Role for chlamydial inclusion membrane proteins in inclusion membrane structure and biogenesis.
The chlamydial inclusion membrane is extensively modified by the insertion of type III secreted effector proteins. These inclusion membrane proteins (Incs) are exposed to the cytosol and share a common structural feature of a long, bi-lobed hydrophobic domain but little or no primary amino acid sequ...
Main Authors: | , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2013-01-01
|
Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC3656976?pdf=render |
id |
doaj-9a10e1aa58e64b0b9b26acd94693321b |
---|---|
record_format |
Article |
spelling |
doaj-9a10e1aa58e64b0b9b26acd94693321b2020-11-25T01:55:54ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0185e6342610.1371/journal.pone.0063426Role for chlamydial inclusion membrane proteins in inclusion membrane structure and biogenesis.Jeffrey MitalNatalie J MillerDavid W DorwardCheryl A DooleyTed HackstadtThe chlamydial inclusion membrane is extensively modified by the insertion of type III secreted effector proteins. These inclusion membrane proteins (Incs) are exposed to the cytosol and share a common structural feature of a long, bi-lobed hydrophobic domain but little or no primary amino acid sequence similarity. Based upon secondary structural predictions, over 50 putative inclusion membrane proteins have been identified in Chlamydia trachomatis. Only a limited number of biological functions have been defined and these are not shared between chlamydial species. Here we have ectopically expressed several C. trachomatis Incs in HeLa cells and find that they induce the formation of morphologically distinct membranous vesicular compartments. Formation of these vesicles requires the bi-lobed hydrophobic domain as a minimum. No markers for various cellular organelles were observed in association with these vesicles. Lipid probes were incorporated by the Inc-induced vesicles although the lipids incorporated were dependent upon the specific Inc expressed. Co-expression of Inc pairs indicated that some colocalized in the same vesicle, others partially overlapped, and others did not associate at all. Overall, it appears that Incs may have an intrinsic ability to induce membrane formation and that individual Incs can induce membranous structures with unique properties.http://europepmc.org/articles/PMC3656976?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Jeffrey Mital Natalie J Miller David W Dorward Cheryl A Dooley Ted Hackstadt |
spellingShingle |
Jeffrey Mital Natalie J Miller David W Dorward Cheryl A Dooley Ted Hackstadt Role for chlamydial inclusion membrane proteins in inclusion membrane structure and biogenesis. PLoS ONE |
author_facet |
Jeffrey Mital Natalie J Miller David W Dorward Cheryl A Dooley Ted Hackstadt |
author_sort |
Jeffrey Mital |
title |
Role for chlamydial inclusion membrane proteins in inclusion membrane structure and biogenesis. |
title_short |
Role for chlamydial inclusion membrane proteins in inclusion membrane structure and biogenesis. |
title_full |
Role for chlamydial inclusion membrane proteins in inclusion membrane structure and biogenesis. |
title_fullStr |
Role for chlamydial inclusion membrane proteins in inclusion membrane structure and biogenesis. |
title_full_unstemmed |
Role for chlamydial inclusion membrane proteins in inclusion membrane structure and biogenesis. |
title_sort |
role for chlamydial inclusion membrane proteins in inclusion membrane structure and biogenesis. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2013-01-01 |
description |
The chlamydial inclusion membrane is extensively modified by the insertion of type III secreted effector proteins. These inclusion membrane proteins (Incs) are exposed to the cytosol and share a common structural feature of a long, bi-lobed hydrophobic domain but little or no primary amino acid sequence similarity. Based upon secondary structural predictions, over 50 putative inclusion membrane proteins have been identified in Chlamydia trachomatis. Only a limited number of biological functions have been defined and these are not shared between chlamydial species. Here we have ectopically expressed several C. trachomatis Incs in HeLa cells and find that they induce the formation of morphologically distinct membranous vesicular compartments. Formation of these vesicles requires the bi-lobed hydrophobic domain as a minimum. No markers for various cellular organelles were observed in association with these vesicles. Lipid probes were incorporated by the Inc-induced vesicles although the lipids incorporated were dependent upon the specific Inc expressed. Co-expression of Inc pairs indicated that some colocalized in the same vesicle, others partially overlapped, and others did not associate at all. Overall, it appears that Incs may have an intrinsic ability to induce membrane formation and that individual Incs can induce membranous structures with unique properties. |
url |
http://europepmc.org/articles/PMC3656976?pdf=render |
work_keys_str_mv |
AT jeffreymital roleforchlamydialinclusionmembraneproteinsininclusionmembranestructureandbiogenesis AT nataliejmiller roleforchlamydialinclusionmembraneproteinsininclusionmembranestructureandbiogenesis AT davidwdorward roleforchlamydialinclusionmembraneproteinsininclusionmembranestructureandbiogenesis AT cheryladooley roleforchlamydialinclusionmembraneproteinsininclusionmembranestructureandbiogenesis AT tedhackstadt roleforchlamydialinclusionmembraneproteinsininclusionmembranestructureandbiogenesis |
_version_ |
1724982685619716096 |