SLPI is a natural anti-inflammatory and antimicrobial peptide found in mucous secretions of the oral, respiratory, and genital mucosa, and is secreted by epithelial cells lining these mucosal surfaces (reviewed in Tomee et al., 1998). SLPI is a relatively small cationic peptide (12 kDa), which acts primarily as an endogenous inhibitor of neutrophil elastase, thus limiting tissue injury and inflammation (Bingle and Tetley, 1996). In addition, SLPI has antiretroviral activity and can kill bacterial and fungal targets, through mechanisms that have not yet been defined (reviewed in Tomee et al., 1998). A pronounced fungicidal and fungistatic activity against metabolically active C. albicans yeast organisms has been demonstrated at physiologic concentrations of this peptide, which was localized primarily in the NH2-terminal domain. On a molar basis this activity was similar with that of defensins and lysozyme (Tomee et al., 1997).
Although the first report on the in vitro antimicrobial activity of SLPI was in saliva (McNeely et al., 1995), to date only one study has addressed the functional role of salivary SLPI during oral infection in vivo (Chattopadhyay et al., 2004). This report on HIV-associated oral candidiasis found significantly higher levels of SLPI among participants with a history of OPC as compared to those with no history of this oral infection, but failed to show significantly higher levels in individuals with current oral infection as compared to uninfected controls. In an attempt to explain these findings the authors suggested that elevated levels of SLPI in response to recurrent infection is an attempt of the host to limit oral infection, a response that may persist long after the infection is resolved (Chattopadhyay et al., 2004).
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