Novel Lysophospholipase A Secreted by Legionella pneumophila-Reference-Cited by-同舟云学术

Novel Lysophospholipase A Secreted by Legionella pneumophila

Published:2001-03-15 Issue:6 Volume:183 Page:2121-2124
ISSN:0021-9193
Container-title:Journal of Bacteriology
language:en
Short-container-title:J Bacteriol

Author:

Flieger Antje¹²,Gong Shimei¹,Faigle Marion¹,Stevanovic Stefan³,Cianciotto Nicholas P.²,Neumeister Birgid¹

Affiliation:

1. Abteilung für Transfusionsmedizin, Universitätsklinikum Tübingen,1 and

2. Department of Microbiology-Immunology, Northwestern University Medical School, Chicago, Illinois 606112

3. Interfakultäres Institut für Zellbiologie, Abteilung Immunologie, Universität Tübingen,3 D-72076 Tübingen, Germany, and

Abstract

ABSTRACT We show that Legionella pneumophila possesses lysophospholipase A activity, which releases fatty acids from lysophosphatidylcholine. The NH 2 -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.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/JB.183.6.2121-2124.2001

Reference31 articles.

1. Gapped BLAST and PSI-BLAST: a new generation of protein database searchprograms;Altschul S. F.;Nucleic Acids Res.,1997

2. Secreted enzymatic activities of wild-type and pilD-deficient Legionella pneumophila;Aragon V.;Infect. Immun.,2000

3. Injury of lung alveolar cells by lysolecithin;Aronson J. F.;Exp. Mol. Pathol.,1977

4. Physical and chemical characterization of the oligomerization state of the Aeromonas hydrophila lipase/acyltransferase;Ausio J.;FEBS Lett.,1993

5. Legionella pneumophila zinc metalloprotease is structurally and functionally homologous to Pseudomonas aeruginosa elastase

Cited by 59 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. The intracellular growth of the vacuolar pathogen Legionella pneumophila is dependent on the acyl chain composition of host membranes;Frontiers in Bacteriology;2024-02-12

2. Structure–function relationships underpin disulfide loop cleavage‐dependent activation of Legionella pneumophila lysophospholipase A PlaA;Molecular Microbiology;2023-12-22

3. The intracellular growth of the vacuolar pathogenLegionella pneumophilais dependent on the acyl chain composition of host membranes;2023-11-20

4. Tools and mechanisms of vacuolar escape leading to host egress in Legionella pneumophila infection: Emphasis on bacterial phospholipases;Molecular Microbiology;2023-10-27

5. Structure-function relationships underpin disulfide loop cleavage-dependent activation ofLegionella pneumophilalysophosholipase A PlaA;2023-03-24