☆ 4.7 Article

Histatin 5 binds to Porphyromonas gingivalis hemagglutinin B (HagB) and alters HagB-induced chemokine responses

SCIENTIFIC REPORTS (2014)

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SCIENTIFIC REPORTS
卷 4, 期 -, 页码 -

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NATURE PORTFOLIO
DOI: 10.1038/srep03904

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Multidisciplinary Sciences

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  1. NIH NIDCR [R01 DE014390]

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Histatins are human salivary gland peptides with anti-microbial and anti-inflammatory activities. In this study, we hypothesized that histatin 5 binds to Porphyromonas gingivalis hemagglutinin B (HagB) and attenuates HagB-induced chemokine responses in human myeloid dendritic cells. Histatin 5 bound to immobilized HagB in a surface plasmon resonance (SPR) spectroscopy-based biosensor system. SPR spectroscopy kinetic and equilibrium analyses, protein microarray studies, and I-TASSER structural modeling studies all demonstrated two histatin 5 binding sites on HagB. One site had a stronger affinity with a K-D1 of 1.9 mu M and one site had a weaker affinity with a K-D2 of 60.0 mu M. Binding has biological implications and predictive modeling studies and exposure of dendritic cells both demonstrated that 20.0 mu M histatin 5 attenuated (p < 0.05) 0.02 mu M HagB-induced CCL3/MIP-1 alpha, CCL4/MIP-1 beta, and TNF alpha responses. Thus histatin 5 is capable of attenuating chemokine responses, which may help control oral inflammation.

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