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Advances in Dental Research, Vol 14, Issue 1, 16-21
Copyright © 2000 by International & American Associations for Dental Research


Articles

Salivary histatin 5 and its similarities to the other antimicrobial proteins in human saliva

M Edgerton and SE Koshlukova

Department of Oral Biology, School of Dental Medicine, State University of New York at Buffalo, 14214, USA. Edgerto@buffalo.edu

Non-immune salivary proteins--including lactoperoxidase, lysozyme, lactoferrin, and histatins--are key components of the innate host defense system in the oral cavity. Many antimicrobial proteins contain multiple functional domains, with the result that one protein may have more than one mechanism of antimicrobial activity. These domains may be separated by proteolytic cleavage, creating smaller proteins with functional antimicrobial activity in saliva as described for lysozyme, lactoferrin, and histatins. These small cationic proteins then exert cytotoxic activity to oral bacteria and fungi. Salivary histatin 5 initiates killing of C. albicans through binding to yeast membrane proteins and non-lytic release of cellular ATP. Extracellular ATP may then activate fungal ATP receptors to induce ultimate cell death. This mechanism for fungal cytotoxicity may be shared by other antimicrobial cationic proteins. Microbicidal domains of salivary and host innate proteins should be considered as potential therapeutic agents in the oral cavity.


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