A single tyrosine in the severe acute respiratory syndrome coronavirus membrane protein cytoplasmic tail is important for efficient interaction with spike protein

Corrin E. McBride, Carolyn E. Machamer

Research output: Contribution to journalArticle

Abstract

Severe acute respiratory syndrome coronavirus (SARS-CoV) encodes 3 major envelope proteins: spike (S), membrane (M), and envelope (E). Previous work identified a dibasic endoplasmic reticulum retrieval signal in the cytoplasmic tail of SARS-CoV S that promotes efficient interaction with SARS-CoV M. The dibasic signal was shown to be important for concentrating S near the virus assembly site rather than for direct interaction with M. Here, we investigated the sequence requirements of the SARS-CoV M protein that are necessary for interaction with SARS-CoV S. The SARS-CoV M tail was shown to be necessary for S localization in the Golgi region when the proteins were exogenously coexpressed in cells. This was specific, since SARS-CoV M did not retain an unrelated glycoprotein in the Golgi. Importantly, we found that an essential tyrosine residue in the SARS-CoV M cytoplasmic tail, Y195, was important for S-M interaction. When Y195 was mutated to alanine, MY195A no longer retained S intracellularly at the Golgi. Unlike wild-type M, M Y195A did not reduce the amount of SARS-CoV S carbohydrate processing or surface levels when the two proteins were coexpressed. Mutating Y 195 also disrupted SARS-CoV S-M interaction in vitro. These results suggest that Y195 is necessary for efficient SARS-CoV S-M interaction and, thus, has a significant involvement in assembly of infectious virus.

Original languageEnglish (US)
Pages (from-to)1891-1901
Number of pages11
JournalJournal of virology
Volume84
Issue number4
DOIs
StatePublished - Feb 1 2010

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

Fingerprint Dive into the research topics of 'A single tyrosine in the severe acute respiratory syndrome coronavirus membrane protein cytoplasmic tail is important for efficient interaction with spike protein'. Together they form a unique fingerprint.

  • Cite this