The N-terminal half part of the oral streptococcal antigen I/IIf contains two distinct binding domains

Abstract In order to investigate the binding properties of the antigen I/IIf from Streptococcus mutans, we analyzed the binding activity of five I/IIf derivatives expressed by I/IIf gene derivatives obtained by insertion of a kanamycin resistance marker. ELISA-derived binding assays showed that the...

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Veröffentlicht in:	FEMS microbiology letters 1997-08, Vol.153 (2), p.439-445
Hauptverfasser:	Sciotti, Michel-Angelo, Yamodo, Innocent, Klein, Jean-Paul, Ogier, Joëlle A.
Format:	Artikel
Sprache:	eng
Schlagworte:	AgI/II Alanine Amino acids Antigens Antigens, Bacterial - chemistry Antigens, Bacterial - genetics Antigens, Bacterial - isolation & purification Antigens, Bacterial - metabolism Bacterial Adhesion - physiology Bacterial Outer Membrane Proteins - chemistry Bacterial Outer Membrane Proteins - genetics Bacterial Outer Membrane Proteins - isolation & purification Bacterial Outer Membrane Proteins - metabolism Bacterial Proteins Binding Carbohydrate Metabolism Carbohydrates Cell Membrane - metabolism Cell membranes Collagen (type I) Derivatives Domains Enzyme-linked immunosorbent assay Epithelial Cells Epithelium - metabolism Escherichia coli - metabolism Extracellular Matrix Proteins - metabolism Fibronectin Humans Kanamycin Keratin Keratins - metabolism Laminin Ligands Membrane Glycoproteins Microbiology Periodic Acid - pharmacology Protein Binding Recombinant Proteins - metabolism Residues Saliva Sodium Streptococcal adherence Streptococcus Streptococcus infections Streptococcus mutans Streptococcus mutans - immunology
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