Removal of either N-glycan site from the envelope receptor binding domain of Moloney and Friend but not AKV mouse ecotropic gammaretroviruses alters receptor usage

Ryan C. Knoper, John Ferrarone, Yuhe Yan, Bernard A.P. Lafont, Christine A. Kozak

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

Three N-linked glycosylation sites were removed from the envelope glycoproteins of Friend, Moloney, and AKV mouse ecotropic gammaretroviruses: gs1 and gs2, in the receptor binding domain; and gs8, in a region implicated in post-binding cell fusion. Mutants were tested for their ability to infect rodent cells expressing 4 CAT-1 receptor variants. Three mutants (Mo-gs1, Mo-gs2, and Fr-gs1) infect NIH 3T3 and rat XC cells, but are severely restricted in Mus dunni cells and Lec8, a Chinese hamster cell line susceptible to ecotropic virus. This restriction is reproduced in ferret cells expressing M. dunni dCAT-1, but not in cells expressing NIH 3T3 mCAT-1. Virus binding assays, pseudotype assays, and the use of glycosylation inhibitors further suggest that restriction is primarily due to receptor polymorphism and, in M. dunni cells, to glycosylation of cellular proteins. Virus envelope glycan size or type does not affect infectivity. Thus, host range variation due to N-glycan deletion is receptor variant-specific, cell-specific, virus type-specific, and glycan site-specific.

Original languageEnglish (US)
Pages (from-to)232-239
Number of pages8
JournalVirology
Volume391
Issue number2
DOIs
StatePublished - Sep 1 2009

Bibliographical note

Funding Information:
This research was supported by the Intramural Research Program of the NIH, NIAID.

Copyright:
Copyright 2009 Elsevier B.V., All rights reserved.

Keywords

  • CAT-1 retrovirus receptor
  • Gammaretrovirus envelope glycosylation sites
  • Mouse ecotropic gammaretrovirus
  • Retrovirus entry

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