The Pro78 residue regulates the capacity of the human immunodeficiency virus type 1 Nef protein to inhibit recycling of major histocompatibility complex class I molecules in an SH3-independent manner

Nicoletta Casartelli, Giorgia Giolo, Francesca Neri, Claudia Haller, Marina Potestà, Paolo Rossi, Oliver T. Fackler, Margherita Doria

Research output: Contribution to journalArticlepeer-review

Abstract

The Nef protein is a crucial pathogenicity factor of human immunodeficiency virus type 1 (HIV-1) that contains a proline-rich motif consisting of four conserved prolines: Pro69 (P69), P72, P75 and P78. P72 and P75 were shown to bind Src homology domains 3 (SH3) and have been implicated in many biological functions of Nef, including downmodulation of cell-surface major histocompatibility complex class I (MHC-I). P78 is involved together with P69 in positioning of the Nef-SH3 complex and it has been shown to be essential for Nef activity of MHC-I downmodulation. It is shown here that alteration of P78 affects recycling of MHC-I molecules to the cell surface, but does not interfere with SH3 binding. In addition, it is demonstrated that P72 and P75, and thus the SH3-binding capacity, are fully dispensable for Nef activity on MHC-I.

Original languageEnglish
Pages (from-to)2291-2296
Number of pages6
JournalJournal of General Virology
Volume87
Issue number8
DOIs
Publication statusPublished - Aug 2006

ASJC Scopus subject areas

  • Virology
  • Immunology

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