Cargando…

The expression, processing and localization of polymorphic membrane proteins in Chlamydia pneumoniae strain CWL029

BACKGROUND: Chlamydiae are obligate intracellular bacteria, which are important human pathogens. Genome sequences of C. trachomatis and C. pneumoniae have revealed the presence of a Chlamydia specific gene family encoding polymorphic outer membrane proteins, Pmps. In C. pneumoniae the family compris...

Descripción completa

Detalles Bibliográficos
Autores principales: Vandahl, Brian Berg, Pedersen, Anna Sofie, Gevaert, Kris, Holm, Arne, Vandekerckhove, Joël, Christiansen, Gunna, Birkelund, Svend
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2002
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC140015/
https://www.ncbi.nlm.nih.gov/pubmed/12453305
http://dx.doi.org/10.1186/1471-2180-2-36
_version_ 1782120588027887616
author Vandahl, Brian Berg
Pedersen, Anna Sofie
Gevaert, Kris
Holm, Arne
Vandekerckhove, Joël
Christiansen, Gunna
Birkelund, Svend
author_facet Vandahl, Brian Berg
Pedersen, Anna Sofie
Gevaert, Kris
Holm, Arne
Vandekerckhove, Joël
Christiansen, Gunna
Birkelund, Svend
author_sort Vandahl, Brian Berg
collection PubMed
description BACKGROUND: Chlamydiae are obligate intracellular bacteria, which are important human pathogens. Genome sequences of C. trachomatis and C. pneumoniae have revealed the presence of a Chlamydia specific gene family encoding polymorphic outer membrane proteins, Pmps. In C. pneumoniae the family comprises twenty-one members, which are all transcribed. In the present study, the expression, processing and localisation of the sixteen full-length Pmps in C. pneumoniae strain CWL029 have been further investigated by two-dimensional gel electrophoresis and immunofluorescence microscopy. RESULTS: Ten Pmps were identified in elementary bodies (EBs). Eight of these were investigated with respect to time dependent expression and all were found to be up-regulated between 36 and 48 hours post infection. Antibodies against Pmp6, 8, 10, 11 and 21 reacted with chlamydiae when infected cells were formalin fixed. Pmp6, Pmp20 and Pmp21 were found in cleaved forms, and the cleavage sites of Pmp6 and Pmp21 were identified. CONCLUSIONS: The Pmps are heavily up-regulated at the time of conversion of RB to EB, and at least ten Pmps are present in EBs. Due to their reaction in formalin fixation it is likely that Pmp6, 8, 10, 11 and 21 are surface exposed. The identified cleavage sites of Pmp6 and Pmp21 are in agreement with the theory that the Pmps are autotransporters.
format Text
id pubmed-140015
institution National Center for Biotechnology Information
language English
publishDate 2002
publisher BioMed Central
record_format MEDLINE/PubMed
spelling pubmed-1400152003-01-17 The expression, processing and localization of polymorphic membrane proteins in Chlamydia pneumoniae strain CWL029 Vandahl, Brian Berg Pedersen, Anna Sofie Gevaert, Kris Holm, Arne Vandekerckhove, Joël Christiansen, Gunna Birkelund, Svend BMC Microbiol Research Article BACKGROUND: Chlamydiae are obligate intracellular bacteria, which are important human pathogens. Genome sequences of C. trachomatis and C. pneumoniae have revealed the presence of a Chlamydia specific gene family encoding polymorphic outer membrane proteins, Pmps. In C. pneumoniae the family comprises twenty-one members, which are all transcribed. In the present study, the expression, processing and localisation of the sixteen full-length Pmps in C. pneumoniae strain CWL029 have been further investigated by two-dimensional gel electrophoresis and immunofluorescence microscopy. RESULTS: Ten Pmps were identified in elementary bodies (EBs). Eight of these were investigated with respect to time dependent expression and all were found to be up-regulated between 36 and 48 hours post infection. Antibodies against Pmp6, 8, 10, 11 and 21 reacted with chlamydiae when infected cells were formalin fixed. Pmp6, Pmp20 and Pmp21 were found in cleaved forms, and the cleavage sites of Pmp6 and Pmp21 were identified. CONCLUSIONS: The Pmps are heavily up-regulated at the time of conversion of RB to EB, and at least ten Pmps are present in EBs. Due to their reaction in formalin fixation it is likely that Pmp6, 8, 10, 11 and 21 are surface exposed. The identified cleavage sites of Pmp6 and Pmp21 are in agreement with the theory that the Pmps are autotransporters. BioMed Central 2002-11-26 /pmc/articles/PMC140015/ /pubmed/12453305 http://dx.doi.org/10.1186/1471-2180-2-36 Text en Copyright © 2002 Vandahl et al; licensee BioMed Central Ltd. This is an Open Access article: verbatim copying and redistribution of this article are permitted in all media for any purpose, provided this notice is preserved along with the article's original URL.
spellingShingle Research Article
Vandahl, Brian Berg
Pedersen, Anna Sofie
Gevaert, Kris
Holm, Arne
Vandekerckhove, Joël
Christiansen, Gunna
Birkelund, Svend
The expression, processing and localization of polymorphic membrane proteins in Chlamydia pneumoniae strain CWL029
title The expression, processing and localization of polymorphic membrane proteins in Chlamydia pneumoniae strain CWL029
title_full The expression, processing and localization of polymorphic membrane proteins in Chlamydia pneumoniae strain CWL029
title_fullStr The expression, processing and localization of polymorphic membrane proteins in Chlamydia pneumoniae strain CWL029
title_full_unstemmed The expression, processing and localization of polymorphic membrane proteins in Chlamydia pneumoniae strain CWL029
title_short The expression, processing and localization of polymorphic membrane proteins in Chlamydia pneumoniae strain CWL029
title_sort expression, processing and localization of polymorphic membrane proteins in chlamydia pneumoniae strain cwl029
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC140015/
https://www.ncbi.nlm.nih.gov/pubmed/12453305
http://dx.doi.org/10.1186/1471-2180-2-36
work_keys_str_mv AT vandahlbrianberg theexpressionprocessingandlocalizationofpolymorphicmembraneproteinsinchlamydiapneumoniaestraincwl029
AT pedersenannasofie theexpressionprocessingandlocalizationofpolymorphicmembraneproteinsinchlamydiapneumoniaestraincwl029
AT gevaertkris theexpressionprocessingandlocalizationofpolymorphicmembraneproteinsinchlamydiapneumoniaestraincwl029
AT holmarne theexpressionprocessingandlocalizationofpolymorphicmembraneproteinsinchlamydiapneumoniaestraincwl029
AT vandekerckhovejoel theexpressionprocessingandlocalizationofpolymorphicmembraneproteinsinchlamydiapneumoniaestraincwl029
AT christiansengunna theexpressionprocessingandlocalizationofpolymorphicmembraneproteinsinchlamydiapneumoniaestraincwl029
AT birkelundsvend theexpressionprocessingandlocalizationofpolymorphicmembraneproteinsinchlamydiapneumoniaestraincwl029
AT vandahlbrianberg expressionprocessingandlocalizationofpolymorphicmembraneproteinsinchlamydiapneumoniaestraincwl029
AT pedersenannasofie expressionprocessingandlocalizationofpolymorphicmembraneproteinsinchlamydiapneumoniaestraincwl029
AT gevaertkris expressionprocessingandlocalizationofpolymorphicmembraneproteinsinchlamydiapneumoniaestraincwl029
AT holmarne expressionprocessingandlocalizationofpolymorphicmembraneproteinsinchlamydiapneumoniaestraincwl029
AT vandekerckhovejoel expressionprocessingandlocalizationofpolymorphicmembraneproteinsinchlamydiapneumoniaestraincwl029
AT christiansengunna expressionprocessingandlocalizationofpolymorphicmembraneproteinsinchlamydiapneumoniaestraincwl029
AT birkelundsvend expressionprocessingandlocalizationofpolymorphicmembraneproteinsinchlamydiapneumoniaestraincwl029