Novel Phospholipase A Activity Secreted by Legionella Species

AUTOR(ES)

Flieger, Antje

FONTE

American Society for Microbiology

RESUMO

Bacterial phospholipases are regarded as a major virulence factor in infection. In bacteria associated with pneumonia, destruction of lung surfactant and host cell membranes by bacterial phospholipases secreted during infection is thought to contribute to the disease. Phospholipase C (PLC) activity has been described in several Legionella species (W. B. Baine, J. Gen. Microbiol. 134:489–498, 1988; W. B. Baine, J. Gen. Microbiol. 131:1383–1391, 1985). By using detection methods such as thin-layer chromatography and mass spectrometry, PLC activity could not be detected in several strains of Legionella pneumophila. Instead, phospholipid degradation was identified to be caused by a novel PLA activity. We could demonstrate that PLA secretion starts at the mid-exponential-growth phase when bacteria were grown in liquid culture. Several Legionella species secreted different amounts of PLA. Legionella PLA may act as a powerful agent in the mediation of pathogenicity due to destruction of lung surfactant and epithelial cells.

Documentos Relacionados

• Novel Lysophospholipase A Secreted by Legionella pneumophila
• The DotA protein from Legionella pneumophila is secreted by a novel process that requires the Dot/Icm transporter
• Phospholipase PlaB of Legionella pneumophila Represents a Novel Lipase Family: PROTEIN RESIDUES ESSENTIAL FOR LIPOLYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND HEMOLYSIS*
• Molecular Characterization of a Secreted Enzyme with Phospholipase B Activity from Moraxella bovis
• In vitro activity of RP 74501-RP 74502, a novel streptogramin antimicrobial mixture, against clinical isolates of Legionella species.