Zika virus M protein latches and locks the E protein from transitioning to an immature state after prM cleavage.

ABSTRACT: During flavivirus maturation, the structural proteins prM (pre-membrane) and E (envelope) undergo extensive low pH-mediated conformational changes, transitioning from spiky trimeric to smooth dimeric prM/E heterodimers which allow for furin cleavage of prM into pr and M and forms the irreversible mature conformation of smooth M/E heterodimers. The mechanisms of irreversible conformational changes to E protein following the pr cleavage are not understood. Utilizing cryo-EM structures of immature virus and structure-based mutagenesis of Zika virus, we identified two critical "latching and locking" interactions mediated by M protein residues Arg38 and Trp19, respectively, that stabilize the E protein structure in the smooth mature stage. M protein thus latches and locks the E protein in an ir

SUBMITTER: Majowicz SA 

PROVIDER: S-EPMC11721464 | biostudies-literature | 2023 Nov

REPOSITORIES: biostudies-literature