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J. Biol. Chem., Vol. 280, Issue 31, 28265-28271, August 5, 2005
The Use of Calnexin and Calreticulin by Cellular and Viral Glycoproteins*![]() ![]() ![]() ![]() ||
From the
Calnexin and calreticulin are homologous lectin chaperones that assist maturation of cellular and viral glycoproteins in the mammalian endoplasmic reticulum. Calnexin and calreticulin share the same specificity for monoglucosylated protein-bound N-glycans but associate with a distinct set of newly synthesized polypeptides. We report here that most calnexin substrates do not associate with calreticulin even upon selective calnexin inactivation, while BiP associates more abundantly with nascent polypeptides under these conditions. Calreticulin associated more abundantly with orphan calnexin substrates only in infected cells and preferentially with polypeptides of viral origin, showing stronger dependence of model viral glycoproteins on endoplasmic reticulum lectins. This may explain why inactivation of the calnexin cycle affects viral replication and infectivity but not viability of mammalian cells.
Received for publication, January 27, 2005 , and in revised form, June 8, 2005. * The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
|| Supported by grants from the Max Cloetta Foundation, Foundation for Research on Neurodegenerative Diseases, Swiss National Center of Competence in Research on Neural Plasticity and Repair, Swiss National Science Foundation, Telethon, Synapsis Foundation, Bangerter-Rhyner Foundation. To whom correspondence should be addressed: Institute for Research in Biomedicine, CH-6500 Bellinzona, Switzerland. Tel.: 41918200319; Fax: 41918200300; E-mail: maurizio.molinari{at}irb.unisi.ch.
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