Processing of Chlamydia abortus polymorphic membrane protein 18D during the chlamydial developmental cycle.
Chlamydia possess a unique family of autotransporter proteins known as the Polymorphic membrane proteins (Pmps). While the total number of pmp genes varies between Chlamydia species, all encode a single pmpD gene. In both Chlamydia trachomatis (C. trachomatis) and C. pneumoniae, the PmpD protein is...
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2012-01-01
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doaj-e3e89932d7484df58f14fbd7d50cbdf32020-11-25T00:48:00ZengPublic Library of Science (PLoS)PLoS ONE1932-62032012-01-01711e4919010.1371/journal.pone.0049190Processing of Chlamydia abortus polymorphic membrane protein 18D during the chlamydial developmental cycle.Nick M WheelhouseMichelle SaitKevin AitchisonMorag LivingstoneFrank WrightKevin McLeanNeil F InglisDavid G E SmithDavid LongbottomChlamydia possess a unique family of autotransporter proteins known as the Polymorphic membrane proteins (Pmps). While the total number of pmp genes varies between Chlamydia species, all encode a single pmpD gene. In both Chlamydia trachomatis (C. trachomatis) and C. pneumoniae, the PmpD protein is proteolytically cleaved on the cell surface. The current study was carried out to determine the cleavage patterns of the PmpD protein in the animal pathogen C. abortus (termed Pmp18D).Using antibodies directed against different regions of Pmp18D, proteomic techniques revealed that the mature protein was cleaved on the cell surface, resulting in a100 kDa N-terminal product and a 60 kDa carboxy-terminal protein. The N-terminal protein was further processed into 84, 76 and 73 kDa products. Clustering analysis resolved PmpD proteins into three distinct clades with C. abortus Pmp18D, being most similar to those originating from C. psittaci, C. felis and C. caviae.This study indicates that C. abortus Pmp18D is proteolytically processed at the cell surface similar to the proteins of C. trachomatis and C. pneumoniae. However, patterns of cleavage are species-specific, with low sequence conservation of PmpD across the genus. The absence of conserved domains indicates that the function of the PmpD molecule in chlamydia remains to be elucidated.http://europepmc.org/articles/PMC3493501?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Nick M Wheelhouse Michelle Sait Kevin Aitchison Morag Livingstone Frank Wright Kevin McLean Neil F Inglis David G E Smith David Longbottom |
spellingShingle |
Nick M Wheelhouse Michelle Sait Kevin Aitchison Morag Livingstone Frank Wright Kevin McLean Neil F Inglis David G E Smith David Longbottom Processing of Chlamydia abortus polymorphic membrane protein 18D during the chlamydial developmental cycle. PLoS ONE |
author_facet |
Nick M Wheelhouse Michelle Sait Kevin Aitchison Morag Livingstone Frank Wright Kevin McLean Neil F Inglis David G E Smith David Longbottom |
author_sort |
Nick M Wheelhouse |
title |
Processing of Chlamydia abortus polymorphic membrane protein 18D during the chlamydial developmental cycle. |
title_short |
Processing of Chlamydia abortus polymorphic membrane protein 18D during the chlamydial developmental cycle. |
title_full |
Processing of Chlamydia abortus polymorphic membrane protein 18D during the chlamydial developmental cycle. |
title_fullStr |
Processing of Chlamydia abortus polymorphic membrane protein 18D during the chlamydial developmental cycle. |
title_full_unstemmed |
Processing of Chlamydia abortus polymorphic membrane protein 18D during the chlamydial developmental cycle. |
title_sort |
processing of chlamydia abortus polymorphic membrane protein 18d during the chlamydial developmental cycle. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2012-01-01 |
description |
Chlamydia possess a unique family of autotransporter proteins known as the Polymorphic membrane proteins (Pmps). While the total number of pmp genes varies between Chlamydia species, all encode a single pmpD gene. In both Chlamydia trachomatis (C. trachomatis) and C. pneumoniae, the PmpD protein is proteolytically cleaved on the cell surface. The current study was carried out to determine the cleavage patterns of the PmpD protein in the animal pathogen C. abortus (termed Pmp18D).Using antibodies directed against different regions of Pmp18D, proteomic techniques revealed that the mature protein was cleaved on the cell surface, resulting in a100 kDa N-terminal product and a 60 kDa carboxy-terminal protein. The N-terminal protein was further processed into 84, 76 and 73 kDa products. Clustering analysis resolved PmpD proteins into three distinct clades with C. abortus Pmp18D, being most similar to those originating from C. psittaci, C. felis and C. caviae.This study indicates that C. abortus Pmp18D is proteolytically processed at the cell surface similar to the proteins of C. trachomatis and C. pneumoniae. However, patterns of cleavage are species-specific, with low sequence conservation of PmpD across the genus. The absence of conserved domains indicates that the function of the PmpD molecule in chlamydia remains to be elucidated. |
url |
http://europepmc.org/articles/PMC3493501?pdf=render |
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