Open AccessIdentification and characterization of a novel Chlamydia trachomatis reticulate body protein
Author(s) -
Shaw Allan C.,
Larsen Martin R.,
Roepstorff Peter,
Christiansen Gunna,
Birkelund Svend
Publication year - 2002
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2002.tb11266.x
Subject(s) - chlamydia trachomatis , biology , proteome , open reading frame , ankyrin repeat , proteomics , obligate , intracellular parasite , genome , chlamydiales , gene , genetics , peptide sequence , virology , ecology
The genome of the obligate intracellular bacterium Chlamydia trachomatis comprises 894 genes predicted by computer‐based analysis. As part of a large‐scale proteome analysis of C. trachomatis , a small abundant protein encoded by a previously unrecognized novel 204‐bp open reading frame was identified by tandem mass spectrometry. No homology of this protein was observed to proteins from other organisms. The protein was conserved in C. trachomatis but not found in Chlamydia pneumoniae . Using proteomics, we show that the expression of the protein is initiated at the middle of the developmental cycle. The protein is rapidly degraded and is only present in reticulate or intermediate bodies, suggesting a possible function in the intracellular stage of C. trachomatis development. We have termed the protein ‘7‐kDa reticulate body protein’.