TY - JOUR
T1 - Structure and intracellular targeting of the SARS-coronavirus orf7a accessory protein
AU - Nelson, Christopher A.
AU - Pekosz, Andrew
AU - Lee, Chung A.
AU - Diamond, Michael S.
AU - Fremont, Daved H.
N1 - Funding Information:
We thank Drs. Stuart Kornfeld, Linton Traub, Kenneth Murphy, Marcel Fremont, and Skip Virgin for comments on the manuscript. We also thank Dr. Vincent Magrini of the Washington University School of Medicine Genome Sequencing Center for the ORF 7a cDNA clone 79A01. The National Institutes of Health Grants GM62414-04 (D.H.F.) and R21AI059328 (A.P., M.S.D., and D.H.F.) supported this work.
PY - 2005/1
Y1 - 2005/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=11844281552&partnerID=8YFLogxK
U2 - 10.1016/j.str.2004.10.010
DO - 10.1016/j.str.2004.10.010
M3 - Article
C2 - 15642263
AN - SCOPUS:11844281552
SN - 0969-2126
VL - 13
SP - 75
EP - 85
JO - Structure
JF - Structure
IS - 1
ER -