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Volume 144, Issue 4

Affinity purification and characterization of a fibrinogen-binding protein complex which protects mice against lethal challenge with Streptococcus Free

Abstract

Cell-wall-associated proteins from subsp. , the causative agent of strangles, were analysed with a view to identifying a potential protective antigen. Preparations of these proteins, isolated from mutanolysin extracts of cell walls, were shown to contain one major high- protein species (apparent 220000 and 550000 when analysed by SDS-PAGE and gel-filtration chromatography, respectively). The high- protein bound horse fibrinogen and was purified under non-denaturing conditions using fibrinogen affinity chromatography. The fibrinogen-binding protein (FgBP) reacted with serum taken from horses recovering from strangles and protected mice against lethal challenge from subsp. . The sequence of the corresponding gene () was determined and shown to encode a mature protein ( 54597) with predicted coiled-coil structure. An FgBP truncate, lacking the C-terminal cell wall/membrane anchor domain, was overexpressed in and purified from and was shown to behave in an analogous fashion to the wild-type product in terms of estimation, fibrinogen binding and seroreactivity.

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Keyword(s): equi , fibrinogen-binding protein , protective antigen and Streptococcus equisubsp
© Society for General Microbiology 1998
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1998-04-01
2024-04-16
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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
Microbiology 144, 993 (1998); https://doi.org/10.1099/00221287-144-4-993
/content/journal/micro/10.1099/00221287-144-4-993
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