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Issue 55, 2018
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Structure, function and antagonism of semen amyloids

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Abstract

Amyloid fibrils are linear polypeptide aggregates with a cross-β structure. These fibrils are best known for their association with neurodegenerative diseases, such as Alzheimer's or Parkinson's, but they may also be used by living organisms as functional units, e.g. in the synthesis of melanin or in the formation of bacterial biofilms. About a decade ago, in a search for semen factors that modulate infection by HIV-1 (a sexually transmitted virus and the causative agent of the acquired immune deficiency syndrome (AIDS)), it was demonstrated that semen harbors amyloid fibrils capable of markedly increasing HIV infection rates. This discovery not only created novel opportunities to prevent sexual HIV-1 transmission but also stimulated research to unravel the natural role of these factors. We discuss here the identification of these intriguing structures, their molecular properties, and their effects on both sexually transmitted diseases and reproductive health. Moreover, we review strategies to antagonize semen amyloid to prevent sexual transmission of viruses.

Graphical abstract: Structure, function and antagonism of semen amyloids

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Publication details

The article was received on 22 Feb 2018, accepted on 23 Apr 2018 and first published on 06 Jun 2018


Article type: Feature Article
DOI: 10.1039/C8CC01491D
Citation: Chem. Commun., 2018,54, 7557-7569
  • Open access: Creative Commons BY-NC license
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    Structure, function and antagonism of semen amyloids

    A. Röcker, N. R. Roan, J. K. Yadav, M. Fändrich and J. Münch, Chem. Commun., 2018, 54, 7557
    DOI: 10.1039/C8CC01491D

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