Characterization of lipoprotein EnvA in Chlamydia psittaci 6BC.
AUTOR(ES)
Everett, K D
RESUMO
The primary sequence of the small cysteine-rich protein (EnvA) of Chlamydia psittaci 6BC has been shown to possess a potential lipid modification/signal peptidase II-processing site, and the mature protein was labeled by a [3H]palmitic acid precursor. We further characterized the mature EnvA, showing that it lacks the N-terminal methionine of the primary peptide, is hydrophobic despite a peptide sequence that is predicted to be hydrophilic, and appears to be lipid modified at an N-terminal 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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=196828Documentos Relacionados
- Architecture of the cell envelope of Chlamydia psittaci 6BC.
- Identification of an early-stage gene of Chlamydia psittaci 6BC.
- Sequence analysis and lipid modification of the cysteine-rich envelope proteins of Chlamydia psittaci 6BC.
- Cloning and sequence analysis of the major outer membrane protein gene of Chlamydia psittaci 6BC.
- Enhancement of in vitro transcription by addition of cloned, overexpressed major sigma factor of Chlamydia psittaci 6BC.
