Site-saturation mutagenesis of the PALTAVETG motif in coxsackievirus A9 capsid protein VP1 reveals evidence of conservation of a periodic hydrophobicity profile
Author:
Affiliation:
1. National Public Health Institute (KTL), Enterovirus Laboratory, Mannerheimintie 166, FIN-00300 Helsinki, Finland1
2. University of Essex, Department of Biological Sciences, John Tabor Laboratories, Wivenhoe Park, Colchester CO4 3SQ, UK2
Abstract
Publisher
Microbiology Society
Subject
Virology
Reference24 articles.
1. The three-dimensional structure of foot-and-mouth disease virus at 2·9 Å resolution;Acharya;Nature,1989
2. Modified base compositions at degenerate positions of a mutagenic oligonucleotide enhance randomness in site-saturation mutagenesis;Airaksinen;Nucleic Acids Research,1998
3. Analysis of the structure of a common cold virus, human rhinovirus 14, refined at a resolution of 3·0 Å;Arnold;Journal of Molecular Biology,1990
4. The nucleotide sequence of coxsackievirus A9; implications for receptor binding and enterovirus classification;Chang;Journal of General Virology,1989
5. Synthetic peptides from four separate regions of the poliovirus type 1 capsid protein VP1 induce neutralizing antibodies;Chow;Proceedings of the National Academy of Sciences, USA,1985
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2. Phylodynamic Characterization of an Ocular-Tropism Coxsackievirus A24 Variant;PLOS ONE;2016-08-16
3. Recognition of coxsackievirus A by Enterovirus genus-specific immune and molecular markers in experimentally infected suckling mice;Pathologie Biologie;2005-07
4. Coxsackievirus A9 VP1 Mutants with Enhanced or Hindered A Particle Formation and Decreased Infectivity;Journal of Virology;2001-01-15
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