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Characterisation of the plasmin receptor(s) of Streptococcus uberis

Reference	BBS/E/I/00000752
Principal Investigator / Supervisor	Professor James Leigh
Co-Investigators / Co-Supervisors
Institution	The Pirbright Institute
Department	The Pirbright Institute Department
Funding type	Research
Value (£)	59,510
Status	Completed
Type	Institute Project
Start date	14/11/1998
End date	13/11/2001
Duration	36 months

Abstract

Plasminogen can be activated to plasmin (a serine protease) by both S.uberis and S.dysgalactiae. Growth of either S.uberis or S.dysgalactiae in media containing bovine plasminogen results in the association of plasmin with the bacterial cells. Both bacteria were less able to bind plasminogen suggesting that activation of plasminogen to plasmin takes place prior to binding. Plasmin binding to S.uberis can be disrupted by lysine and lysine analogues and bound plasmin is more resistant to inhibition by natural protease inhibitors. The consequence of S.uberis and S.dysgalactiae binding plasmin in such a fashion is that they acquire an unregulated host protease which may have many roles in pathogenesis, not least the supply of peptides and amino acids for bacterial growth. A gene homologous to that encoding a protein capable of binding plasmin (Plr) in S. pyogenes has been identified in S.uberis and S.dysglactiae. That from S. uberis will be cloned and expressed in E. coli to allow studies of its molecular character.

Summary

unavailable

Committee	Closed Committee - Animal Sciences (AS)
Research Topics	X – not assigned to a current Research Topic
Research Priority	X – Research Priority information not available
Research Initiative	X - not in an Initiative
Funding Scheme	X – not Funded via a specific Funding Scheme

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