Semen contains amyloid fibrils that significantly increase HIV-1 infection rates. Strategies to block these amyloid structures offer new ways to prevent sexual transmission of viruses like HIV.
Area of Science:
- Biochemistry
- Immunology
- Virology
Background:
- Amyloid fibrils are polypeptide aggregates with a cross-β structure.
- While associated with neurodegenerative diseases, they also have functional roles in biological systems.
- Semen contains amyloid fibrils that enhance HIV-1 infection rates.
Purpose of the Study:
- To discuss the identification and properties of semen amyloid fibrils.
- To explore their impact on sexually transmitted diseases and reproductive health.
- To review strategies for antagonizing semen amyloid to prevent viral transmission.
Main Methods:
- Identification of amyloid structures in semen.
- Molecular characterization of these fibrils.
- Assessment of their effects on HIV-1 infection and reproductive health.
Main Results:
- Semen harbors amyloid fibrils that markedly increase HIV-1 infection rates.
- These fibrils have implications for sexual transmission of viruses.
- Understanding these factors opens avenues for novel prevention strategies.
Conclusions:
- Semen amyloid fibrils play a significant role in modulating viral transmission.
- Targeting these amyloid structures presents a promising approach for preventing sexually transmitted infections.
- Further research is needed to fully elucidate their biological functions and therapeutic potential.
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