scholarly journals Characteristics of gene encoding coat protein isolated from soybean mosaic virus

2014 ◽  
Vol 36 (1se) ◽  
Author(s):  
Lo Thi Mai Thu ◽  
Hoang Ha ◽  
Le Van Son ◽  
Chu Hoang Ha ◽  
Chu Hoang Mau
Keyword(s):  
Coat Protein ◽  
Mosaic Virus ◽  
Soybean Mosaic Virus ◽  
Gene Encoding

Transformation of Wheat With the Gene Encoding the Coat Protein of Barley Yellow Mosaic Virus

1996 ◽  
Vol 23 (4) ◽  
pp. 429 ◽  
Author(s):  
S Karunaratne ◽  
A Sohn ◽  
A Mouradov ◽  
J Scott ◽  
HH Steinbiss ◽  
...  
Keyword(s):  
Gene Expression ◽  
Coat Protein ◽  
Mosaic Virus ◽  
Yellow Mosaic Virus ◽  
Bar Gene ◽  
Gene Encoding ◽  
Barley Yellow Mosaic Virus ◽  
Virus Coat Protein ◽  
Wheat Embryos ◽  
Virus Coat

Wheat plants (Triticum aestivum cv. Hartog) were stably transformed with the bar gene and the gene encoding the barley yellow mosaic virus coat protein. Cultured immature wheat embryos were bombarded with tungsten particles coated with the pEmuPAT-cp construct. Fifteen regenerating 'PPT- resistant' plants were selected on medium containing phosphinothricin. Of these, 11 plants had both the bar and cp genes integrated into the wheat genome and two plants had only the bar gene. Transmission of the two genes to progeny of two independent plants was confirmed. The barley yellow mosaic virus coat protein was detected in both the parent and progeny plants; however, bar gene expression occurred only in the parent plants.

scholarly journals Coat Protein Gene-Mediated Resistance to Soybean Mosaic Virus in Transgenic Soybean

2006 ◽  
Vol 56 (2) ◽  
pp. 119-124 ◽  
Author(s):  
Noriyuki Furutani ◽  
Soh Hidaka ◽  
Yoshitaka Kosaka ◽  
Yoshiaki Shizukawa ◽  
Seiji Kanematsu
Keyword(s):  
Coat Protein ◽  
Mosaic Virus ◽  
Coat Protein Gene ◽  
Protein Gene ◽  
Soybean Mosaic Virus ◽  
Transgenic Soybean

A DnaJ protein that interacts with soybean mosaic virus coat protein serves as a key susceptibility factor for viral infection

2020 ◽  
Vol 281 ◽  
pp. 197870 ◽  
Author(s):  
Tingxuan Zong ◽  
Jinlong Yin ◽  
Tongtong Jin ◽  
Liqun Wang ◽  
Minxuan Luo ◽  
...  
Keyword(s):  
Coat Protein ◽  
Viral Infection ◽  
Mosaic Virus ◽  
Soybean Mosaic Virus ◽  
Susceptibility Factor ◽  
Dnaj Protein ◽  
Virus Coat Protein ◽  
Virus Coat

scholarly journals Importance of the C-terminal domain of soybean mosaic virus coat protein for subunit interactions

2006 ◽  
Vol 87 (1) ◽  
pp. 225-229 ◽  
Author(s):  
Sung-Hwan Kang ◽  
Won-Seok Lim ◽  
Sung-Hyun Hwang ◽  
Jin-Woo Park ◽  
Hong-Soo Choi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Coat Protein ◽  
Mosaic Virus ◽  
Virus Assembly ◽  
Soybean Mosaic Virus ◽  
Cell Movement ◽  
Aphid Transmission ◽  
Terminal Region ◽  
Virus Coat ◽  
Two Hybrid

The potyvirus coat protein (CP) is involved in aphid transmission, cell-to-cell movement and virus assembly, not only by binding to viral RNA, but also by self-interaction or interactions with other factors. In this study, a number of CP mutants of Soybean mosaic virus (SMV) containing deletions and site-directed mutations were generated and cloned into yeast two-hybrid vectors. Interaction was confirmed by the expression of reporter genes, including HIS3, ADE2 and MEL1, in yeast strain AH109. Deletion of the C-terminal region of the CP caused loss of the CP–CP self-interaction ability detected in CP mutants with the C-terminal region. Alanine substitution at the amino acid positions R190, E191, E212, R245, H246 and R249 disrupted CP–CP interaction, whereas substitutions at the amino acid positions R188, D189, D198, K205, K218 and D250 did not. These results indicate that the C-terminal region of SMV CP may contain a domain(s) or amino acids required for CP–CP interaction and virus assembly.

scholarly journals The charged residues in the surface-exposed C-terminus of the Soybean mosaic virus coat protein are critical for cell-to-cell movement

Virology ◽  
2013 ◽  
Vol 446 (1-2) ◽  
pp. 95-101 ◽  
Author(s):  
Jang-Kyun Seo ◽  
Mi Sa Vo Phan ◽  
Sung-Hwan Kang ◽  
Hong-Soo Choi ◽  
Kook-Hyung Kim
Keyword(s):  
Coat Protein ◽  
Mosaic Virus ◽  
Soybean Mosaic Virus ◽  
Cell Movement ◽  
Virus Coat Protein ◽  
C Terminus ◽  
Charged Residues ◽  
Virus Coat

scholarly journals Expression and purification of recombinant coat protein of sugarcane mosaic virus from Indonesian isolate as an antigen for antibody production

2019 ◽  
Vol 24 (1) ◽  
pp. 57
Author(s):  
Natalia Tri Astuti ◽  
Nurmalasari Darsono ◽  
Suvia Widyaningrum ◽  
Widhi Dyah Sawitri ◽  
Sri Puji Astuti ◽  
...  
Keyword(s):  
Coat Protein ◽  
Mosaic Virus ◽  
Polyclonal Antibodies ◽  
Molecular Study ◽  
Insoluble Fraction ◽  
Sugarcane Mosaic Virus ◽  
Gene Encoding ◽  
Iptg Induction ◽  
Sds Page ◽  
Saccharum Sp

Sugarcane mosaic virus (SCMV, genus Potyvirus, family Potyviridae) is a prominent pathogen of sugarcane (Saccharum sp. hybrids). It can cause losses in susceptible varieties, in crop as well as sugar production, economically. Although it has been studied in major sugar-producing countries, research on the definement of SCMV from Indonesian isolates based on molecular study has been very limited. This study aimed to obtain a proper recombinant antigens emanating from coat protein of SCMV from Indonesian isolate in order to produce polyclonal antibodies that cann be used for immunodiagnosis assays in a subsequent study. A gene-encoding coat protein of SCMV (CP-SCMV) was amplified using RT-PCR and cloned into vector pJET1.2. The cDNA was inserted into 6X His-tag expression plasmid of pET28a(+) and over-expressed in Escherichia coli BL21(DE3) to produce a recombinant protein. The highest expression was found in 0.1M IPTG induction media for 5 h at 37oC. SDS-PAGE analysis clarified that the recombinant CP-SCMV remained as an insoluble fraction. Purifications was carried out by the affinity Ni-NTA resin, followed by electroelution to obtain a highly purified protein. To meet the quality requirements of a proper antigen, the highly purified protein was concentrated. A molecular weight of the rCP-SCMV (approximately 40 kDa) was clearly observed by 10% SDS-PAGE at the concentration of 16.184 mg/mL. 

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