Table of Contents
ISRN Virology
Volume 2013, Article ID 709734, 14 pages
http://dx.doi.org/10.5402/2013/709734
Research Article

A Novel Human Membrane Protein Interacting with the Short Fiber of Enteric Adenovirus

1Institut de Biologie Structurale Jean-Pierre Ebel, 41, rue Jules Horowitz, 38027 Grenoble Cedex 1, France
2IRBA-CRSSA, Unité de Virologie, 38702 La Tronche, France
3Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawinskiego 5a, 02106 Warszawa, Poland
4CRBM, Universote Montpellier 1, 34293 Montpellier, France
5Department of Microbiology, Biomedical Sciences Institute, University of Sao Paulo, 05508-900 Sao Paulo, SP, Brazil
6TheREx, TIMC-IMAG, UMR 5525, CNRS/UJF, Domaine de La Merci, 38700 La Tronche, France

Received 11 October 2012; Accepted 30 October 2012

Academic Editors: A. Berdis, A. Kajon, N. Maneekarn, and J. Tozser

Copyright © 2013 Anne-Laure Favier et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Human enteric adenoviruses of species F, HAdV-40 and HAdV-41 (Ad40 and Ad41), are associated with gastroenteritis in children. Ad attachment to the primary receptor on the cell surface is mediated by the distal head domain of the fiber protein, an antenna-like component of the adenovirus capsid. Differently from the majority of human Ads that possess one type of fiber on their capsid, the Ad40 and 41 have two distinct fibers. The long fiber recognizes the host membrane protein CAR, which permits virus attachment, but nothing is known about the role of the short fiber. Using the head domain of the Ad41 short fiber, we fished out a putative membrane protein that has never been previously described. This partner of the short fiber of enteric Ad41 (ParAd41) is a small, hydrophobic protein with three putative trans membrane domains, which interacts with the Ad41 short fiber but not with the Ad41 long fiber or with the fiber of respiratory Ad2 serotype. ParAd41 is localized in intracellular membranes including the nuclear membrane. Saturation of the short fiber with ParAd41 inhibits virus infectivity, which substantiates the putative role of ParAd41 in enteric Ads tropism. It is conceivable that the interaction of the short fiber with ParAd41 mediates virus postattachment endocytosis step as well as interaction with the nuclear membrane prior to the injection of viral DNA into the nucleus, thus enabling enteric adenovirus infection. This study is the first one to probe the molecular nature of enteric Ad41 tropism.