ArticleJournal of bacteriology2010
Discovery and characterization of cadherin domains in Saccharophagus degradans 2-40.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 33 citations in OpenAlex.
- Article
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- Metabolic reconstruction of the near complete microbiome of the model sponge Ianthella basta.Environmental microbiology · 2023Article
- Cultured Bacteria Provide Insight into the Functional Potential of the Coral-Associated Microbiome.mSystems · 2022Article
- Collective behavior and virulence arsenal of the fish pathogenFrontiers in cellular and infection microbiology · 2022Article
- A genomic view of the microbiome of coral reef demosponges.The ISME journal · 2021Article
- Cadherins in early neural development.Cellular and molecular life sciences : CMLS · 2021Review
- A genomic view of trophic and metabolic diversity in clade-specific Lamellodysidea sponge microbiomes.Microbiome · 2020Article
- Genome-Wide Identification and Functional Characterization of β-Agarases inFrontiers in microbiology · 2020Article
- Recent Advances and Challenges towards Sustainable Polyhydroxyalkanoate (PHA) Production.Bioengineering (Basel, Switzerland) · 2017Review
- Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex.Structure (London, England : 1993) · 2017Article
- Phosphate Limitation Induces Drastic Physiological Changes, Virulence-Related Gene Expression, and Secondary Metabolite Production in Pseudovibrio sp. Strain FO-BEG1.Applied and environmental microbiology · 2015Article
- Biofilm formation by Psychrobacter arcticus and the role of a large adhesin in attachment to surfaces.Applied and environmental microbiology · 2013Article
- Expression patterns reveal niche diversification in a marine microbial assemblage.The ISME journal · 2013Article
- RapA2 is a calcium-binding lectin composed of two highly conserved cadherin-like domains that specifically recognize Rhizobium leguminosarum acidic exopolysaccharides.The Journal of biological chemistry · 2013Article
- The evolutionary origin of epithelial cell-cell adhesion mechanisms.Current topics in membranes · 2013Article
- S-layer homology domain proteins Csac_0678 and Csac_2722 are implicated in plant polysaccharide deconstruction by the extremely thermophilic bacterium Caldicellulosiruptor saccharolyticus.Applied and environmental microbiology · 2012Article
- Cadherin domains in the polysaccharide-degrading marine bacterium Saccharophagus degradans 2-40 are carbohydrate-binding modules.Journal of bacteriology · 2011Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Saccharophagus degradans strain 2-40 is a prominent member of newly discovered group of marine and estuarine bacteria that recycle complex polysaccharides. The S. degradans 2-40 genome codes for 15 extraordinary long polypeptides, ranging from 274 to 1,600 kDa. Five of these contain at least 52 cadherin (CA) and cadherin-like (CADG) domains, the types of which were reported to bind calcium ions and mediate protein/protein interactions in metazoan systems. In order to evaluate adhesive features of these domains, recombinant CA doublet domains (two neighboring domains) from CabC (Sde_3323) and recombinant CADG doublet domains from CabD (Sde_0798) were examined qualitatively and quantitatively for homophilic and heterophilic interactions. In addition, CA and CADG doublet domains were tested for adhesion to the surface of S. degradans 2-40. Results showed obvious homophilic and heterophilic, calcium ion-dependent interactions between CA and CADG doublet domains. Likewise, CA and CADG doublet domains adhered to the S. degradans 2-40 surface of cells that were grown on xylan from birch wood or pectin, respectively, as a sole carbon source. This research shows for the first time that bacterial cadherin homophilic and heterophilic interactions may be similar in their nature to cadherin domains from metazoan lineages. We hypothesize that S. degradans 2-40 cadherin and cadherin-like multiple domains contribute to protein-protein interactions that may mediate cell-cell contact in the marine environment.
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Registered trials
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