The Passage of Chaperonins to Extracellular Locations in <i>Legionella pneumophila</i> Requires a Functional Dot/Icm System.

ABSTRACT: HtpB, the chaperonin of the bacterial pathogen L. pneumophila, is found in extracellular locations, even the cytoplasm of host cells. Although chaperonins have an essential cytoplasmic function in protein folding, HtpB exits the cytoplasm to perform extracellular virulence-related functions that support L. pneumophila's lifestyle. The mechanism by which HtpB reaches extracellular locations is not currently understood. To address this experimental gap, immunoelectron microscopy, trypsin-accessibility assays, and cell fractionation were used to localize HtpB in various L. pneumophila secretion mutants. Dot/Icm type IV secretion mutants displayed less surface-exposed HtpB and more periplasmic HtpB than parent strains. The analysis of periplasmic extracts and outer membran

SUBMITTER: Robertson P 

PROVIDER: S-EPMC11763710 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature