Semen-derived amyloid fibrils drastically enhance HIV infection

Cell. 2007 Dec 14;131(6):1059-71. doi: 10.1016/j.cell.2007.10.014.


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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, N.I.H., Intramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acid Phosphatase
  • Amyloid / isolation & purification
  • Amyloid / physiology*
  • Animals
  • Animals, Genetically Modified
  • HIV Infections / transmission*
  • Humans
  • Peptide Fragments / physiology*
  • Peptide Library
  • Protein Tyrosine Phosphatases / chemistry*
  • Protein Tyrosine Phosphatases / physiology*
  • Rats
  • Semen / enzymology
  • Semen / metabolism*
  • Semen / physiology
  • Sexually Transmitted Diseases, Viral / metabolism*
  • Viral Load


  • Amyloid
  • Peptide Fragments
  • Peptide Library
  • Acid Phosphatase
  • prostatic acid phosphatase
  • prostatic acid phosphatase (248-286), human
  • Protein Tyrosine Phosphatases