ArticleInfection and immunity2001
Identification of independent Streptococcus gordonii SspA and SspB functions in coaggregation with Actinomyces naeslundii.
Article in Infection and immunity, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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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
25 citing papers in PubMed, 69 citations in OpenAlex.
- An innovative microplate-based method to measure coaggregation between a model pair of coaggregating oral bacteria.Journal of oral microbiology · 2026Article
- Subgingival Microbiota Profile in Association with Cigarette Smoking in Young Adults: A Cross-Sectional Study.Dentistry journal · 2021Article
- Polymer Adhesin Domains in Gram-Positive Cell Surface Proteins.Frontiers in microbiology · 2020Review
- Streptococcus mutans SpaP binds to RadD of Fusobacterium nucleatum ssp. polymorphum.Molecular oral microbiology · 2017Article
- Effects of surface reaction-type pre-reacted glass ionomer on oral biofilm formation of Streptococcus gordonii.Odontology · 2016Article
- Structural and Functional Analysis of Cell Wall-anchored Polypeptide Adhesin BspA in Streptococcus agalactiae.The Journal of biological chemistry · 2016Article
- Biofilms as "Connectors" for Oral and Systems Medicine: A New Opportunity for Biomarkers, Molecular Targets, and Bacterial Eradication.Omics : a journal of integrative biology · 2016Review
- Probing of microbial biofilm communities for coadhesion partners.Applied and environmental microbiology · 2014Article
- Microbial interactions in building of communities.Molecular oral microbiology · 2013Review
- Adhesion determinants of the Streptococcus species.Microbial biotechnology · 2010Review
- Two intramolecular isopeptide bonds are identified in the crystal structure of the Streptococcus gordonii SspB C-terminal domain.Journal of molecular biology · 2010Article
- Platelet-bacterial interactions.Cellular and molecular life sciences : CMLS · 2010Review
- The Bifidobacterium dentium Bd1 genome sequence reflects its genetic adaptation to the human oral cavity.PLoS genetics · 2009Article
- Streptococcus gordonii modulates Candida albicans biofilm formation through intergeneric communication.Infection and immunity · 2009Article
- Crystal structure of the variable domain of the Streptococcus gordonii surface protein SspB.Protein science : a publication of the Protein Society · 2009Article
- The thrombotic potential of oral pathogens.Journal of oral microbiology · 2009Article
- Bacterial and host interactions of oral streptococci.DNA and cell biology · 2009Review
- A crystallizable form of the Streptococcus gordonii surface antigen SspB C-domain obtained by limited proteolysis.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
- Coaggregation by the freshwater bacterium Sphingomonas natatoria alters dual-species biofilm formation.Applied and environmental microbiology · 2009Article
- Role of Streptococcus gordonii surface proteins SspA/SspB and Hsa in platelet function.Infection and immunity · 2007Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The initial stages of dental plaque formation involve the adherence of early colonizing organisms such as Streptococcus gordonii and Actinomyces naeslundii to the saliva-coated tooth surface and to each other. The S. gordonii surface proteins SspA and SspB are known to play a role in adherence to salivary proteins and mediate coaggregation with other bacteria. Coaggregation is the adhesin receptor-mediated interaction between genetically distinct cell types and appears to be ubiquitous among oral isolates. To define the function of SspA and SspB separately on the surface of their natural host, we constructed and analyzed the coaggregation properties of an isogenic sspB mutant of S. gordonii DL1, an sspAB double mutant, and a previously described sspA mutant. A. naeslundii strains have been previously classified into six coaggregation groups based on the nature of their coaggregations with S. gordonii DL1 and other oral streptococci. Coaggregation assays with the sspA and sspB mutants showed that SspA and SspB are the streptococcal proteins primarily responsible for defining these coaggregation groups and, thus, are highly significant in the establishment of early dental plaque. SspA exhibited two coaggregation-specific functions. It participated in lactose-inhibitable and -noninhibitable interactions, while SspB mediated only lactose-noninhibitable coaggregations. Accordingly, the sspAB double mutant lacked these functions and allowed us to detect a third coaggregation interaction with one of these organisms. These proteins may play an important role in development of S. gordonii-A. naeslundii communities in early dental plaque. Understanding these adhesin proteins will aid investigations of complex microbial communities that characterize periodontal diseases.
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