The interaction of streptococcal enolase with canine plasminogen: the role of surfaces in complex formation.

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ID: 74254
2014
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Abstract
The enolase from Streptococcus pyogenes (Str enolase F137L/E363G) is a homo-octamer shaped like a donut. Plasminogen (Pgn) is a monomeric protein composed of seven discrete separated domains organized into a lock washer. The enolase is known to bind Pgn. In past work we searched for conditions in which the two proteins would bind to one another. The two native proteins in solution would not bind under any of the tried conditions. We found that if the structures were perturbed binding would occur. We stated that only the non-native Str enolase or Pgn would interact such that we could detect binding. We report here the results of a series of dual polarization interferometry (DPI) experiments coupled with atomic force microscopy (AFM), isothermal titration calorimetry (ITC), dynamic light scattering (DLS), and fluorescence. We show that the critical condition for forming stable complexes of the two native proteins involves Str enolase binding to a surface. Surfaces that attract Str enolase are a sufficient condition for binding Pgn. Under certain conditions, Pgn adsorbed to a surface will bind Str enolase.
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balhara2014theplos Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Balhara, Vinod;Deshmukh, Sasmit S;Kálmán, László;Kornblatt, Jack A;
Journal PloS one
Year 2014
DOI
DOI not found
URL
http://europepmc.org/articles/PMC3919783?pdf=render
Keywords
chemistry Medicine Materials of engineering and construction. Mechanics of materials Technology (General) Chemical technology Technology Science textile bleaching, dyeing, printing, etc.

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