scholarly journals Assembly of Sesbania mosaic virus: Role of the coat protein N-terminal R domain

2014 ◽  
Vol 70 (a1) ◽  
pp. C1820-C1820
Author(s):  
Ashutosh Gulati ◽  
H.S. Savithri ◽  
M.R.N Murthy
Keyword(s):  
Coat Protein ◽  
Mosaic Virus ◽  
Protein A ◽  
Dimensional Structure ◽  
Globular Domain ◽  
Coat Proteins ◽  
Divalent Metal Ions ◽  
Intrinsically Disordered ◽  
R Domain

Coat proteins of several isometric viruses consist of two domains, a disordered N-terminal R-domain consisting of several positively charged residues and a shell (S) domain characterized by a jelly roll β-barrel structure. The three-dimensional structure of Sesbania mosaic virus (SeMV), a T=3 plant virus, has been determined at 3 Å resolution. The full length coat protein, when expressed in E. coli, assembles into T=3 icosahedral shells (VLPs) resembling native virus particles. In the present investigations, the role of N-terminal R domain in the assembly of VLPs was explored by replacing the R domain with a presumably globular domain (SeMV-P10) and other intrinsically disordered (SeMV-P8, and SeMV-VPg) SeMV encoded domains. The R domain was also replaced with the non-viral globular B-domain of Staphyloccocus aureus protein A. These domains were of nearly the same size as that of the R-domain. Most of the chimeric coat proteins, when expressed in E.coli, formed VLPs, which could be purified by ultra-centrifugation. The purified VLPs were examined by transmission electron microscopy (TEM), which suggested that a fraction of the expressed proteins could assemble into T=3 VLPs, although often, the particles were heterogeneous. Interestingly, the SeMV NΔ65B CP could also be purified by Ni-NTA chromatography as a dimer which assembled into T=1 VLPs under crystallization conditions. The structure of NΔ65B-CP VLPs revealed that the assembled particles were devoid of divalent metal ions at the canonical site and there was no density corresponding to the B domain. However, the S domain could be superimposed on that of SeMV NΔ65VLPs determined earlier. The other VLPs- SeMVNΔ65P10 CP, SeMVNΔ65P8 CP and SeMVNΔ65VPg could not be crystallized because of their heterogeneity. These studies suggest a subtle interplay between the length, sequence and structure of the R-domain polypeptide and the assembly of particles.

Role of alfalfa mosaic virus coat protein gene in symptom formation

Virology ◽  
1991 ◽  
Vol 181 (2) ◽  
pp. 687-693 ◽  
Author(s):  
Lyda Neeleman ◽  
Antoinette C. Van Der Kuyl ◽  
John F. Bol
Keyword(s):  
Coat Protein ◽  
Mosaic Virus ◽  
Coat Protein Gene ◽  
Protein Gene ◽  
Alfalfa Mosaic Virus ◽  
Virus Coat Protein ◽  
Virus Coat ◽  
Symptom Formation

Role of Hexahistidine in Directed Nanoassemblies of Tobacco Mosaic Virus Coat Protein

ACS Nano ◽  
2011 ◽  
Vol 5 (3) ◽  
pp. 1606-1616 ◽  
Author(s):  
Michael A. Bruckman ◽  
Carissa M. Soto ◽  
Heather McDowell ◽  
Jinny L. Liu ◽  
Banahalli R. Ratna ◽  
...  
Keyword(s):  
Coat Protein ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Virus Coat Protein ◽  
Virus Coat

scholarly journals Role of Recombination in the Evolution of Host Specialization Within Bean yellow mosaic virus

2009 ◽  
Vol 99 (5) ◽  
pp. 512-518 ◽  
Author(s):  
S. J. Wylie ◽  
R. A. C. Jones
Keyword(s):  
Coat Protein ◽  
Mosaic Virus ◽  
Genetic Recombination ◽  
Bean Yellow Mosaic Virus ◽  
Host Specialization ◽  
Yellow Mosaic Virus ◽  
Complete Genomes ◽  
Tentative Evidence ◽  
Firm Evidence

Seven complete genomes and 64 coat protein gene sequences belonging to Bean yellow mosaic virus (BYMV) isolates from different continents were examined for evidence of genetic recombination using six different recombination-detection programs. In the seven complete genomes and a single complete genome of the related virus Clover yellow vein virus (ClYVV), evidence for eight recombination patterns was found by four or more programs, giving firm evidence of their presence, and five additional recombination patterns were detected by three or fewer programs, giving tentative evidence of their occurrence. When the nucleotide sequences of 64 BYMV and one ClYVV coat protein genes were analyzed, three firm recombination patterns were detected in 21 isolates (32%). With another six isolates (9%), tentative evidence was found for three further recombination patterns. Of the 19 firm or tentative recombination patterns detected within and between strain groups of BYMV, and with ClYVV, 12 involved a generalist group of isolates as a parent but none of the other BYMV groups acted as parents more than six times. These findings suggest that recombination played an important role in the evolution of BYMV strain groups that specialize in infecting particular groups of domesticated plants.

scholarly journals Characterization of a New Potyvirus Naturally Infecting Chickpea

Plant Disease ◽  
2003 ◽  
Vol 87 (11) ◽  
pp. 1366-1371 ◽  
Author(s):  
Richard C. Larsen ◽  
Walter J. Kaiser ◽  
Stephen D. Wyatt ◽  
Keri L. Buxton-Druffel ◽  
Phillip H. Berger
Keyword(s):  
Coat Protein ◽  
Mosaic Virus ◽  
Yellow Mosaic Virus ◽  
Plum Pox Virus ◽  
Cdna Clones ◽  
Coat Proteins ◽  
Serological Reaction ◽  
Protein Amino Acid ◽  
Western Blots ◽  
Putative Coat Protein

During the 1999 to 2001 growing seasons, symptoms consisting of mosaic, stunting, yellowing, wilting, shortening of internodes, and phloem discoloration were observed in chickpea (Cicer arietinum) grown in the Department of Chuquisaca in southern Bolivia. In some fields, approximately 10% of the plants exhibited viruslike symptoms and suffered greatly reduced seed yields. Lentil (Lens culinaris) was also observed to be infected but not pea (Pisum sativum) or faba bean (Vicia faba) growing in nearby fields. Infected chickpea tissue reacted positively to the potyvirus group-specific monoclonal antibody (MAb), but there was no serological reaction with antisera to the potyviruses Bean yellow mosaic virus, Clover yellow vein virus, Cowpea aphid-borne mosaic virus, Pea seedborne mosaic virus, Bean common mosaic virus, or Bean common mosaic necrosis virus. Western blots of total protein extracts probed with the potyvirus MAb revealed a single band ca. 32 kDa. Comparative sequence analysis of cDNA clones generated from the putative coat protein gene consisted of 282 amino acids (31.9 kDa) and showed moderate identities of 67, 66, 63, 63, and 61% with the coat proteins of potyviruses Pepper severe mosaic virus, Pepper yellow mosaic virus, Potato virus Y, Plum pox virus, and Pepper mottle virus, respectively. Phylogenetic analysis of the coat protein amino acid sequence revealed that this virus is a unique member of the family Potyviridae and is phylogenetically most closely related to a group of Solanaceae-infecting potyviruses rather than to other legumeinfecting potyviruses. The proposed name for the new causal agent is Chickpea yellow mosaic virus.

scholarly journals Coat–protein–mediated resistance to tobacco mosaic virus: discovery mechanisms and exploitation

1999 ◽  
Vol 354 (1383) ◽  
pp. 659-664 ◽  
Author(s):  
Roger N. Beachy
Keyword(s):  
Coat Protein ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Structural Basis ◽  
Challenge Virus ◽  
Transgenic Cell ◽  
Coat Protein Mediated Resistance ◽  
Local Cell

In 1986 we reported that transgenic plants which accumulate the coat protein of tobacco mosaic virus (TMV) are protected from infection by TMV, and by closely related tobamoviruses. The phenomenon is referred to as coat–protein–mediated resistance (CP–MR), and bears certain similarities to cross protection, a phenomenon described by plant pathologists early in this century. Our studies of CP–MR against TMV have demonstrated that transgenically expressed CP interferes with disassembly of TMV particles in the inoculated transgenic cell. However, there is little resistance to local, cell–to–cell spread of infection. CP–MR involves interaction between the transgenic CP and the CP of the challenge virus, and resistance to TMV is greater than to tobamoviruses that have CP genes more distantly related to the transgene. Using the known coordinates of the three–dimensional structure of TMV we developed mutant forms of CP that have stronger inter–subunit interactions, and confer increased levels of CP–MR compared with wild–type CP. Similarly, it is predicted that understanding the cellular and structural basis of CP–MR will lead to the development of variant CP transgenes that each can confer high levels of resistance against a range of tobamoviruses.

scholarly journals The Role of the Coat Protein A-Domain in P22 Bacteriophage Maturation

Viruses ◽  
2014 ◽  
Vol 6 (7) ◽  
pp. 2708-2722 ◽  
Author(s):  
David Morris ◽  
Peter Prevelige
Keyword(s):  
Coat Protein ◽  
Protein A

scholarly journals Genetic diversity analysis of the coat protein gene revealed strong evolutionary constraints on Ornithogalum mosaic virus

2017 ◽  
Author(s):  
Fangluan Gao ◽  
Zhenguo Du ◽  
Jianguo Shen ◽  
Hongkai Yang ◽  
Furong Liao
Keyword(s):  
Coat Protein ◽  
Mosaic Virus ◽  
Molecular Mechanisms ◽  
Protein Gene ◽  
Purifying Selection ◽  
Evolutionary Constraints ◽  
Diversity Analysis ◽  
Molecular Variance ◽  
Genetic Diversity Analysis

Ornithogalum mosaic virus (OrMV) has a wide host range and affects the production of a variety of ornamentals. In this study, the coat protein (CP) gene of OrMVwas used to investigate the molecular mechanisms underlying the evolution of this virus. The 36 OrMV isolates fell into two groups which have a significant subpopulation differentiation with an FST value of 0.470. One isolate was identified as a recombinant and the other 35 recombination-free isolates could be divided into two major clades under different evolutionary constraints with ω-values of 0.055 and 0.028, respectively, indicating a role of purifying selection in the differentiation of OrMV. In addition, the results from molecular variance of analysis (AMOVA) indicated that the effect of host species on the genetic divergence of OrMV is greater than that of geography. In BaTS analysis, OrMV isolates from the genera Ornithogalum, Lachenalia, Diuri tended to group together, indicating that OrMV diversification was maintained, in part, by host-driven adaptation. Furthermore, age calculations suggested that the first divergence event of the OrMV isolates analyzed might take place around 1068 BC.

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