Salivary histatin as an inhibitor of a protease produced by the oral bacterium Bacteroides gingivalis

Respiratory inhibition of isolated mammalian mitochondria by salivary antifungal peptide histatin-5

“…Many of the smaller members of the histatin family are proteolytic products of Hist-1 and Hist-3. Histatins demonstrate a number of biological activities in vitro, including maintenance of tooth surface integrity, the induction of histamine release, and inhibition of proteases [5][6][7][8][9]. Histatins have potential as therapeutic agents against oral candidiasis [10], being potent antifungal molecules with a low toxicity to human cells, as evidenced by its lack of lytic activity to human erythrocytes and various human cell lines and primary cells [11,12].…”

Cationic Peptide Interactions with Biological Macromolecules

“…Surprisingly, the human neutrophil defensin 1 (HNP-1) which differs structurally to histatins appeared to act in the same manner as histatin 5, probably sharing the same molecular target in Candida albicans [77]. Besides, histatin 5 was found to be an inhibitor of B. gingivalis trypsin-like protease probably accounting for natural protection against periodontitis [78]. They reduce the activity of a Bacteroides gingivalis trypsin-like protease by competitive inhibition [78].…”

“…Besides, histatin 5 was found to be an inhibitor of B. gingivalis trypsin-like protease probably accounting for natural protection against periodontitis [78]. They reduce the activity of a Bacteroides gingivalis trypsin-like protease by competitive inhibition [78]. This protease may be responsible for the periodontitis caused by B. gingivalis [79,80], implying that histatins play an important role in combating oral pathogens.…”

IL-22 Induces an Acute-Phase Response Associated to a Cohort of Acute Phase Proteins and Antimicrobial Peptides as Players of Homeostasis

“…In a mouse model of septicemia, LL-37 binds to and neutralizes LPS and protects against endotoxic shock (Bals et al, 1999). Histatins protect from periodontal disease by inhibiting the B. gingivalis protease (Nishikata et al, 1991). Due the efficiency against microbes the use of AMP, some AMP have been extracted from species different of those where effects are needed.…”