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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Active site mutants of human secreted Group IIA Phospholipase A(2) lacking hydrolytic activity retain their bactericidal effect

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Author(s):
Chioato, Lucimara [1] ; Aragao, Elisangela Aparecida [2] ; Ferreira, Tatiana Lopes [1] ; Ward, Richard J. [2]
Total Authors: 4
Affiliation:
[1] Univ Sao Paulo, Dept Biochem & Immunol, FMRP USP, BR-14040901 Ribeirao Preto, SP - Brazil
[2] Univ Sao Paulo, Dept Quim, Fac Filosofia Ciencias & Letras Ribeirao Preto, FFCLRP USP, BR-14040901 Ribeirao Preto, SP - Brazil
Total Affiliations: 2
Document type: Journal article
Source: Biochimie; v. 94, n. 1, p. 132-136, JAN 2012.
Web of Science Citations: 4
Abstract

The Human Secreted Group IIA Phospholipase A(2) (hsPIA2GIIA) presents potent bactericidal activity, and is considered to contribute to the acute-phase immune response. Hydrolysis of inner membrane phospholipids is suggested to underlie the bactericidal activity, and we have evaluated this proposal by comparing catalytic activity with bactericidal and liposome membrane damaging effects of the G30S, H48Q and D49K h5PLA2GIIA mutants. All mutants showed severely impaired hydrolytic activities against mixed DOPC:DOPG liposome membranes, however the bactericidal effect against Micrococcus luteus was less affected, with 50% killing at concentrations of 1, 3, 7 and 9 mu g/mL for the wild-type, D49K, H48Q and G30S mutants respectively. Furthermore, all proteins showed Ca2+-independent damaging activity against Liposome membranes demonstrating that in addition to the hydrolysis-dependent membrane damage, the hsPLA2GIIA presents a mechanism for permeabilization of phospholipid bilayers that is independent of catalytic activity, which may play a role in the bactericidal function of the protein (C) 2011 Elsevier Masson SAS. All rights reserved. (AU)