HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Casartelli, N. Articles by Doria, M. Search for Related Content PubMed PubMed Citation Articles by Casartelli, N. Articles by Doria, M. Agricola Articles by Casartelli, N. Articles by Doria, M.

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^1,

¹ Division of Immunology and Infectious Disease, Children's Hospital Bambino Gesù, Piazza S. Onofrio 4, 00165 Rome, Italy
² Department of Virology, Universitätsklinikum Heidelberg, 69120 Heidelberg, Germany
³ Department of Pediatrics, University Tor Vergata, 00133 Rome, Italy

Correspondence
Margherita Doria
doria{at}uniroma2.it

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.

Present address: Virus and Immunity Group, Department of Virology, Institut Pasteur, 75724 Paris Cedex 15, France.

This article has been cited by other articles:

				S. Rauch, K. Pulkkinen, K. Saksela, and O. T. Fackler Human Immunodeficiency Virus Type 1 Nef Recruits the Guanine Exchange Factor Vav1 via an Unexpected Interface into Plasma Membrane Microdomains for Association with p21-Activated Kinase 2 Activity J. Virol., March 15, 2008; 82(6): 2918 - 2929. [Abstract] [Full Text] [PDF]

				C. M. Noviello, S. Benichou, and J. C. Guatelli Cooperative Binding of the Class I Major Histocompatibility Complex Cytoplasmic Domain and Human Immunodeficiency Virus Type 1 Nef to the Endosomal AP-1 Complex via Its {micro} Subunit J. Virol., February 1, 2008; 82(3): 1249 - 1258. [Abstract] [Full Text] [PDF]

				G. Giolo, F. Neri, N. Casartelli, M. Potesta, F. Belleudi, M. R. Torrisi, and M. Doria Internalization and intracellular retention of CD4 are two separate functions of the human immunodeficiency virus type 1 Nef protein J. Gen. Virol., November 1, 2007; 88(11): 3133 - 3138. [Abstract] [Full Text] [PDF]