Open AccessOuter membrane complex proteins of Chlamydia pneumoniae
Author(s) -
Melgosa Mercedes Perez,
Kuo Chochou,
Ann Campbell Lee
Publication year - 1993
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.1574-6968.1993.tb06448.x
Subject(s) - chlamydophila pneumoniae , chlamydia , bacterial outer membrane , chlamydiaceae , cysteine , methionine , microbiology and biotechnology , immune system , biology , antibody , chlamydiales , membrane protein , klebsiella pneumoniae , amino acid , chemistry , biochemistry , gene , membrane , escherichia coli , immunology , enzyme
The protein composition of the outer membrane complex (OMC) of Chlamydia pneumoniae strain AR‐39 was analyzed by metabolic labeling with [ 35 S]methionine and [ 35 S]cysteine. Cysteine‐rich proteins with molecular masses of 98, 60 doublet, 39.5 (MOMP) and 15.5 kDa were found in the OMC of C. pneumoniae . The cysteine‐rich proteins of the OMCs of the threee Chlamydia species showed specific reaction patterns by immunoassay and autoradiography to rabbit or turkey immune sera. Recognition of the MOMP and 60‐kDa proteins of the three species was cross‐reactive. However, the C. pneumoniae 98‐kDa protein was recognized by anti‐ C. pneumoniae (AR‐39) and anti‐ C. psittaci (TT3) immune sera. None of the immunee sera recognized the 12‐kDa cysteine‐rich complex.