Structural characterization of Treponema pallidum Tp0225 reveals an unexpected leucine-rich repeat architecture.

ABSTRACT: The phylogenetically divergent spirochete bacterium Treponema pallidum subsp. pallidum is the causative agent of syphilis. Central to the capacity of T. pallidum to establish infection is the ability of the pathogen to attach to a diversity of host cells. Many pathogenic bacteria employ leucine-rich repeat (LRR) domain-containing proteins to mediate protein-protein interactions, including attachment to host components and establishment of infection. Intriguingly, T. pallidum expresses only one putative LRR domain-containing protein (Tp0225) with an unknown function. In an effort to ascribe a function to Tp0225, a comprehensive phylogenetic analysis was first performed; this investigation revealed that Tp0225 clusters with the pathogenic clade of treponemes. Its crystal structure was then d

SUBMITTER: Ramaswamy R 

PROVIDER: S-EPMC6613448 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature