Naturally occurring fragments from two distinct regions of the prostatic acid phosphatase form amyloidogenic enhancers of HIV infection

J Virol. 2012 Jan;86(2):1244-9. doi: 10.1128/JVI.06121-11. Epub 2011 Nov 16.


Semen is the major vector for HIV-1 transmission. We previously isolated C-proximal fragments of the prostatic acid phosphatase (PAP) from semen which formed amyloid fibrils that potently enhanced HIV infection. Here, we used the same methodology and identified another amyloidogenic peptide. Surprisingly, this peptide is derived from an N-proximal fragment of PAP (PAP85-120) and forms, similar to the C-proximal fragments, positively charged fibrillar structures that increase virion attachment to cells. Our results provide a first example for amyloid formation by fragments of distinct regions of the same precursor and further emphasize the possible importance of amyloidogenic peptides in HIV transmission.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acid Phosphatase
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Amyloid / chemistry
  • Amyloid / metabolism*
  • Cell Line
  • HIV Infections / enzymology*
  • HIV Infections / transmission
  • HIV Infections / virology
  • HIV-1 / physiology*
  • Humans
  • Male
  • Molecular Sequence Data
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism*
  • Protein Tyrosine Phosphatases / chemistry*
  • Protein Tyrosine Phosphatases / genetics
  • Protein Tyrosine Phosphatases / metabolism*
  • Semen / chemistry
  • Semen / enzymology*
  • Sequence Alignment
  • Virus Attachment


  • Amyloid
  • Peptide Fragments
  • Acid Phosphatase
  • prostatic acid phosphatase
  • Protein Tyrosine Phosphatases