The antibacterial properties of secreted phospholipases A2
The antibacterial properties of secreted phospholipases A2
There is a considerable body of evidence to support the antibacterial properties of the group IIa phospholipase A2 as an important physiological function. This enzyme is able to act as an acute phase protein and may be part of the innate defence system of the body, acting in concert with other antibacterial proteins and peptides. The enzyme is most effective against Gram-positive bacteria whereas penetration of the lipopolysaccharide coat of Gram-negative bacteria requires bactericidal/permeability-increasing protein (BPI) as an additional permeabilising factor. The global cationic nature of this protein (pI>10.5) appears to facilitate penetration of the anionic bacterial cell wall. In addition, the considerable preference of the enzyme for anionic phospholipid interfaces provides specificity toward anionic bacterial membranes as opposed to zwitterionic eucaryotic cell membranes.
group iia secreted phospholipase a2, membrane hydrolysis, antimicrobial, gram-negative, gram-positive, bactericidal/permeability-increasing protein
71-82
Buckland, Andrew G.
c0b3a024-9df7-4414-9853-11fc6e55f7d1
Wilton, David C.
4b995f66-ad6c-4d96-9179-c64f3b54466a
October 2000
Buckland, Andrew G.
c0b3a024-9df7-4414-9853-11fc6e55f7d1
Wilton, David C.
4b995f66-ad6c-4d96-9179-c64f3b54466a
Buckland, Andrew G. and Wilton, David C.
(2000)
The antibacterial properties of secreted phospholipases A2.
Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 1488 (1-2), .
(doi:10.1016/S1388-1981(00)00111-6).
Abstract
There is a considerable body of evidence to support the antibacterial properties of the group IIa phospholipase A2 as an important physiological function. This enzyme is able to act as an acute phase protein and may be part of the innate defence system of the body, acting in concert with other antibacterial proteins and peptides. The enzyme is most effective against Gram-positive bacteria whereas penetration of the lipopolysaccharide coat of Gram-negative bacteria requires bactericidal/permeability-increasing protein (BPI) as an additional permeabilising factor. The global cationic nature of this protein (pI>10.5) appears to facilitate penetration of the anionic bacterial cell wall. In addition, the considerable preference of the enzyme for anionic phospholipid interfaces provides specificity toward anionic bacterial membranes as opposed to zwitterionic eucaryotic cell membranes.
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Published date: October 2000
Keywords:
group iia secreted phospholipase a2, membrane hydrolysis, antimicrobial, gram-negative, gram-positive, bactericidal/permeability-increasing protein
Organisations:
Centre for Biological Sciences
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Local EPrints ID: 372350
URI: http://eprints.soton.ac.uk/id/eprint/372350
ISSN: 1388-1981
PURE UUID: 9bd11132-5922-4ce6-a78d-78410969322a
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Date deposited: 01 Dec 2014 13:37
Last modified: 14 Mar 2024 18:35
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Author:
Andrew G. Buckland
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