title: Characterization of protein-protein interactions between the nucleocapsid protein and membrane protein of the SARS coronavirus.
abstract: The human coronavirus, associated with severe acute respiratory syndrome (SARS-CoV), was identified and molecularly characterized in 2003. Sequence analysis of the virus indicates that there is only 20% amino acid (aa) identity with known coronaviruses. Previous studies indicate that protein-protein interactions amongst various coronavirus proteins are critical for viral assembly. Yet, little sequence homology between the newly identified SARS-CoV and those previously studied coronaviruses suggests that determination of protein-protein interaction and identification of amino acid sequences, responsible for such interaction in SARS-CoV, are necessary for the elucidation of the molecular mechanism of SARS-CoV replication and rationalization of anti-SARS therapeutic intervention. In this study, we employed mammalian two-hybrid system to investigate possible interactions between SARS-CoV nucleocapsid (N) and the membrane (M) proteins. We found that interaction of the N and M proteins takes place in vivo and identified that a stretch of amino acids (168-208) in the N protein may be critical for such protein-protein interactions. Importantly, the same region has been found to be required for multimerization of the N protein (He et al., 2004) suggesting this region may be crucial in maintaining correct conformation of the N protein for self-interaction and interaction with the M protein.
authors.affiliation: National Microbiology Laboratory, Health Canada, 1015 Arlington St., Winnipeg, Man., Canada R3E 3R2. runtao_he@hc-sc.gc.ca
authors.forename: Runtao
authors.initials: R
authors.lastname: He
authors.forename: Andrew
authors.initials: A
authors.lastname: Leeson
authors.forename: Melissa
authors.initials: M
authors.lastname: Ballantine
authors.forename: Anton
authors.initials: A
authors.lastname: Andonov
authors.forename: Lindsay
authors.initials: L
authors.lastname: Baker
authors.forename: Frederick
authors.initials: F
authors.lastname: Dobie
authors.forename: Yan
authors.initials: Y
authors.lastname: Li
authors.forename: Nathalie
authors.initials: N
authors.lastname: Bastien
authors.forename: Heinz
authors.initials: H
authors.lastname: Feldmann
authors.forename: Ute
authors.initials: U
authors.lastname: Strocher
authors.forename: Steven
authors.initials: S
authors.lastname: Theriault
authors.forename: Todd
authors.initials: T
authors.lastname: Cutts
authors.forename: Jingxin
authors.initials: J
authors.lastname: Cao
authors.forename: Timothy F
authors.initials: TF
authors.lastname: Booth
authors.forename: Frank A
authors.initials: FA
authors.lastname: Plummer
authors.forename: Shaun
authors.initials: S
authors.lastname: Tyler
authors.forename: Xuguang
authors.initials: X
authors.lastname: Li
mesh_terms: D001665:Binding Sites; D000086862:Coronavirus M Proteins; D000086462:Coronavirus Nucleocapsid Proteins; D019590:Nucleocapsid Proteins / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D025941:Protein Interaction Mapping; D045473:Severe acute respiratory syndrome-related coronavirus / Q000378:metabolism* / Q000502:physiology; D017384:Sequence Deletion; D020798:Two-Hybrid System Techniques; D014763:Viral Matrix Proteins / Q000378:metabolism*; D014764:Viral Proteins / Q000378:metabolism; D019065:Virus Assembly
chemical_list: D000086862:Coronavirus M Proteins; D000086462:Coronavirus Nucleocapsid Proteins; C000706237:M protein, SARS-CoV; D019590:Nucleocapsid Proteins; D014763:Viral Matrix Proteins; D014764:Viral Proteins