A single amino acid substitution in the capsid protein VP1 of Coxsackievirus B3 (CVB3) alters plaque phenotype in Vero cells but not cardiovirulence in a mouse model

1995 ◽  
Vol 140 (5) ◽  
pp. 959-966 ◽  
Author(s):  
H. Zhang ◽  
N. W. Blake ◽  
X. Ouyang ◽  
Y. A. Pandolfino ◽  
P. Morgan-Capner ◽  
...  
Keyword(s):  
Amino Acid ◽  
Mouse Model ◽  
Capsid Protein ◽  
Amino Acid Substitution ◽  
Vero Cells ◽  
Coxsackievirus B3 ◽  
Single Amino Acid Substitution ◽  
Single Amino Acid ◽  
Plaque Phenotype ◽  
Capsid Protein Vp1

scholarly journals Site-saturation mutagenesis of the PALTAVETG motif in coxsackievirus A9 capsid protein VP1 reveals evidence of conservation of a periodic hydrophobicity profile

1999 ◽  
Vol 80 (8) ◽  
pp. 1919-1927 ◽  
Author(s):  
Antero Airaksinen ◽  
Merja Roivainen ◽  
Glyn Stanway ◽  
Tapani Hovi
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Capsid Protein ◽  
Amino Acid Substitution ◽  
Saturation Mutagenesis ◽  
Single Amino Acid ◽  
Site Saturation ◽  
Coxsackievirus A9 ◽  
Capsid Protein Vp1 ◽  
Hydrophobicity Profile

Enteroviruses possess a highly conserved 9 amino acid stretch of mainly hydrophobic character in the capsid protein VP1. A novel strategy, combining site-saturation mutagenesis and a single-tube cloning and transfection procedure, has been developed for the analysis of this motif in coxsackievirus A9 (CAV-9). Four individual amino acids were separately mutated. Mutagenesis of three of the four positions in CAV-9 resulted in a number of viable but impaired mutant strains, each containing a single amino acid substitution. In contrast, no mutants with amino acid substitutions at leucine 31 were isolated, although three different leucine codons were found among the viruses recovered. Small plaque size was regularly associated with reduced yields of infectious virus and an amino acid substitution at the target site in the viruses isolated from the site-saturated virus pools. From the range of amino acids observed in viable mutants, it was possible to estimate the characteristics that are required at individual amino acid positions. It seems that in the motif studied here, a periodic hydrophobicity profile needs to be conserved. The constraints observed on the ranges of acceptable amino acids presumably reflect the structural–functional requirements that have resulted in the conservation of the motif.

scholarly journals A large compressibility change of protein induced by a single amino acid substitution

1996 ◽  
Vol 5 (3) ◽  
pp. 542-545 ◽  
Author(s):  
Kunihiko Gekko ◽  
Youjiro Tamura ◽  
Eiji Ohmae ◽  
Hideyuki Hayashi ◽  
Hiroyuki Kagamiyama ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Single Amino Acid Substitution ◽  
Single Amino Acid
Sign in / Sign up

Export Citation Format

Share Document