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National Pharmaceutical Biotechnology Centre, BioResearch Ireland
Department of Microbiology, Moyne Institute of Preventive Medicine
Bioresources Unit Trinity College, Dublin 2, Ireland
ABSTRACT
Cell-wall-associated proteins from Streptococcus equi subsp. equi, 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-Mr protein species (apparent Mr 220000 and 550000 when analysed by SDS-PAGE and gel-filtration chromatography, respectively). The high-Mr 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 S. equi subsp. equi. The sequence of the corresponding gene (fbp) was determined and shown to encode a mature protein (Mr 54597) with predicted coiled-coil structure. An FgBP truncate, lacking the C-terminal cell wall/membrane anchor domain, was overexpressed in and purified from Escherichia coli and was shown to behave in an analogous fashion to the wild-type product in terms of Mr estimation, fibrinogen binding and seroreactivity.
*Author for correspondence: Peter Owen. Tel: +35 3 1 6081188. Fax: +35 3 1 6799294. e-mail: powen@tcd.ie
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