During characterization of the surface antigens of serotype III group B streptococci (GBS), a protein with an apparent M(r) of approximately 173,500 migrating on a SDS--polyacrylamide gel was found to have an N-terminal amino acid sequence identical to that of the plasmin receptor (Plr) of group A streptococci, a surface-localized glyceraldehyde-3-phosphate dehydrogenase (GAPDH). This work begins to characterize GBS GAPDH and to assess its functional activity on the cell surface. The 1.0-kb gapC gene of GBS was amplified by PCR. plr and gapC demonstrated 87% homology. An anti-Plr monoclonal antibody reacted with GBS whole cells, suggesting GBS GAPDH is surface localized. Multiple serotypes of GBS demonstrated functional GAPDH on their surfaces. The anti-Plr monoclonal antibody recognized GBS protein bands of approximately 41 and 173.5 kDa, by Western blot. Presumably, these represent monomeric and tetrameric forms of the GAPDH molecule. GBS GAPDH was demonstrated by Western blot analysis to interact with lys- and glu-plasminogens. Fluid-phase GBS GAPDH interacted, by means of ELISA, with immobilized lys-plasminogen, glu-plasminogen, actin, and fibrinogen. Enzymatically active GAPDH, capable of binding cytoskeletal and extracellular matrix proteins, is expressed on the surface of GBS.
"Alcohol acetaldehyde dehydrogenase/Listeria adhesion protein (LAP) enables Listeria monocytogenes to bind to intestinal epithelial cells and aids in infection (Jagadeesan et al., 2010). Enolase (Knaust et al., 2007; Agarwal et al., 2008; Castaldo et al., 2009), phosphoglycerate kinase (Boone et al., 2011; Fulde et al., 2013), and glyceraldehyde 3-phosphate dehydrogenase (Pancholi and Fischetti, 1992; Seifert et al., 2003; Bergmann et al., 2004; Jobin et al., 2004; Barbosa et al., 2006; Hurmalainen et al., 2007; Matta et al., 2010) are cytosolic enzymes that have a second role in pathogenic bacteria as a cell surface receptor for collagen, fibronectin, or plasminogen (Figure 1C). "
"Its role in pathogenicity has been analyzed using a variety of in vivo and ex vivo infection models (Pancholi and Fischetti, 1998; Pancholi and Chhatwal, 2003; Bergmann et al., 2005, 2013; Agarwal et al., 2012). In addition, many moonlighting proteins have been characterized as adhesive molecules mediating streptococcal binding to proteins of the extracellular matrix (ECM) like fibronectin (Table 1) (Pancholi and Fischetti, 1992; Seifert et al., 2003; Bergmann and Hammerschmidt, 2006; Esgleas et al., 2008; Paterson and Orihuela, 2010; Bernardo-Garcia et al., 2011; Voss et al., 2012). This interaction promotes the contact of the bacteria with epithelial and endothelial cell surfaces (Esgleas et al., 2008) and contributes to bacterial colonization of host niches. "
[Show abstract][Hide abstract] ABSTRACT: The ability to take advantage of plasminogen and its activated form plasmin is a common mechanism used by commensal as well as pathogenic bacteria in interaction with their respective host. Hence, a huge variety of plasminogen binding proteins and activation mechanisms exist. This review solely focuses on the genus Streptococcus and, in particular, on the so-called non-activating plasminogen binding proteins. Based on structural and functional differences, as well as on their mode of surface linkaging, three groups can be assigned: M-(like) proteins, surface displayed cytoplasmatic proteins with enzymatic activities ("moonlighting proteins") and other surface proteins. Here, the plasminogen binding sites and the interaction mechanisms are compared. Recent findings on the functional consequences of these interactions on tissue degradation and immune evasion are summarized.
Frontiers in Cellular and Infection Microbiology 11/2013; 3:85. DOI:10.3389/fcimb.2013.00085 · 3.72 Impact Factor
"GAPDH of S. pyogenes and S. pneumoniae binds preferentially to Lys-plasminogen and plasmin, and this interaction is mediated by the C-terminal lysine residue in GAPDH . Interestingly, it has been shown that GAPDH of group B streptococcus interacts with both Glu-and Lys-plasminogen but not plasmin . "
[Show abstract][Hide abstract] ABSTRACT: Multiple species of bacteria are able to sequester the host zymogen plasminogen to the cell surface. Once localised to the bacterial surface, plasminogen can act as a cofactor in adhesion, or, following activation to plasmin, provide a source of potent proteolytic activity. Numerous bacterial plasminogen receptors have been identified, and the mechanisms by which they interact with plasminogen are diverse. Here we provide an overview of bacterial plasminogen receptors and discuss the diverse role bacterial plasminogen acquisition plays in the relationship between bacteria and the host.
BioMed Research International 10/2012; 2012(10):272148. DOI:10.1155/2012/272148 · 2.71 Impact Factor
Data provided are for informational purposes only. Although carefully collected, accuracy cannot be guaranteed. The impact factor represents a rough estimation of the journal's impact factor and does not reflect the actual current impact factor. Publisher conditions are provided by RoMEO. Differing provisions from the publisher's actual policy or licence agreement may be applicable.