Defining the structural basis of human plasminogen binding by streptococcal surface enolase.

Cork, AJ; Jergic, S; Hammerschmidt, S; Kobe, B; Pancholi, V; Benesch, JL; Robinson, CV; Dixon, NE; Aquilina, JA; Walker, MJ

Abstract:

The flesh-eating bacterium group A Streptococcus (GAS) binds and activates human plasminogen, promoting invasive disease. Streptococcal surface enolase (SEN), a glycolytic pathway enzyme, is an identified plasminogen receptor of GAS. Here we used mass spectrometry (MS) to confirm that GAS SEN is octameric, thereby validating in silico modeling based on the crystal structure of Streptococcus pneumoniae alpha-enolase. Site-directed mutagenesis of surface-located lysine residues (SEN(K252 + 255A...

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APA Style

Cork, A. J., Jergic, S., Hammerschmidt, S., Kobe, B., Pancholi, V., Benesch, J. L., Robinson, C. V., Dixon, N. E., Aquilina, J. A., & Walker, M. J. (2009). Defining the structural basis of human plasminogen binding by streptococcal surface enolase. The Journal of Biological Chemistry, 284(25), 17129–17137.

MLA Style

Cork, A. J., et al. “Defining the Structural Basis of Human Plasminogen Binding by Streptococcal Surface Enolase.” The Journal of Biological Chemistry, vol. 284, no. 25, 2009, pp. 17129–37.

Chicago Style

Cork, AJ, S Jergic, S Hammerschmidt, B Kobe, V Pancholi, JL Benesch, CV Robinson, NE Dixon, JA Aquilina, and MJ Walker. 2009. “Defining the Structural Basis of Human Plasminogen Binding by Streptococcal Surface Enolase.” The Journal of Biological Chemistry 284 (25): 17129–37.
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