role of inter-subunit ionic interactions in the assembly of Physalis mottle tymovirus
Physalis mottle tymovirus (PhMV) is a small spherical plant virus with its RNA genome encapsidated in a protein shell made of 180 identical coat protein (CP) subunits. The amino acid residues involved in two interfacial salt bridges, Asp-83/Arg-159 and Arg-68/Asp-150 and Lys-153, were targeted for m...
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| Veröffentlicht in: | Archives of virology 2006-10, Vol.151 (10), p.1917-1931 |
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| creator | Umashankar, M Murthy, M. R. N Singh, S. A Appu Rao, A. G Savithri, H. S |
| description | Physalis mottle tymovirus (PhMV) is a small spherical plant virus with its RNA genome encapsidated in a protein shell made of 180 identical coat protein (CP) subunits. The amino acid residues involved in two interfacial salt bridges, Asp-83/Arg-159 and Arg-68/Asp-150 and Lys-153, were targeted for mutagenesis with a view to delineate the role of interfacial ionic interactions in the subunit folding and assembly of the virus. R159A and D83A-R159A recombinant CP (rCP) mutants formed stable T = 3 capsids, indicating that the D83-R159 interfacial salt bridge is dispensable for the folding and assembly of PhMV. However, D150A and R68Q-D150A mutant rCPs were present in the insoluble fraction, suggesting that the R68-D150 interfacial salt bridge is crucial for subunit folding and assembly. Similarly, K153Q, D83A-K153Q, and H69A-K153Q mutant rCPs were present in the insoluble fraction. Interestingly, the R68Q-D150A, D83A-K153Q, and H69A-K153Q double mutant rCPs could be refolded into partially folded soluble heterogeneous aggregates of 14-16 S. The results further confirm our earlier observation that subunit folding and assembly are concerted events in PhMV. |
| doi_str_mv | 10.1007/s00705-006-0783-2 |
| format | Article |
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Similarly, K153Q, D83A-K153Q, and H69A-K153Q mutant rCPs were present in the insoluble fraction. Interestingly, the R68Q-D150A, D83A-K153Q, and H69A-K153Q double mutant rCPs could be refolded into partially folded soluble heterogeneous aggregates of 14-16 S. The results further confirm our earlier observation that subunit folding and assembly are concerted events in PhMV.</description><identifier>ISSN: 0304-8608</identifier><identifier>EISSN: 1432-8798</identifier><identifier>DOI: 10.1007/s00705-006-0783-2</identifier><identifier>PMID: 16732495</identifier><language>eng</language><publisher>Wien: Vienna : Springer-Verlag</publisher><subject>Biological and medical sciences ; Capsid Proteins - chemistry ; Capsid Proteins - genetics ; Capsid Proteins - metabolism ; Capsid Proteins - physiology ; DNA polymerase ; E coli ; Fundamental and applied biological sciences. 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R. N</creatorcontrib><creatorcontrib>Singh, S. A</creatorcontrib><creatorcontrib>Appu Rao, A. G</creatorcontrib><creatorcontrib>Savithri, H. S</creatorcontrib><title>role of inter-subunit ionic interactions in the assembly of Physalis mottle tymovirus</title><title>Archives of virology</title><addtitle>Arch Virol</addtitle><description>Physalis mottle tymovirus (PhMV) is a small spherical plant virus with its RNA genome encapsidated in a protein shell made of 180 identical coat protein (CP) subunits. The amino acid residues involved in two interfacial salt bridges, Asp-83/Arg-159 and Arg-68/Asp-150 and Lys-153, were targeted for mutagenesis with a view to delineate the role of interfacial ionic interactions in the subunit folding and assembly of the virus. R159A and D83A-R159A recombinant CP (rCP) mutants formed stable T = 3 capsids, indicating that the D83-R159 interfacial salt bridge is dispensable for the folding and assembly of PhMV. 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R. N</au><au>Singh, S. A</au><au>Appu Rao, A. G</au><au>Savithri, H. S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>role of inter-subunit ionic interactions in the assembly of Physalis mottle tymovirus</atitle><jtitle>Archives of virology</jtitle><addtitle>Arch Virol</addtitle><date>2006-10-01</date><risdate>2006</risdate><volume>151</volume><issue>10</issue><spage>1917</spage><epage>1931</epage><pages>1917-1931</pages><issn>0304-8608</issn><eissn>1432-8798</eissn><abstract>Physalis mottle tymovirus (PhMV) is a small spherical plant virus with its RNA genome encapsidated in a protein shell made of 180 identical coat protein (CP) subunits. The amino acid residues involved in two interfacial salt bridges, Asp-83/Arg-159 and Arg-68/Asp-150 and Lys-153, were targeted for mutagenesis with a view to delineate the role of interfacial ionic interactions in the subunit folding and assembly of the virus. R159A and D83A-R159A recombinant CP (rCP) mutants formed stable T = 3 capsids, indicating that the D83-R159 interfacial salt bridge is dispensable for the folding and assembly of PhMV. However, D150A and R68Q-D150A mutant rCPs were present in the insoluble fraction, suggesting that the R68-D150 interfacial salt bridge is crucial for subunit folding and assembly. Similarly, K153Q, D83A-K153Q, and H69A-K153Q mutant rCPs were present in the insoluble fraction. Interestingly, the R68Q-D150A, D83A-K153Q, and H69A-K153Q double mutant rCPs could be refolded into partially folded soluble heterogeneous aggregates of 14-16 S. The results further confirm our earlier observation that subunit folding and assembly are concerted events in PhMV.</abstract><cop>Wien</cop><cop>New York, NY</cop><pub>Vienna : Springer-Verlag</pub><pmid>16732495</pmid><doi>10.1007/s00705-006-0783-2</doi><tpages>15</tpages></addata></record> |
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| subjects | Biological and medical sciences Capsid Proteins - chemistry Capsid Proteins - genetics Capsid Proteins - metabolism Capsid Proteins - physiology DNA polymerase E coli Fundamental and applied biological sciences. Psychology Genomes Ions - metabolism Microbiology Miscellaneous Models, Molecular Mutagenesis Mutagenesis, Site-Directed Physalis Physalis - virology Physalis mottle tymovirus Protein Folding Protein Subunits - chemistry Protein Subunits - metabolism Protein Subunits - physiology Proteins Recombinant Proteins - genetics Recombinant Proteins - metabolism Tymovirus Tymovirus - chemistry Tymovirus - physiology Virology Virus Assembly Viruses |
| title | role of inter-subunit ionic interactions in the assembly of Physalis mottle tymovirus |
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