The Type III Secretion System-Related CPn0809 from Chlamydia pneumoniae.
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 ni...
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doaj-0953a5bc24d1454caef073e24b97bc0f2020-11-25T01:50:35ZengPublic Library of Science (PLoS)PLoS ONE1932-62032016-01-01112e014850910.1371/journal.pone.0148509The Type III Secretion System-Related CPn0809 from Chlamydia pneumoniae.Astrid C EngelFrauke HerbstAnne KerresJan N GalleJohannes H HegemannChlamydia 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.http://europepmc.org/articles/PMC4760673?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Astrid C Engel Frauke Herbst Anne Kerres Jan N Galle Johannes H Hegemann |
spellingShingle |
Astrid C Engel Frauke Herbst Anne Kerres Jan N Galle Johannes H Hegemann The Type III Secretion System-Related CPn0809 from Chlamydia pneumoniae. PLoS ONE |
author_facet |
Astrid C Engel Frauke Herbst Anne Kerres Jan N Galle Johannes H Hegemann |
author_sort |
Astrid C Engel |
title |
The Type III Secretion System-Related CPn0809 from Chlamydia pneumoniae. |
title_short |
The Type III Secretion System-Related CPn0809 from Chlamydia pneumoniae. |
title_full |
The Type III Secretion System-Related CPn0809 from Chlamydia pneumoniae. |
title_fullStr |
The Type III Secretion System-Related CPn0809 from Chlamydia pneumoniae. |
title_full_unstemmed |
The Type III Secretion System-Related CPn0809 from Chlamydia pneumoniae. |
title_sort |
type iii secretion system-related cpn0809 from chlamydia pneumoniae. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2016-01-01 |
description |
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. |
url |
http://europepmc.org/articles/PMC4760673?pdf=render |
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