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The Interaction of Canine Plasminogen with Streptococcus pyogenes Enolase: They Bind to One Another but What Is the Nature of the Structures Involved?

Title:

The Interaction of Canine Plasminogen with Streptococcus pyogenes Enolase: They Bind to One Another but What Is the Nature of the Structures Involved?

Kornblatt, M. Judith and Kornblatt, Jack A. and Hancock, Mark A. (2011) The Interaction of Canine Plasminogen with Streptococcus pyogenes Enolase: They Bind to One Another but What Is the Nature of the Structures Involved? PLoS ONE, 6 (12). e28481. ISSN 1932-6203

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Official URL: http://dx.doi.org/10.1371/journal.pone.0028481

Abstract

For years it has been clear that plasminogen from different sources and enolase from different sources interact strongly. What is less clear is the nature of the structures required for them to interact. This work examines the interaction between canine plasminogen (dPgn) and Streptococcus pyogenes enolase (Str enolase) using analytical ultracentrifugation (AUC), surface plasmon resonance (SPR), fluorescence polarization, dynamic light scattering (DLS), isothermal titration calorimetry (ITC), and simple pull-down reactions. Overall, our data indicate that a non-native structure of the octameric Str enolase (monomers or multimers) is an important determinant of its surface-mediated interaction with host plasminogen. Interestingly, a non-native structure of plasminogen is capable of interacting with native enolase. As far as we can tell, the native structures resist forming stable mixed complexes.

Divisions:Concordia University > Faculty of Arts and Science > Biology
Concordia University > Faculty of Arts and Science > Chemistry and Biochemistry
Item Type:Article
Refereed:Yes
Authors:Kornblatt, M. Judith and Kornblatt, Jack A. and Hancock, Mark A.
Journal or Publication:PLoS ONE
Date:2011
Funders:
  • Concordia Open Access Author Fund
ID Code:973694
Deposited By:ANDREA MURRAY
Deposited On:26 Mar 2012 15:30
Last Modified:22 Jan 2014 12:28
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