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... More
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.
