| http://purl.uniprot.org/citations/16319056 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16319056 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16319056 | http://www.w3.org/2000/01/rdf-schema#comment | "Group A streptococci (GAS) display receptors for the human zymogen plasminogen on the cell surface, one of which is the plasminogen-binding group A streptococcal M protein (PAM). Characterization of PAM genes from 12 GAS isolates showed significant variation within the plasminogen-binding repeat motifs (a1/a2) of this protein. To determine the impact of sequence variation on protein function, recombinant proteins representing five naturally occurring variants of PAM, together with a recombinant M1 protein, were expressed and purified. Equilibrium dissociation constants for the interaction of PAM variants with biotinylated Glu-plasminogen ranged from 1.58 to 4.99 nm. Effective concentrations of prototype PAM required for 50% inhibition of plasminogen binding to immobilized PAM variants ranged from 0.68 to 22.06 nm. These results suggest that although variation in the a1/a2 region of the PAM protein does affect the comparative affinity of PAM variants, the functional capacity to bind plasminogen is conserved. Additionally, a potential role for the a1 region of PAM in eliciting a protective immune response was investigated by using a mouse model for GAS infection. The a1 region of PAM was found to protect immunized mice challenged with a PAM-positive GAS strain. These data suggest a link between selective immune pressure against the plasminogen-binding repeats and the functional conservation of the binding domain in PAM variants."xsd:string |
| http://purl.uniprot.org/citations/16319056 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.M508758200"xsd:string |
| http://purl.uniprot.org/citations/16319056 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m508758200"xsd:string |
| http://purl.uniprot.org/citations/16319056 | http://purl.uniprot.org/core/author | "Walker M.J."xsd:string |
| http://purl.uniprot.org/citations/16319056 | http://purl.uniprot.org/core/author | "Walker M.J."xsd:string |
| http://purl.uniprot.org/citations/16319056 | http://purl.uniprot.org/core/author | "Sriprakash K.S."xsd:string |
| http://purl.uniprot.org/citations/16319056 | http://purl.uniprot.org/core/author | "Sriprakash K.S."xsd:string |
| http://purl.uniprot.org/citations/16319056 | http://purl.uniprot.org/core/author | "Ranson M."xsd:string |
| http://purl.uniprot.org/citations/16319056 | http://purl.uniprot.org/core/author | "Ranson M."xsd:string |
| http://purl.uniprot.org/citations/16319056 | http://purl.uniprot.org/core/author | "Dowton M."xsd:string |
| http://purl.uniprot.org/citations/16319056 | http://purl.uniprot.org/core/author | "Dowton M."xsd:string |
| http://purl.uniprot.org/citations/16319056 | http://purl.uniprot.org/core/author | "Batzloff M."xsd:string |
| http://purl.uniprot.org/citations/16319056 | http://purl.uniprot.org/core/author | "Batzloff M."xsd:string |
| http://purl.uniprot.org/citations/16319056 | http://purl.uniprot.org/core/author | "Sanderson-Smith M."xsd:string |
| http://purl.uniprot.org/citations/16319056 | http://purl.uniprot.org/core/author | "Sanderson-Smith M."xsd:string |
| http://purl.uniprot.org/citations/16319056 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16319056 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16319056 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/16319056 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/16319056 | http://purl.uniprot.org/core/pages | "3217-3226"xsd:string |
| http://purl.uniprot.org/citations/16319056 | http://purl.uniprot.org/core/pages | "3217-3226"xsd:string |
| http://purl.uniprot.org/citations/16319056 | http://purl.uniprot.org/core/title | "Divergence in the plasminogen-binding group a streptococcal M protein family: functional conservation of binding site and potential role for immune selection of variants."xsd:string |
| http://purl.uniprot.org/citations/16319056 | http://purl.uniprot.org/core/title | "Divergence in the plasminogen-binding group a streptococcal M protein family: functional conservation of binding site and potential role for immune selection of variants."xsd:string |