Structural domains of Porphyromonas gingivalis recombinant fimbrillin that mediate binding to salivary proline-rich protein and statherin
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چکیده
منابع مشابه
Binding of Porphyromonas gingivalis fimbriae to proline-rich glycoproteins in parotid saliva via a domain shared by major salivary components.
Porphyromonas gingivalis, a putative periodontopathogen, can bind to human saliva through its fimbriae. We previously found that salivary components from the submandibular and sublingual glands bind to P. gingivalis fimbriae and that acidic proline-rich protein (PRP) and statherin function as receptor molecules for fimbriae. In this study, we investigated the fimbria-binding components in parot...
متن کاملBinding of a histidine-rich peptide to Porphyromonas gingivalis.
Porphyromonas gingivalis 381 cells were incubated with 125I-histidine-rich polypeptide (histatin) 5 in the presence or absence of unlabeled histatin 5, to evaluate the histatin-binding capacity of the cells. The binding of histatin 5 was rapid, reversible, saturable and specific. The number of histatin 5-binding sites per cell was 3,600, and the dissociation constant (Kd) was in the order of 10...
متن کاملRegulation of the Porphyromonas gingivalis fimA (Fimbrillin) gene.
In common with many bacterial virulence genes, the fimbrillin (fimA) gene of Porphyromonas gingivalis is modulated in response to environmental fluctuation. The trans-acting components that comprise the regulatory system for transcriptional activity of the fimA gene in P. gingivalis were investigated. Three major proteins were found to bind to the upstream region of the fimA promoter. One of th...
متن کاملHuman salivary acidic proline-rich proteins and statherin promote the attachment of Actinomyces viscosus LY7 to apatitic surfaces.
Actinomyces viscosus LY7 cells adsorbed in high numbers to experimental pellicles formed on hydroxyapatite (HA) from human parotid or submandibular saliva but not to pellicles prepared from human plasma or serum. To determine the nature of the salivary components responsible for promoting adhesion, pellicles were prepared from fractions of submandibular and parotid saliva obtained by chromatogr...
متن کاملSalivary proline-rich protein genes on chromosome 8 of mouse.
Endonuclease restriction (Hind III) fragments of DNA from Chinese hamster X mouse somatic cell hybrids hybridized with proline-rich protein complementary DNA clones only when the DNA was isolated from cells containing mouse chromosome 8, or a fragment of chromosome 8. The evidence suggests that proline-rich protein genes are located at the proximal portion of chromosome 8 toward the centromere.
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ژورنال
عنوان ژورنال: Infection and Immunity
سال: 1996
ISSN: 0019-9567,1098-5522
DOI: 10.1128/iai.64.5.1631-1637.1996