Binding of group B streptococcal phosphoglycerate kinase to plasminogen and actin

Tyler J. Boone, Carey Ann D. Burnham, Gregory J. Tyrrell

Research output: Contribution to journalArticle

28 Scopus citations

Abstract

The glycolytic enzyme, phosphoglycerate kinase (PGK) of group B streptococci (GBS), has previously been identified as expressed on the GBS cell surface. The data presented describes the ability of group B streptococcal phosphoglycerate kinase (GBS-PGK) to bind to plasminogen and to bind actin. GBS-PGK binding to plasminogen was inhibited by the lysine analogue, 6-aminocaproic acid, suggesting plasminogen binding is achieved through GBS-PGK lysine residues. In addition to GBS-PGK surface expression, GBS-PGK was also found to be released from the bacterial cell suggesting GBS-PGK may affect its environment independent of GBS. To determine the effect of GBS-PGK on the actin cytoskeleton within a host cell, GBS-PGK attached to green fluorescent protein was transfected into and expressed in HeLa cells. Transfected GBS-PGK disrupted the actin cytoskeleton resulting in a compact or ovoid shaped HeLa cell rather than a typical epithelioid appearance.In conclusion, we have shown GBS-PGK binds to plasminogen and actin. We have also shown that GBS-PGK can be released from the bacterial cell and that transfected GBS-PGK can alter the epithelial cell cytoskeleton.

Original languageEnglish
Pages (from-to)255-261
Number of pages7
JournalMicrobial Pathogenesis
Volume51
Issue number4
DOIs
StatePublished - Oct 1 2011
Externally publishedYes

Keywords

  • Actin
  • Group B streptococcus
  • Phosphoglycerate kinase
  • Plasminogen

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