title: Intermolecular Interactions of Chrysanthemum virus B Coat Protein: Implications for Capsid Assembly.
abstract: Chrysanthemum virus B coat protein constitutes the viral capsid which, besides other functions, encapsulates and protects the viral nucleic acid. We have demonstrated homotypic interaction of the coat protein subunits, essentially important for dimer formation, which is the first step during capsid assembly in vivo and in vitro. Interaction capacity of full length and truncated protein has been investigated and important regions have been identified through protein-protein interaction in yeast and by co-immunoprecipitation assays. Complete coat protein was found to interact strongly with similar subunits. Constructs with 102 amino acids from the N-terminal and 64 amino acids from C-terminal were found to be inconsequential for dimer formation as they did not show any interaction with similar subunits or with full length protein when analysed for β-galactosidase or histidine prototrophy. Results suggest that the region of 98-184 amino acids from the middle plays an important role in the process, probably without the involvement of N- and C- terminals.
authors: Plant Virology Lab, Institute of Himalayan Bioresource Technology, Palampur, Himachal Pradesh 176061 India.
authors: Lakhmir
authors: L
authors: Singh
authors: Vipin
authors: V
authors: Hallan
authors: Aijaz A
authors: AA
authors: Zaidi
keywords: Capsid; Chrysanthemum virus B; Dimer; Protein–protein
references: Virology. 1996 Apr 1;218(1):43-51
references: 8615040
references: Nucleic Acids Res. 1981 Jun 25;9(12):2741-52
references: 7279660
references: Genome Biol. 2000;1(5):REVIEWS3002
references: 11178263
references: J Gen Virol. 1994 Sep;75 ( Pt 9):2509-12
references: 8077955
references: Virology. 2000 Mar 1;268(1):29-40
references: 10683324
references: Curr Genet. 1989 Dec;16(5-6):339-46
references: 2692852
references: Arch Virol. 2001;146(9):1765-73
references: 11699961
references: J Bacteriol. 1983 Jan;153(1):163-8
references: 6336730
references: Virology. 1999 Jul 20;260(1):182-9
references: 10405370
references: Trends Biotechnol. 1998 Feb;16(2):61-5
references: 9487732
references: Proc Natl Acad Sci U S A. 1999 Jan 5;96(1):55-60
references: 9874771
references: J Gen Virol. 1991 Jan;72 ( Pt 1):9-14
references: 1990070
references: Virology. 1996 Aug 15;222(2):383-90
references: 8806522
references: Virology. 1975 Mar;64(1):86-95
references: 234655
references: Arch Virol. 2007 Feb;152(2):405-13
references: 17006596
references: J Gen Virol. 1991 Jan;72 ( Pt 1):1-7
references: 1990057
references: J Gen Virol. 1990 Aug;71 ( Pt 8):1877-80
references: 2391504
references: Nucleic Acids Res. 1992 Mar 25;20(6):1425
references: 1561104
references: Nucleic Acids Res. 1991 Oct 25;19(20):5791
references: 1945859
references: Genetics. 1996 Dec;144(4):1425-36
references: 8978031
references: Nature. 1989 Jul 20;340(6230):245-6
references: 2547163
references: Acta Virol. 1998 Nov;42(5):347-51
references: 10358737
references: J Virol. 1992 Aug;66(8):5157-60
references: 1629970
references: Cell. 1993 Nov 19;75(4):805-16
references: 8242751
references: Virology. 1995 Mar 10;207(2):486-94
references: 7886952
references: Virus Genes. 1992 Jan;6(1):47-52
references: 1312755
references: Virology. 1996 Aug 15;222(2):339-51
references: 8806518