title: The interaction of streptococcal enolase with canine plasminogen: the role of surfaces in complex formation.
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.
authors: Department of Chemistry and Biochemistry, Concordia University, Montréal, Quebec, Canada.
authors: Vinod
authors: V
authors: Balhara
authors: Department of Physics, Concordia University, Montréal, Quebec, Canada.
authors: Sasmit S
authors: SS
authors: Deshmukh
authors: Department of Physics, Concordia University, Montréal, Quebec, Canada.
authors: László
authors: L
authors: Kálmán
authors: Department of Biology and the Centre for Structural and Functional Genomics, Concordia University, Montréal, Quebec, Canada.
authors: Jack A
authors: JA
authors: Kornblatt
mesh_terms: D000818:Animals; D002151:Calorimetry; D018360:Crystallography, X-Ray; D004285:Dogs; D004800:Enzymes, Immobilized / Q000378:metabolism; D005453:Fluorescence; D006801:Humans; D007368:Interferometry; D008027:Light; D018625:Microscopy, Atomic Force; D008958:Models, Molecular; D010715:Phosphatidylglycerols / Q000737:chemistry; D010751:Phosphopyruvate Hydratase / Q000737:chemistry / Q000378:metabolism*; D010958:Plasminogen / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D012542:Scattering, Radiation; D013297:Streptococcus pyogenes / Q000201:enzymology*; D013499:Surface Properties
chemical_list: D004800:Enzymes, Immobilized; D010715:Phosphatidylglycerols; C051388:1,2-dioleoyl-sn-glycero-3-phosphoglycerol; D010958:Plasminogen; D010751:Phosphopyruvate Hydratase