Document Detail


Phospholipid synthesis by Staphylococcus aureus during (Sub)Lethal attack by mammalian 14-kilodalton group IIA phospholipase A2.
MedLine Citation:
PMID:  10678935     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Killing of gram-positive bacteria by mammalian group IIA phospholipases A2 (PLA2) requires the catalytic activity of the enzyme. However, nearly complete degradation of the phospholipids can occur with little effect on bacterial viability, suggesting that PLA2-treated bacteria can biosynthetically replace phospholipids that are lost due to PLA2 action. In the presence of albumin, phospholipid degradation products are quantitatively sequestered extracellularly. In the absence of albumin, the bacteria retain and substantially reutilize the phospholipid breakdown products and survive an otherwise lethal dose of PLA2. PLA2-treated bacteria also continue to incorporate sodium [2-(14)C]acetate into phospholipids, suggesting that the bacteria are attempting to repair the damaged membranes by de novo synthesis of phospholipids. To determine whether PLA2 action also triggers activation of bacterial lipolytic enzymes, the effects of nisin and PLA2 on the degradation of S. aureus lipids were compared. In contrast to nisin treatment, PLA2 treatment does not stimulate endogenous phospholipase activity in S. aureus. These findings show that S. aureus responds to PLA2 attack by continued phospholipid (re)synthesis by both de novo and salvage pathways. The fate of PLA2-treated S. aureus therefore appears to depend on the relative rates of phospholipid degradation and synthesis.
Authors:
A K Foreman-Wykert; J Weiss; P Elsbach
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Infection and immunity     Volume:  68     ISSN:  0019-9567     ISO Abbreviation:  Infect. Immun.     Publication Date:  2000 Mar 
Date Detail:
Created Date:  2000-03-16     Completed Date:  2000-03-16     Revised Date:  2010-09-10    
Medline Journal Info:
Nlm Unique ID:  0246127     Medline TA:  Infect Immun     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1259-64     Citation Subset:  IM    
Affiliation:
Department of Microbiology, New York University School of Medicine, New York, New York 10016, USA.
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MeSH Terms
Descriptor/Qualifier:
Acetates / metabolism
Albumins / pharmacology
Animals
Lysophospholipids / biosynthesis
Membrane Lipids / biosynthesis*
Phospholipases A / pharmacology*
Phospholipases A2
Phospholipids / biosynthesis*
Rabbits
Staphylococcus aureus / drug effects*,  metabolism
Grant Support
ID/Acronym/Agency:
AI-18571/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/Acetates; 0/Albumins; 0/Lysophospholipids; 0/Membrane Lipids; 0/Phospholipids; 0/lysophosphatidylglycerol; EC 3.1.1.-/Phospholipases A; EC 3.1.1.4/Phospholipases A2
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