Unknown

Dataset Information

0

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


ABSTRACT: 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 KD1 of 1.9 ?M and one site had a weaker affinity with a KD2 of 60.0 ?M. Binding has biological implications and predictive modeling studies and exposure of dendritic cells both demonstrated that 20.0 ?M histatin 5 attenuated (p < 0.05) 0.02 ?M HagB-induced CCL3/MIP-1?, CCL4/MIP-1?, and TNF? responses. Thus histatin 5 is capable of attenuating chemokine responses, which may help control oral inflammation.

SUBMITTER: Borgwardt DS 

PROVIDER: S-EPMC3912440 | biostudies-literature | 2014 Jan

REPOSITORIES: biostudies-literature

altmetric image

Publications


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 mo  ...[more]

Similar Datasets

| S-EPMC3665294 | biostudies-other
2023-04-12 | PXD041477 | iProX
| S-EPMC2713102 | biostudies-literature
| S-EPMC4293770 | biostudies-literature
| S-EPMC3647041 | biostudies-literature
| S-EPMC3001241 | biostudies-literature
| S-EPMC5193354 | biostudies-literature