Structural and functional analysis of the Francisella lysine decarboxylase as a key actor in oxidative stress resistance.

ABSTRACT: Francisella tularensis is one of the most virulent pathogenic bacteria causing the acute human respiratory disease tularemia. While the mechanisms underlying F. tularensis pathogenesis are largely unknown, previous studies have shown that a F. novicida transposon mutant with insertions in a gene coding for a putative lysine decarboxylase was attenuated in mouse spleen, suggesting a possible role of its protein product as a virulence factor. Therefore, we set out to structurally and functionally characterize the F. novicida lysine decarboxylase, which we termed LdcF. Here, we investigate the genetic environment of ldcF as well as its evolutionary relationships with other basic AAT-fold amino acid decarboxylase superfamily members, known as key actors in bacterial adaptative stress response

SUBMITTER: Felix J 

PROVIDER: S-EPMC7806604 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature