CCR5 N-terminus peptides enhance X4 HIV-1 infection by CXCR4 up-regulation

M. Dettin, M. Zanchetta, A. Pasquato, M. Borrello, D. Piatier-Tonneau, C. Di Bello, A. De Rossi

Research output: Contribution to journalArticlepeer-review


The HIV-1 envelope glycoprotein gp120 interacts consecutively with CD4 and CCR5 to mediate the entry of R5-HIV-1 strains into target cells. The N-terminus of CCR5, which contains several sulfated tyrosines, plays a critical role in gp120-CCR5 binding and, consequently, in viral entry. Here, we demonstrate that a tyrosine sulfated peptide, reproducing the entire N-terminal extracellular region of CCR5, its unsulfated analogue, and a point-mutated peptide are unable to inhibit R5-HIV-1 mediated infection, competing with the entire CCR5 in the formation of gp120-CD4-CCR5 complex. Surprisingly, these peptides show the capability of enhancing HIV-1 infection caused by X4 strains through the up-regulation of both CD4 and CXCR4 receptors.

Original languageEnglish
Pages (from-to)640-646
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number3
Publication statusPublished - Aug 1 2003


  • AIDS
  • CCR5
  • CD4
  • CXCR4
  • gp120
  • HIV-1
  • Peptide
  • Sulfated tyrosines
  • Up-regulation
  • Viral entry

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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