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J Biomed Sci. 2008 Nov;15(6):707-17. doi: 10.1007/s11373-008-9278-3. Epub 2008 Sep 16.

Interactions between M protein and other structural proteins of severe, acute respiratory syndrome-associated coronavirus.

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Graduate Institute of Molecular and Cellular Biology, Tzu Chi University, 701, Section 3, Chung Yang Road, Hualien, Taiwan.


Severe acute respiratory syndrome-associated coronavirus (SARS-CoV) structural proteins (S, E, M, and NC) localize in different subcellular positions when expressed individually. However, SARS-CoV M protein is co-localized almost entirely with S, E, or NC protein when co-expressed in the cells. On the other hand, only partial co-localization was observed when S and E, S and NC, or E and NC were co-expressed in the cells. Interactions between SARS-CoV M and other structural proteins but not interactions between S and E, S and NC, or E and NC were further demonstrated by co-immunoprecipitation assay. These results indicate that SARS-CoV M protein, similar to the M proteins of other coronaviruses, plays a pivotal role in virus assembly. The cytoplasmic C-terminus domain of SARS-CoV M protein was responsible for binding to NC protein. Multiple regions of M protein interacted with E and S proteins. A model for the interactions between SARS-CoV M protein and other structural proteins is proposed. This study helps us better understand protein-protein interactions during viral assembly of SARS-CoV.

[Indexed for MEDLINE]

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