ArticleThe Journal of biological chemistry2013
RapA2 is a calcium-binding lectin composed of two highly conserved cadherin-like domains that specifically recognize Rhizobium leguminosarum acidic exopolysaccharides.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 33 citations in OpenAlex.
- The calcium signal regulatory network and the roles of calcium-binding proteins in bacteria.World journal of microbiology & biotechnology · 2026Review
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- Factors governing attachment ofmSystems · 2024Article
- Unveiling the Secrets of Calcium-Dependent Proteins in Plant Growth-Promoting Rhizobacteria: An Abundance of Discoveries Awaits.Plants (Basel, Switzerland) · 2023Review
- Interacting bactofilins impact cell shape of the MreB-less multicellular Rhodomicrobium vannielii.PLoS genetics · 2023Article
- A Germin-Like Protein GLP1 of Legumes Mediates Symbiotic Nodulation by Interacting with an Outer Membrane Protein of Rhizobia.Microbiology spectrum · 2023Article
- Mycobacterial Adhesion: From Hydrophobic to Receptor-Ligand Interactions.Microorganisms · 2022Review
- RapD Is a Multimeric Calcium-Binding Protein That Interacts With theFrontiers in microbiology · 2022Article
- Cadherins in early neural development.Cellular and molecular life sciences : CMLS · 2021Review
- Mechanisms Underlying the Rhizosphere-To-Rhizoplane Enrichment ofMicroorganisms · 2020Article
- Rhizobia: from saprophytes to endosymbionts.Nature reviews. Microbiology · 2018Review
- Shining a light on the dark world of plant root-microbe interactions.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The Regulatory Protein RosR Affects Rhizobium leguminosarum bv. trifolii Protein Profiles, Cell Surface Properties, and Symbiosis with Clover.Frontiers in microbiology · 2016Article
- AFrontiers in microbiology · 2016Article
- Adhesins Involved in Attachment to Abiotic Surfaces by Gram-Negative Bacteria.Microbiology spectrum · 2015Review
- 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
- Lipopolysaccharide O-chain core region required for cellular cohesion and compaction of in vitro and root biofilms developed by Rhizobium leguminosarum.Applied and environmental microbiology · 2015Article
- Structure and sequence analyses of Bacteroides proteins BVU_4064 and BF1687 reveal presence of two novel predominantly-beta domains, predicted to be involved in lipid and cell surface interactions.BMC bioinformatics · 2015Article
- Mutation of praR in Rhizobium leguminosarum enhances root biofilms, improving nodulation competitiveness by increased expression of attachment proteins.Molecular microbiology · 2014Article
- Attachment of Agrobacterium to plant surfaces.Frontiers in plant science · 2014Review
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In silico analyses have revealed a conserved protein domain (CHDL) widely present in bacteria that has significant structural similarity to eukaryotic cadherins. A CHDL domain was shown to be present in RapA, a protein that is involved in autoaggregation of Rhizobium cells, biofilm formation, and adhesion to plant roots as shown by us and others. Structural similarity to cadherins suggested calcium-dependent oligomerization of CHDL domains as a mechanistic basis for RapA action. Here we show by circular dichroism spectroscopy, light scattering, isothermal titration calorimetry, and other methods that RapA2 from Rhizobium leguminosarum indeed exhibits a cadherin-like β-sheet conformation and that its proper folding and stability are dependent on the binding of one calcium ion per protein molecule. By further in silico analysis we also reveal that RapA2 consists of two CHDL domains and expand the range of CHDL-containing proteins in bacteria and archaea. However, light scattering assays at various concentrations of added calcium revealed that RapA2 formed neither homo-oligomers nor hetero-oligomers with RapB (a distinct CHDL protein), indicating that RapA2 does not mediate cellular interactions through a cadherin-like mechanism. Instead, we demonstrate that RapA2 interacts specifically with the acidic exopolysaccharides (EPSs) produced by R. leguminosarum in a calcium-dependent manner, sustaining a role of these proteins in the development of the biofilm matrix made of EPS. Because EPS binding by RapA2 can only be attributed to its two CHDL domains, we propose that RapA2 is a calcium-dependent lectin and that CHDL domains in various bacterial and archaeal proteins confer carbohydrate binding activity to these proteins.
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