Isolation and characterization of a Streptococcus pyogenes protein that binds to basal laminae of human cardiac muscle
| Autor: | B. D. Winters, M. W. Stinson, Narayanan Ramasubbu |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
Streptococcus pyogenes
Molecular Sequence Data Immunology Biology medicine.disease_cause Microbiology Basement Membrane Mice Bacterial Proteins Affinity chromatography medicine Animals Humans Amino Acid Sequence Amino Acids Tyrosine Peptide sequence Histidine Glycosaminoglycans Alanine chemistry.chemical_classification Circular Dichroism Myocardium Binding protein Amino acid Infectious Diseases Biochemistry chemistry Parasitology Rabbits Carrier Proteins Research Article |
| Zdroj: | Infection and Immunity. 61:3259-3264 |
| ISSN: | 1098-5522 0019-9567 |
| DOI: | 10.1128/iai.61.8.3259-3264.1993 |
| Popis: | A 9-kDa glycosaminoglycan-binding protein (GAG-BP) was isolated from Streptococcus pyogenes and purified to homogeneity by affinity chromatography on heparin-agarose. The protein selectively bound to the basal laminae of human cardiac muscle and had an apparent dissociation constant of 2.5 x 10(-7) M. Chemical analyses indicated that the GAG-BP was rich in alanine, lysine, and arginine (pI 9.5) and devoid of tyrosine, methionine, histidine, and half-cystine. There were no detectable carbohydrate or phosphate substituents. The amino acid sequence of the N terminus of GAG-BP showed homology with those of histone-like DNA-binding proteins of several other bacteria. Circular dichroism spectroscopy indicated that the protein was made up of 50% beta-sheet and 50% beta-turn and random coil in aqueous solution; however, when the protein complexed with heparin, it adopted a more ordered structure containing 25% alpha-helix, 50% beta-sheet, and 25% beta-turn and random coil. The GAG-BP cross-reacted serologically with a component of similar size in extracts of other group A streptococci and was present in the culture medium during late logarithmic growth. |
| Databáze: | OpenAIRE |
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