Spontaneous mutations restore the viability of tick-borne encephalitis virus mutants with large deletions in protein C.

ABSTRACT: The capsid protein, C, of tick-borne encephalitis virus has recently been found to tolerate deletions up to a length of 16 amino acid residues that partially removed the central hydrophobic domain, a sequence element conserved among flaviviruses which may be crucial for virion assembly. In this study, mutants with deletion lengths of 19, 21, 27, or 30 residues, removing more or all of this hydrophobic domain, were found to yield viable virus progeny, but this was without exception accompanied by the emergence of additional mutations within protein C. These point mutations or sequence duplications were located downstream of the engineered deletion and generally increased the hydrophobicity, suggesting that they may compensate for the loss of the central hydrophobic domain. Two of the second

SUBMITTER: Kofler RM 

PROVIDER: S-EPMC140642 | biostudies-literature | 2003 Jan

REPOSITORIES: biostudies-literature