Andrew G. Buckland، نويسنده , , David C. Wilton، نويسنده ,

1601672

The antibacterial properties of secreted phospholipases A

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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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Group IIa secreted phospholipase A2 , Membrane hydrolysis , Gram-negative , Gram-positive , Bactericidal/permeability-increasing protein , antimicrobial

Studia Iranica

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