Human common salivary protein 1 (CSP-1) promotes binding of Streptococcus mutans to experimental salivary pellicle and glucans formed on hydroxyapatite surface.
J Proteome Res
; 9(12): 6605-14, 2010 Dec 03.
Article
em En
| MEDLINE
| ID: mdl-20858015
The saliva proteome includes host defense factors and specific bacterial-binding proteins that modulate microbial growth and colonization of the tooth surface in the oral cavity. A multidimensional mass spectrometry approach identified the major host-derived salivary proteins that interacted with Streptococcus mutans (strain UA159), the primary microorganism associated with the pathogenesis of dental caries. Two abundant host proteins were found to tightly bind to S. mutans cells, common salivary protein-1 (CSP-1) and deleted in malignant brain tumor 1 (DMBT1, also known as salivary agglutinin or gp340). In contrast to gp340, limited functional information is available on CSP-1. The sequence of CSP-1 shares 38.1% similarity with rat CSP-1. Recombinant CSP-1 (rCSP-1) protein did not cause aggregation of S. mutans cells and was devoid of any significant biocidal activity (2.5 to 10 µg/mL). However, S. mutans cells exposed to rCSP-1 (10 µg/mL) in saliva displayed enhanced adherence to experimental salivary pellicle and to glucans in the pellicle formed on hydroxyapatite surfaces. Thus, our data demonstrate that the host salivary protein CSP-1 binds to S. mutans cells and may influence the initial colonization of this pathogenic bacterium onto the tooth surface.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Proteínas e Peptídeos Salivares
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Streptococcus mutans
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Durapatita
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Película Dentária
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Glucanos
Idioma:
En
Ano de publicação:
2010
Tipo de documento:
Article
País de afiliação:
Estados Unidos