CHARACTERIZATION OF LIPOPROTEIN ENVA IN CHLAMYDIA-PSITTACI 6BC

The primary sequence of the small cysteine-rich protein (EnvA) of Chla mydia psittaci 6BC has been shown to possess a potential lipid modific ation/signal peptidase II-processing site, and the mature protein was labeled by a [H-3]palmitic acid precursor. We further characterized th e mature EnvA, showing that it lacks the N-terminal methionine of the primary peptide, is hydrophobic despite a peptide sequence that is pre dicted to be hydrophilic, and appears to be lipid modified at an N-ter minal cysteine in a manner analogous to that of murein lipoproteins of gram-negative bacteria. We also report the fatty acid content of the small cysteine-rich proteins of C. psittaci and Chlamydia trachomatis L2 as determined by combined gas chromatography-mass spectrometry.