Antibacterial properties of recombinant human non-pancreatic secretory phospholipase A(2).

Abstract

Human non-pancreatic secretory phospholipase A2 (hnpsPLA2) is a group IIA phospholipase A2 which plays an important role in the innate immune response. This enzyme was found to exhibit bactericidal activity toward Gram-positive bacteria, but not Gram-negative ones. Though native hnpsPLA2 is active over a broad pH range, it is only highly active at alkaline conditions with the optimum activity pH of about 8.5. In order to make it highly active at neutral pH, we have obtained two hnpsPLA2 mutants, Glu89Lys and Arg100Glu that work better at neutral pH in a previous study. In the present study, we tested the bactericidal effects of the native hnpsPLA2 and the two mutants. Both native hnpsPLA2 and the two mutants exhibit bactericidal activity toward Gram-positive bacteria. Furthermore, they can also kill Escherichia coli, a Gram-negative bacterium. The two mutants showed better bactericidal activity for E. coli at neutral pH than the native enzyme, which is consistent with the enzyme activities. As hnpsPLA2 is highly stable and biocompatible, it may provide a promising therapy for bacteria infection treatment or other bactericidal applications.

• Authors: Shunchen Qiu, Luhua Lai
• Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 441 Issue 2 Pg. 453-6 (Nov 15 2013) ISSN: 1090-2104 [Electronic] United States
• PMID: 24369901 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
• Copyright: Copyright © 2013 Elsevier Inc. All rights reserved.

Chemical References

• Anti-Bacterial Agents
• Recombinant Proteins
• Group II Phospholipases A2

Topics

• Anti-Bacterial Agents (pharmacology)
• Escherichia coli (drug effects)
• Group II Phospholipases A2 (genetics, pharmacology)
• Humans
• Mutation
• Recombinant Proteins (genetics, pharmacology)
• Staphylococcus aureus (drug effects)