Interactions between Coat and Scaffolding Proteins of Phage P22 Are Alteredin Vitroby Amino Acid Substitutions in Coat Protein That Cause a Cold-Sensitive Phenotype†

Biochemistry ◽  
1996 ◽  
Vol 35 (47) ◽  
pp. 14831-14840 ◽  
Author(s):  
Carolyn M. Teschke ◽  
Derek G. Fong
Keyword(s):  
Amino Acid ◽  
Coat Protein ◽  
Amino Acid Substitutions ◽  
Scaffolding Proteins ◽  
Phage P22 ◽  
Cold Sensitive

Kazakh strains of tobacco mosaic virus: two strains with potentially destabilizing amino acid substitutions in the coat protein

2000 ◽  
Vol 56 (2) ◽  
pp. 71-77 ◽  
Author(s):  
VICTOR K. NOVIKOV ◽  
EKATERINA V. BELENOVICH ◽  
EVGENY N. DOBROV ◽  
SERGEI K. ZAVRIEV
Keyword(s):  
Amino Acid ◽  
Coat Protein ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Amino Acid Substitutions

Role of Entropic Interactions in Viral Capsids: Single Amino Acid Substitutions in P22 Bacteriophage Coat Protein Resulting in Loss of Capsid Stability

Biochemistry ◽  
1995 ◽  
Vol 34 (4) ◽  
pp. 1120-1126 ◽  
Author(s):  
Debora Foguel ◽  
Carolyn M. Teschke ◽  
Peter E. Jr. Prevelige ◽  
Jerson L. Silva
Keyword(s):  
Amino Acid ◽  
Coat Protein ◽  
Single Amino Acid ◽  
Amino Acid Substitutions ◽  
Viral Capsids ◽  
Capsid Stability

scholarly journals Host and phi X 174 mutations affecting the morphogenesis or stabilization of the 50S complex, a single-stranded DNA synthesizing intermediate.

Genetics ◽  
1995 ◽  
Vol 140 (4) ◽  
pp. 1167-1174
Author(s):  
M C Ekechukwu ◽  
D J Oberste ◽  
B A Fane
Keyword(s):  
Amino Acid ◽  
Coat Protein ◽  
Protein A ◽  
Amino Acid Substitutions ◽  
Preinitiation Complex ◽  
Viral Coat Protein ◽  
Single Stranded Dna ◽  
Rep Protein ◽  
Viral Coat ◽  
Axis Of Symmetry

Abstract The morphogenetic pathway of bacteriophage phi X 174 was investigated in rep mutant hosts that specifically block stage III single-stranded DNA synthesis. The defects conferred by the mutant rep protein most likely affect the formation or stabilization of the 50S complex, a single-stranded DNA synthesizing intermediate, which consists of a viral prohead and a DNA replicating intermediate (preinitiation complex). phi X 174 mutants, ogr (rep), which restore the ability to propagate in the mutant rep hosts, were isolated. The org (rep) mutations confer amino acid substitutions in the viral coat protein, a constituent of the prohead, and the viral A protein, a constituent of the preinitiation complex. Four of the six coat protein substitutions are localized on or near the twofold axis of symmetry in the atomic structure of the mature virion.

scholarly journals Two Amino Acid Substitutions in the Coat Protein of Pepper mild mottle virus Are Responsible for Overcoming the L4 Gene-Mediated Resistance in Capsicum spp.

2007 ◽  
Vol 97 (7) ◽  
pp. 787-793 ◽  
Author(s):  
Yoshikatsu Genda ◽  
Ayami Kanda ◽  
Hiroyuki Hamada ◽  
Kyoko Sato ◽  
Jun Ohnishi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Coat Protein ◽  
Resistance Gene ◽  
Site Directed Mutagenesis ◽  
Mottle Virus ◽  
Amino Acid Substitutions ◽  
Pepper Mild Mottle Virus ◽  
Biological Assays ◽  
Capsicum Spp ◽  
Capsicum Chacoense

The Capsicum spp. L genes (L1 to L4) confer resistance to tobamoviruses. Currently, the L4 gene from Capsicum chacoense is the most effective resistance gene and has been used widely in breeding programs in Japan which have developed new resistant cultivars against Pepper mild mottle virus (PMMoV). However, in 2004, mild mosaic symptoms began appearing on the leaves of commercial pepper plants in the field which possessed the L4 resistance gene. Serological and biological assays on Capsicum spp. identified the causal virus strain as a previously unreported pathotype, P1,2,3,4. PMMoV sequence analysis of the virus and site-directed mutagenesis using a PMMoV-J of the P1,2 pathotype revealed that two amino acid substitutions in the coat protein, Gln to Arg at position 46 and Gly to Lys at position 85, were responsible for overcoming the L4 resistance gene.

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