The C-terminal coiled-coil domain of Corynebacterium diphtheriae DIP0733 is crucial for interaction with epithelial cells and pathogenicity in invertebrate animal model systems.

ABSTRACT:

Background

Corynebacterium diphtheriae is the etiologic agent of diphtheria and different systemic infections. The bacterium has been classically described as an extracellular pathogen. However, a number of studies revealed its ability to invade epithelial cells, indicating a more complex pathogen-host interaction. The molecular mechanisms controlling and facilitating internalization of C. diphtheriae still remains unclear. Recently, the DIP0733 transmembrane protein was found to play an important role in the interaction with matrix proteins and cell surfaces, nematode colonization, cellular internalization and induction of cell death.

Results

In this study, we identified a number of short linear motifs and structural elements of DIP0733 with putative importance in virulence

SUBMITTER: Weerasekera D 

PROVIDER: S-EPMC6123952 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature