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The influence of truncating the carboxy-terminal amino acid residues of streptococcal enolase on its ability to interact with canine plasminogen


The influence of truncating the carboxy-terminal amino acid residues of streptococcal enolase on its ability to interact with canine plasminogen

Deshmukh, Sasmit S., Kornblatt, M. Judith and Kornblatt, Jack A. ORCID: https://orcid.org/0000-0002-9802-8321 (2019) The influence of truncating the carboxy-terminal amino acid residues of streptococcal enolase on its ability to interact with canine plasminogen. PLOS ONE, 14 (1). e0206338. ISSN 1932-6203

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Official URL: http://dx.doi.org/10.1371/journal.pone.0206338


The native octameric structure of streptococcal enolase from Streptococcus pyogenes increasingly dissociates as amino acid residues are removed one by one from the carboxy-terminus. These truncations gradually convert native octameric enolase into monomers and oligomers. In this work, we investigated how these truncations influence the interaction between Streptococcal enolase and canine plasminogen. We used dual polarization interferometry (DPI), localized surface plasmon resonance (LSPR), and sedimentation velocity analytical ultracentrifugation (AUC) to study the interaction. The DPI was our first technique, was performed on all the truncations and used one exclusive kind of chip. The LSRP was used to show that the DPI results were not dependent on the type of chip used. The AUC was required to show that our surface results were not the result of selecting a minority population in any given sample; the majority of the protein was responsible for the binding phenomenon we observed. By comparing results from these techniques we identified one detail that is essential for streptococcal enolase to bind plasminogen: In our hands the individual monomers bind plasminogen; dimers, trimers, tetramers may or may not bind, the fully intact, native, octamer does not bind plasminogen. We also evaluated the contribution to the equilibrium constant made by surface binding as well as in solution. On a surface, the association coefficient is about twice that in solution. The difference is probably not significant. Finally, the fully octameric form of the protein that does not contain a hexa-his N-terminal peptide does not bind to a silicon oxynitride surface, does not bind to an Au-nanoparticle surface, does not bind to a surface coated with Ni-NTA nor does it bind to a surface coated with DPgn. The likelihood is great that the enolase species on the surface of Streptococcus pyogenes is an x-mer of the native octamer.

Divisions:Concordia University > Faculty of Arts and Science > Biology
Item Type:Article
Authors:Deshmukh, Sasmit S. and Kornblatt, M. Judith and Kornblatt, Jack A.
Journal or Publication:PLOS ONE
  • Concordia Open Access Author Fund
  • Natural Sciences and Engineering Research Council of Canada, Grant Number 9988-2006
Digital Object Identifier (DOI):10.1371/journal.pone.0206338
ID Code:985057
Deposited By: Krista Alexander
Deposited On:13 Mar 2019 20:06
Last Modified:13 Mar 2019 20:06


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