Cell Surface Antigens of Mycoplasma Species Bovine Group 7 Bind to and Activate Plasminogen

Author:

Bower Kylie12,Djordjevic Steven P.2,Andronicos Nicholas M.1,Ranson Marie1

Affiliation:

1. Department of Biological Sciences, University of Wollongong, Wollongong, New South Wales 2522

2. NSW Agriculture, Elizabeth Macarthur Agricultural Institute, Camden, New South Wales 2570, Australia

Abstract

ABSTRACT Mycoplasma species bovine group 7 bound plasminogen at the cell surface in a lysine-dependent manner. Cell-bound plasminogen was rapidly activated to plasmin by exogenous urokinase, and this activity was associated with plasminogen binding capacity. Binding assays using plasminogen modified with a trifunctional cross-linking agent revealed several binding proteins.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Immunology,Microbiology,Parasitology

Reference36 articles.

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2. Andronicos, N. M., M. Ranson, J. Bognacki, and M. S. Baker. 1997. The human ENO1 gene product (recombinant human α-enolase) displays the characteristics required for a plasminogen binding protein. Biochem. Biophys. Acta1337:27-39.

3. Broeseker, J. A., M. D. Boyle, and R. Lottenberg. 1988. Characterisation of the interactions of human plasmin with its specific receptor on a group A streptococcus. Microb. Pathog.5:19-27.

4. Castellino F. J. 1995. Plasminogen p. 495-510. In K. A. High and H. R. Roberts (ed.) Molecular basis of thrombosis and hemostasis. Marcel Dekker Inc. New York N.Y.

5. Coleman, J. L., and J. L. Benach. 1999. Use of the plasminogen activation system by microorganisms. J. Lab. Clin. Med.134:567-576.

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