Novel Lysophospholipase A Secreted by Legionella pneumophila
AUTOR(ES)
Flieger, Antje
FONTE
American Society for Microbiology
RESUMO
We show that Legionella pneumophila possesses lysophospholipase A activity, which releases fatty acids from lysophosphatidylcholine. The NH2-terminal sequence of the enzyme contained FGDSLS, corresponding to a catalytic domain in a recently described group of lipolytic enzymes. Culture supernatants of a L. pneumophila pilD mutant lost the ability to cleave lysophosphatidylcholine.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=95111Documentos Relacionados
- Characterization of the Gene Encoding the Major Secreted Lysophospholipase A of Legionella pneumophila and Its Role in Detoxification of Lysophosphatidylcholine
- Novel Phospholipase A Activity Secreted by Legionella Species
- The DotA protein from Legionella pneumophila is secreted by a novel process that requires the Dot/Icm transporter
- lvgA, a Novel Legionella pneumophila Virulence Factor
- Secreted Enzymatic Activities of Wild-Type and pilD-Deficient Legionella pneumophila