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Pellicle receptors for Actinomyces viscosus type 1 fimbriae in vitro.
- Source :
-
Infection and immunity [Infect Immun] 1989 Oct; Vol. 57 (10), pp. 3003-8. - Publication Year :
- 1989
-
Abstract
- Actinomyces viscosus T14V-J1 and its fimbria-deficient mutant strain possessing type 1 fimbriae strongly aggregated with latex beads treated with acidic proline-rich protein 1, basic proline-rich proteins, and proline-rich glycoprotein and its deglycosylated derivative. These type 1+ strains did not aggregate with latex beads treated with other proteins, such as salivary amylase, salivary histidine-rich polypeptides, laminin, type 1 collagen, fibronectin, or C1q. The type 1+ strains also adsorbed well to experimental pellicles formed with acidic proline-rich protein 1, basic proline-rich proteins, and proline-rich glycoprotein and its deglycosylated derivative on hydroxyapatite (HA) surfaces. These interactions were inhibited with immunoglobulins and Fabs specific for type 1 fimbriae. Type 1- actinomyces exhibited feeble adsorption to latex beads or HA treated with any of the aforementioned proteins. Collectively, these data indicate that actinomyces type 1 fimbriae may specifically interact with several proline-rich salivary molecules, forming experimental pellicles on HA or polystyrene surfaces.
- Subjects :
- Actinomyces drug effects
Actinomyces immunology
Adsorption
Amino Acid Sequence
Durapatite
Hydroxyapatites
Immunoglobulin Fab Fragments physiology
Immunoglobulin G physiology
Latex Fixation Tests methods
Molecular Sequence Data
Peptides pharmacology
Polystyrenes
Proline-Rich Protein Domains
Salivary Proteins and Peptides pharmacology
Actinomyces physiology
Fimbriae, Bacterial physiology
Peptides physiology
Receptors, Immunologic physiology
Salivary Proteins and Peptides physiology
Subjects
Details
- Language :
- English
- ISSN :
- 0019-9567
- Volume :
- 57
- Issue :
- 10
- Database :
- MEDLINE
- Journal :
- Infection and immunity
- Publication Type :
- Academic Journal
- Accession number :
- 2570751
- Full Text :
- https://doi.org/10.1128/iai.57.10.3003-3008.1989