Structure and intracellular targeting of the SARS-coronavirus orf7a accessory protein

Christopher A. Nelson, Andrew Pekosz, Chung A. Lee, Michael S. Diamond, Daved H. Fremont

Research output: Contribution to journalArticlepeer-review

Abstract

The open reading frame (ORF) 7a of the SARS-associated coronavirus (SARS-CoV) encodes a unique type I transmembrane protein of unknown function. We have determined the 1.8 Å resolution crystal structure of the N-terminal ectodomain of orf7a, revealing a compact seven-stranded β sandwich unexpectedly similar in fold and topology to members of the Ig superfamily. We also demonstrate that, in SARS-CoV- infected cells, the orf7a protein is expressed and retained intracellularly. Confocal microscopy studies using orf7a and orf7a/CD4 chimeras implicate the short cytoplasmic tail and transmembrane domain in trafficking of the protein within the endoplasmic reticulum and Golgi network. Taken together, our findings provide a structural and cellular framework in which to explore the role of orf7a in SARS-CoV pathogenesis.

Original languageEnglish (US)
Pages (from-to)75-85
Number of pages11
JournalStructure
Volume13
Issue number1
DOIs
StatePublished - Jan 2005
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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