Gopinath, K and Sundareshan, S and Bhuvaneswari, M and Karande, A and Murthy, MRN and Nayudu, MV and Savithri, HS (1994) Primary structure of sesbania mosaic virus coat protein: its implications to the assembly and architecture of the virus. In: Indian Journal of Biochemistry & Biophysics, 31 (4). 322-328 .Full text not available from this repository.
Sesbania mosaic virus (SMV) is a plant virus that infects Sesbania grandiflora plants in Andhra Pradesh, India. The amino acid sequence of the coat protein of SMV was determined using purified peptides generated by cleavage with trypsin, chymotrypsin, V8 protease and clostripain. The 230 residues so far determined were compared to the corresponding residues of southern bean mosaic virus (SBMV), the type member of sobemoviruses. The overall identity between the sequences is 61.7%. The amino terminal 64 residues, which constitute an independent domain (R-domain) known to interact with RNA, are conserved to a lower extent (52.5%). Comparison of the positively charged residues in this domain suggests that the RNA-protein interactions are considerably weaker in SMV. The residues that constitute the major domain of the coat protein, the surface domain (S-domain, residues 65-260), are better conserved (66.5%). The positively charged residues of this domain that face the nucleic acid are well conserved. The longest conserved stretch of residues (131-142) corresponds to the loop involved in intersubunit interactions between subunits related by the quasi 3-fold symmetry. A unique cation binding site located on the quasi 3-fold axis contributes to the stability of SMV. These differences are reflected in the increased stability of the SMV coat protein and its ability to be reconstituted with RNA at pH 7.5. A major epitope was identified using monoclonal antibodies to SMV in the segment 201-223 which contains an exposed helix in the capsid structure. This region is highly conserved between SMV and SBMV (70%) suggesting that it could represent the site of an important function such as vector recognition.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to National institute of science communication and information resources.|
|Department/Centre:||Division of Biological Sciences > Biochemistry
Division of Biological Sciences > Molecular Biophysics Unit
|Date Deposited:||11 Apr 2011 04:37|
|Last Modified:||11 Apr 2011 04:37|
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