期刊论文详细信息
PLoS One
The Type III Secretion System-Related CPn0809 from Chlamydia pneumoniae
Astrid C. Engel1  Anne Kerres1  Johannes H. Hegemann1  Frauke Herbst1  Jan N. Galle1 
[1] Lehrstuhl für Funktionelle Genomforschung der Mikroorganismen, Heinrich-Heine-Universität, Düsseldorf, Germany
关键词: Chlamydia infection;    Chlamydophila pneumoniae;    Membrane proteins;    Operons;    Chlamydia;    Antibodies;    Plasmid construction;    Secretion systems;   
DOI  :  10.1371/journal.pone.0148509
学科分类:医学(综合)
来源: Public Library of Science
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【 摘 要 】

Chlamydia pneumoniae is an intracellular Gram-negative bacterium that possesses a type III secretion system (T3SS), which enables the pathogen to deliver, in a single step, effector proteins for modulation of host-cell functions into the human host cell cytosol to establish a unique intracellular niche for replication. The translocon proteins located at the top of the T3SS needle filament are essential for its function, as they form pores in the host-cell membrane. Interestingly, unlike other Gram-negative bacteria, C. pneumoniae has two putative translocon operons, named LcrH_1 and LcrH_2. However, little is known about chlamydial translocon proteins. In this study, we analyzed CPn0809, one of the putative hydrophobic translocators encoded by the LcrH_1 operon, and identified an ‘SseC-like family’ domain characteristic of T3S translocators. Using bright-field and confocal microscopy, we found that CPn0809 is associated with EBs during early and very late phases of a C. pneumoniae infection. Furthermore, CPn0809 forms oligomers, and interacts with the T3SS chaperone LcrH_1, via its N-terminal segment. Moreover, expression of full-length CPn0809 in the heterologous host Escherichia coli causes a grave cytotoxic effect that leads to cell death. Taken together, our data indicate that CPn0809 likely represents one of the translocon proteins of the C. pneumoniae T3SS, and possibly plays a role in the translocation of effector proteins in the early stages of infection.

【 授权许可】

CC BY   

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