Localization and characterization of the ligand-binding domain of the fibrinogen-binding protein (FgBP) of Streptococcus equi subsp. equi

Article Abstract:

Streptococcus equi subsp. equi. is discussed relative to characterization and localization of the ligand-binding domain of the fibrinogen-binding protein (FgBP). The protein is cell-wall-associated and binds horse fibrinogen (Fg). It reacts with convalescent horse serum and protects against lethal S. equi challenge in a small animal model. It has been found that the region needed for maximum binding of Fg extends over the first half of the mature protein.

Observations, Cytochemistry, Bacterial cell walls, Ligand binding (Biochemistry), Gram-positive bacteria, Bacterial proteins

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The fibrinogen-binding protein (FgBP) of Streptococcus equi subsp. equi additionally binds IgG and contributes to virulence in a mouse model

Article Abstract:

Research has been conducted on the M-like fibrinogen-binding protein of the equine pathogen Streptococcus equi subsp. equi which binds equine fibrinogen. Results indicate that this protein additionally binds equine IgG-Fc.

Statistical Data Included, Analysis, Genetic aspects, Microbiological research

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Affinity purification and characterization of a fibrinogen-binding protein complex which protects mice against lethal challenge with streptococcus equi subsp. equi

Article Abstract:

The fibrinogen binding protein (FgBP) of Streptococcus equi subspecies equi, the causative agent of equine strangle, is a promising antigen in vaccine research. FgBP has been purified using affinity techniques. The purified protein was bound by serum from horses recovering from strangle and protected mice from contracting the disease. The gene coding for FgBP has been identified and cloned. Genetic engineering methods have been uilized to express this protein in Escherichia coli.

Bacterial antigens, O antigens

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