A cationic antimicrobial peptide enhances the infectivity of Coxiella burnetii

Purified Coxiella burnetii (Nine Mile, phase I) ricketssiae were exposed to a synthetic peptide (CAP37(20-44)) based on the amino acid sequence of CAP37--a 37 K human neutrophil granule-associated cationic antimicrobial protein--and their capacity to infect L929 mouse fibroblast cells was assessed d...

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Bibliographic Details
Published in:	Acta virologica (Anglickâa verze) Vol. 39; no. 4; p. 223
Main Authors:	Aragon, A S, Pereira, H A, Baca, O G
Format:	Journal Article
Language:	English
Published:	Slovakia 01-09-1995
Subjects:	Animals Antimicrobial Cationic Peptides Blood Proteins - pharmacology Carrier Proteins Cell Line Coxiella burnetii - drug effects Coxiella burnetii - growth & development Dose-Response Relationship, Drug Humans Mice
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Summary:	Purified Coxiella burnetii (Nine Mile, phase I) ricketssiae were exposed to a synthetic peptide (CAP37(20-44)) based on the amino acid sequence of CAP37--a 37 K human neutrophil granule-associated cationic antimicrobial protein--and their capacity to infect L929 mouse fibroblast cells was assessed during a 10-day post-exposure period. Because the parasite thrives within the acidic phagolysosome we anticipated that CAP37(20-44) would have no adverse effect on the organism. This was borne out by the experiments; however, to our surprise, treated C. burnetii had a much greater capacity to infect L cells than the non-treated counterpart. We speculate that the peptide exhibits opsonin-like properties, enhancing attachment of the rickettsia to the host cell surface and subsequent entry.
ISSN:	0001-723X