Mapping of functional elements in the stem-anchor region of tick-borne encephalitis virus envelope protein E.

ABSTRACT: Envelope protein E of the flavivirus tick-borne encephalitis virus mediates membrane fusion, and the structure of the N-terminal 80% of this 496-amino-acid-long protein has been shown to differ significantly from that of other viral fusion proteins. The structure of the carboxy-terminal 20%, the stem-anchor region, is not known. It contains sequences that are important for membrane anchoring, interactions with prM (the precursor of membrane protein M) during virion assembly, and low-pH-induced structural changes associated with the fusion process. To identify specific functional elements in this region, a series of C-terminal deletion mutants were constructed and the properties of the resulting truncated recombinant E proteins were examined. Full-length E proteins and proteins lacking the

SUBMITTER: Allison SL 

PROVIDER: S-EPMC112618 | biostudies-literature | 1999 Jul

REPOSITORIES: biostudies-literature