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Chlamydia trachomatis has penicillin-binding proteins but not detectable muramic acid

1982; American Society for Microbiology; Volume: 151; Issue: 1 Linguagem: Inglês

10.1128/jb.151.1.420-428.1982

1098-5530

Alan G. Barbour, Ken‐ichi Amano, Ted Hackstadt, L Perry, Harlan D. Caldwell,

Clostridium difficile and Clostridium perfringens research

Chlamydia trachomatis LGV-434 was grown in HeLa 229 cells. Benzylpenicillin completely inhibited the formation of infectious elementary bodies (EBs) at a concentration of 19 pmol/ml or higher and produced abnormally large reticulate bodies (RBs) in the inclusions at 30 pmol/ml or higher. The possible targets for penicillin in C. trachomatis were three penicillin-binding proteins (PBPs) which were identified in the Sarkosyl-soluble fractions of both RBs and EBs. The apparent subunit molecular weights were 88,000 (PBP 1), 61,000 (BPB 2), and 36,000 (PBP 3). The 50% binding concentrations of [3H]penicillin for PBPs 1 to 3 in EBs and RBs were between 7 and 70 pmol/ml. Such high susceptibility to penicillin was shown by an organism that did not have detectable muramic acid (less than 0.02% by weight) in preparations of either whole cells or sodium dodecyl sulfate-insoluble residues.