Document Detail

Secretory Phospholipase A(2) in Dromedary Tears: a Host Defense Against Staphylococci and Other Gram-Positive Bacteria.
MedLine Citation:
PMID:  23344945     Owner:  NLM     Status:  Publisher    
The best known physiologic function of secreted phospholipase A(2) (sPLA(2)) group IIA (sPLA(2)-IIA) is defense against bacterial infection through hydrolytic degradation of bacterial membrane phospholipids. In fact, sPLA(2)-IIA effectively kills Gram-positive bacteria and to a lesser extent Gram-negative bacteria and is considered a major component of the eye's innate immune defense system. The antibacterial properties of sPLA(2) have been demonstrated in rabbit and human tears. In this report, we have analyzed the bactericidal activity of dromedary tears and the subsequently purified sPLA(2) on several Gram-positive bacteria. Our results showed that the sPLA(2) displays a potent bactericidal activity against all the tested bacteria particularly against the Staphylococcus strains when tested in the ionic environment of tears. There is a synergic action of the sPLA(2) with lysozyme when added to the bacteria culture prior to sPLA(2). Interestingly, lysozyme purified from dromedary tears showed a significant bactericidal activity against Listeria monocytogene and Staphylococcus epidermidis, whereas the one purified from human tears displayed no activity against these two strains. We have also demonstrated that Ca(2+) is crucial for the activity of dromedary tear sPLA(2) and to a less extent Mg(2+) ions. Given the presence of sPLA(2) in tears and intestinal secretions, this enzyme may play a substantial role in innate mucosal and systemic bactericidal defenses against Gram-positive bacteria.
Abir Ben Bacha; Islem Abid
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-1-24
Journal Detail:
Title:  Applied biochemistry and biotechnology     Volume:  -     ISSN:  1559-0291     ISO Abbreviation:  Appl. Biochem. Biotechnol.     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-1-24     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8208561     Medline TA:  Appl Biochem Biotechnol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Biochemistry Department, Science College, King Saud University, P.O. Box 22452, Riyadh, 11495, Saudi Arabia,
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