2. Academic Validation
  3. Semen-derived amyloid fibrils drastically enhance HIV infection

Semen-derived amyloid fibrils drastically enhance HIV infection

  • Cell. 2007 Dec 14;131(6):1059-71. doi: 10.1016/j.cell.2007.10.014.
Jan Münch 1,  Elke Rücker,  Ludger Ständker,  Knut Adermann,  Christine Goffinet,  Michael Schindler,  Steffen Wildum,  Raghavan Chinnadurai,  Devi Rajan,  Anke Specht,  Guillermo Giménez-Gallego,  Pedro Cuevas Sánchez,  Douglas M Fowler,  Atanas Koulov,  Jeffery W Kelly,  Walther Mothes,  Jean-Charles Grivel,  Leonid Margolis,  Oliver T Keppler,  Wolf-Georg Forssmann,  Frank Kirchhoff
Affiliations

Affiliation

  • 1 Institute of Virology, University Clinic of Ulm, 89081 Ulm, Germany.
PMID: 18083097 DOI: 10.1016/j.cell.2007.10.014
Abstract

Sexual intercourse is the major route of HIV transmission. To identify endogenous factors that affect the efficiency of sexual viral transmission, we screened a complex peptide/protein library derived from human semen. We show that naturally occurring fragments of the abundant semen marker prostatic acidic Phosphatase (PAP) form amyloid fibrils. These fibrils, termed Semen-derived Enhancer of Virus Infection (SEVI), capture HIV virions and promote their attachment to target cells, thereby enhancing the infectious virus titer by several orders of magnitude. Physiological concentrations of SEVI amplified HIV Infection of T cells, macrophages, ex vivo human tonsillar tissues, and transgenic rats in vivo, as well as trans-HIV Infection of T cells by dendritic or epithelial cells. Amyloidogenic PAP fragments are abundant in seminal fluid and boost semen-mediated enhancement of HIV Infection. Thus, they may play an important role in sexual transmission of HIV and could represent new targets for its prevention.

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