A unipolarly located, cell-surface-associated agglutinin, RapA, belongs to a family of Rhizobium-adhering proteins (Rap) in rhizobium leguminosarum bv. trifolii

Article Abstract:

Results reveal that RapA1 is one of the four rhizobium-adhering proteins in Rhizobium leguminosarum bv. trifolii strain R200, which binds to bacterial receptors. The binding is mediated by two homologous Ra domains of RapA1 and the protein agglutinates R200 cells by virtue of its similarities to lectin domains.

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A second IgG-binding protein in Staphylococcus aureus

Article Abstract:

Studies have shown the existence of a second immunoglobulin G (IgG) binding protein in Staphylococcus aureus designated as Sbi encoded in the gene sbi. The gene has been cloned and sequenced. Further investigations revealed that the gene is present in a number of S. aureus strains. Further, the Sbi polypeptide has 436 amino acid residues and has similar IgG binding properties as protein A.

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Structural and putative regulatory genes involved in cellulose synthesis in Rhizobium leguminosarum bv. trifolii

Article Abstract:

A study was conducted to analyze genes involved in the cellulose synthesis in Rhizobium leguminosarum bv. trifolii. The genes were identified using Tn5 mutagenesis. Four of the genes supported homology to the previously cloned and sequenced Agrobacterium tumefaciens cellulose genes celA, celB, celC and celE. Two tandemly located genes were also shown to be involved in the regulation of cellulose synthesis.

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