dc.contributor.author | He, R | |
dc.contributor.author | Leeson, A | |
dc.contributor.author | Ballantine, M | |
dc.contributor.author | Andonov, A | |
dc.contributor.author | Baker, L | |
dc.contributor.author | Dobie, F | |
dc.contributor.author | Li, Y | |
dc.contributor.author | Bastien, N | |
dc.contributor.author | Feldmann, H | |
dc.contributor.author | Strocher, U | |
dc.contributor.author | Theriault, S | |
dc.contributor.author | Cutts, T | |
dc.contributor.author | Cao, J | |
dc.contributor.author | Booth, TF | |
dc.contributor.author | Plummer, FA | |
dc.contributor.author | Tyler, S | |
dc.contributor.author | Li, X. | |
dc.date.accessioned | 2013-06-28T15:16:57Z | |
dc.date.available | 2013-06-28T15:16:57Z | |
dc.date.issued | 2004-10 | |
dc.identifier.citation | Virus Res. 2004 Oct;105(2):121-5. | en |
dc.identifier.uri | http://hinari-gw.who.int/whalecomwww.ncbi.nlm.nih.gov/whalecom0/pubmed/15351485 | |
dc.identifier.uri | http://erepository.uonbi.ac.ke:8080/xmlui/handle/123456789/41994 | |
dc.description.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. | en |
dc.language.iso | en | en |
dc.publisher | University of Nairobi | en |
dc.title | Characterization Of Protein-protein Interactions Between The Nucleocapsid Protein And Membrane Protein Of The Sars Coronavirus. | en |
dc.type | Article | en |
local.publisher | Department of Medical Microbiology | en |