Please use this identifier to cite or link to this item: https://doi.org/10.1021/bi062057p
Title: The 3a accessory protein of SARS coronavirus specifically interacts with the 5′UTR of its genomic RNA, using a unique 75 amino acid interaction domain
Authors: Sharma, K.
Surjit, M.
Satija, N.
Liu, B. 
Chow, V.T.K. 
Lai, S.K.
Issue Date: 5-Jun-2007
Citation: Sharma, K., Surjit, M., Satija, N., Liu, B., Chow, V.T.K., Lai, S.K. (2007-06-05). The 3a accessory protein of SARS coronavirus specifically interacts with the 5′UTR of its genomic RNA, using a unique 75 amino acid interaction domain. Biochemistry 46 (22) : 6488-6499. ScholarBank@NUS Repository. https://doi.org/10.1021/bi062057p
Abstract: More than four years have passed since the outbreak of the severe acute respiratory syndrome (SARS) epidemic, and still very little is known about the molecular biology and pathogenesis of this deadly virus. Among the accessory proteins of the SARS Coronavirus (SARS-CoV), the 3a protein has been shown to interact with the spike, envelope, and membrane glycoprotein and has recently been established to be a structural component of capsid. Recent studies suggest that the 3a protein may function as an ion channel and may promote virus release. In order to further characterize the functional properties of this protein, we initiated studies to check its RNA binding activity. Using the yeast three-hybrid system, electrophoretic mobility shift assay (EMSA), and ultraviolet (UV) cross-linking techniques, we have shown that the 3a protein is capable of binding specifically to the 5′ untranslated region (5′UTR) of the SARS virus genomic RNA. Further, we have mapped the interaction domain of the 3a protein responsible for this RNA - protein interaction using a series of deletion mutants and defined it to the central 75 amino acid region. This RNA binding motif of 3a does not share homology with any other known RNA binding protein and may have an important role in viral capsid assembly and pathogenesis. © 2007 American Chemical Society.
Source Title: Biochemistry
URI: http://scholarbank.nus.edu.sg/handle/10635/107625
ISSN: 00062960
DOI: 10.1021/bi062057p
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

12
checked on Sep 19, 2018

WEB OF SCIENCETM
Citations

10
checked on Sep 19, 2018

Page view(s)

33
checked on Sep 21, 2018

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.