Helices alpha2 and alpha3 of West Nile virus capsid protein are dispensable for assembly of infectious virions.

ABSTRACT: The internal hydrophobic sequence within the flaviviral capsid protein (protein C) plays an important role in the assembly of infectious virions. Here, this sequence was analyzed in a West Nile virus lineage I isolate (crow V76/1). An infectious cDNA clone was constructed and used to introduce deletions into the internal hydrophobic domain which comprises helix alpha2 and part of the loop intervening helices alpha2 and alpha3. In total, nine capsid deletion mutants (4 to 14 amino acids long) were constructed and tested for virus viability. Some of the short deletions did not significantly affect growth in cell culture, whereas larger deletions removing almost the entire hydrophobic region significantly impaired viral growth. Efficient growth of the majority of mutants could, however, be re

SUBMITTER: Schlick P 

PROVIDER: S-EPMC2681950 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature