Isolation and characterization of Actinomyces viscosus mutants defective in binding salivary proline-rich proteins
نویسندگان
چکیده
منابع مشابه
Isolation and characterization of Actinomyces viscosus mutants defective in binding salivary proline-rich proteins.
Recent studies have provided evidence for human salivary proline-rich proteins (PRPs) serving as potential receptors in the acquired pellicle for Actinomyces viscosus type 1 fimbriae. We report here the isolation of mutants derived from A. viscosus T14V-J1 which are defective in binding to PRPs partially purified from parotid gland saliva. Mutagenesis with ethyl methanesulfonate preceded enrich...
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 کاملSusceptibility to Dental Caries and the Salivary Proline-Rich Proteins
Early childhood caries affects 28% of children aged 2-6 in the US and is not decreasing. There is a well-recognized need to identify susceptible children at birth. Caries-free adults neutralize bacterial acids in dental biofilms better than adults with severe caries. Saliva contains acidic and basic proline-rich proteins (PRPs) which attach to oral streptococci. The PRPs are encoded within a sm...
متن کاملIsolation of Actinomyces viscosus from two patients with clinical infections.
The isolation of Actinomyces viscosus from two patients is described. One was a case of multiple myeloma, the organism being found on blood culture; the other was a patient with a submandibular abscess. These are believed to be the first such isolations of A. viscosus in this country.
متن کاملThe nature of the hydroxyapatite-binding site in salivary acidic proline-rich proteins.
Protein A and C, which are major components of the acidic proline-rich proteins in human saliva, were digested, before or after adsorption to hydroxyapatite, with alkaline phosphatase, trypsin, thermolysin and a proteinase preparation from salivary sediment. The results demonstrate that the binding site is located in the proline-poor N-terminal part of the protein, possibly between residues 3 ...
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ژورنال
عنوان ژورنال: Infection and Immunity
سال: 1992
ISSN: 0019-9567,1098-5522
DOI: 10.1128/iai.60.3.1095-1100.1992