ArticleInfection and immunity1992
Influence of saliva on aggregation and adherence of Streptococcus gordonii HG 222.
Article in Infection and immunity, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
20 citing papers in PubMed, 72 citations in OpenAlex.
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- Interactions of Streptococcus mutans fimbria-associated surface proteins with salivary components.Clinical and diagnostic laboratory immunology · 1999Article
- Cell surface polypeptide CshA mediates binding of Streptococcus gordonii to other oral bacteria and to immobilized fibronectin.Infection and immunity · 1996Article
- Interaction of the salivary low-molecular-weight mucin (MG2) with Actinobacillus actinomycetemcomitans.Antonie van Leeuwenhoek · 1996Article
- Structure, biosynthesis, and function of salivary mucins.Molecular and cellular biochemistry · 1994Review
- Colonization of the murine oral cavity by Streptococcus gordonii.Infection and immunity · 1994Article
- Inactivation of the gene encoding surface protein SspA in Streptococcus gordonii DL1 affects cell interactions with human salivary agglutinin and oral actinomyces.Infection and immunity · 1993Article
- Adherence of Streptococcus gordonii HG 222 in the presence of saliva.Antonie van Leeuwenhoek · 1993Article
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Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The influence of saliva on the aggregation and adherence of Streptococcus gordonii HG 222 was studied. The aggregation was measured spectrophotometrically, and the adherence of S. gordonii to microtiter plate wells was measured in an enzyme-linked immunosorbent assay system. The aggregation of HG 222 was induced primarily by mucous saliva, whereas the adherence of HG 222 to microtiter plates was mediated by both mucous and serous saliva. Fractions of submandibular saliva, obtained by gel filtration and containing low-molecular-weight mucins (MG-2), induced both bacterial aggregation and adherence. Purified MG-2 induced aggregation and promoted adherence, whereas high-molecular-weight mucins (MG-1) did not. After incubating clarified human whole saliva with HG 222, only MG-2, and not MG-1, was bound by the bacteria. Proline-rich proteins (PRPs) and proline-rich glycoprotein (PRG) promoted the adherence of HG 222. These proteins in solution bound to HG 222 but did not induce aggregation of the bacterial cells. PRPs and PRG in solution were not able to inhibit adherence to microtiter plate wells coated with the same components. Purified alpha-amylase hardly promoted adherence to microtiter plates but, in the soluble state, readily bound to HG 222. In conclusion, these results indicate that the aggregation of S. gordonii HG 222 is mediated primarily by MG-2. These mucins also promote adherence. Several other salivary components, such as PRPs and PRG, are also involved in the adherence of HG 222.
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