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

National Public Health Institute (KTL), Enterovirus Laboratory, Mannerheimintie 166, FIN-00300 Helsinki, Finland¹
University of Essex, Department of Biological Sciences, John Tabor Laboratories, Wivenhoe Park, Colchester CO4 3SQ, UK²

Author for correspondence: Antero Airaksinen.Fax +358 9 4744 8355. e-mail antero.airaksinen{at}ktl.fi

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.

This article has been cited by other articles:

				A. Airaksinen, M. Roivainen, and T. Hovi Coxsackievirus A9 VP1 Mutants with Enhanced or Hindered A Particle Formation and Decreased Infectivity J. Virol., January 15, 2001; 75(2): 952 - 960. [Abstract] [Full Text]