| http://purl.uniprot.org/citations/25359607 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/25359607 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/25359607 | http://www.w3.org/2000/01/rdf-schema#comment | "Mycobacterium tuberculosis, the primary causative agent of tuberculosis, infects macrophages and transforms the hostile intracellular environment into a permissive niche. M. tuberculosis infects macrophages using a variety of microbial ligand/cell receptor systems. In this study, binding assays with biotin-labelled mycobacterial cell wall proteins revealed five Concanavalin A-reactive proteins that bind macrophages. Among these proteins, we identified PstS-1, a 38-kDa M. tuberculosis mannosylated glycolipoprotein, and characterized it as an adhesin. Inhibition assays with mannan and immunoprecipitation demonstrated that PstS-1 binds the mannose receptor. We purified PstS-1 to 95.9% purity using ion exchange chromatography. The presence of mannose in purified PstS-1 was demonstrated by Concanavalin A interaction, which was abolished in the presence of sodium m-periodate and α-D-mannosidase. Gas chromatography revealed that purified PstS-1 contained 1% of carbohydrates by weight, which was mainly mannose. Finally, we used fluorescent microbeads coated with purified PstS-1 in phagocytosis assays and discovered that microbead uptake was inhibited by the pre-incubation of cells with GlcNAc, mannan and α-methyl mannoside. The interaction of PstS-1 coated beads with the mannose receptor was confirmed by confocal colocalization studies that showed high Pearson and Manders's colocalization coefficients. Our findings contribute to a better understanding of the strategies M. tuberculosis uses to infect host cells, the critical first step in the pathogenesis of tuberculosis."xsd:string |
| http://purl.uniprot.org/citations/25359607 | http://purl.org/dc/terms/identifier | "doi:10.1111/sji.12249"xsd:string |
| http://purl.uniprot.org/citations/25359607 | http://purl.org/dc/terms/identifier | "doi:10.1111/sji.12249"xsd:string |
| http://purl.uniprot.org/citations/25359607 | http://purl.uniprot.org/core/author | "Esparza M."xsd:string |
| http://purl.uniprot.org/citations/25359607 | http://purl.uniprot.org/core/author | "Esparza M."xsd:string |
| http://purl.uniprot.org/citations/25359607 | http://purl.uniprot.org/core/author | "Espinosa P."xsd:string |
| http://purl.uniprot.org/citations/25359607 | http://purl.uniprot.org/core/author | "Espinosa P."xsd:string |
| http://purl.uniprot.org/citations/25359607 | http://purl.uniprot.org/core/author | "Garcia T."xsd:string |
| http://purl.uniprot.org/citations/25359607 | http://purl.uniprot.org/core/author | "Garcia T."xsd:string |
| http://purl.uniprot.org/citations/25359607 | http://purl.uniprot.org/core/author | "Mancilla R."xsd:string |
| http://purl.uniprot.org/citations/25359607 | http://purl.uniprot.org/core/author | "Mancilla R."xsd:string |
| http://purl.uniprot.org/citations/25359607 | http://purl.uniprot.org/core/author | "Palomares B."xsd:string |
| http://purl.uniprot.org/citations/25359607 | http://purl.uniprot.org/core/author | "Palomares B."xsd:string |
| http://purl.uniprot.org/citations/25359607 | http://purl.uniprot.org/core/author | "Zenteno E."xsd:string |
| http://purl.uniprot.org/citations/25359607 | http://purl.uniprot.org/core/author | "Zenteno E."xsd:string |
| http://purl.uniprot.org/citations/25359607 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
| http://purl.uniprot.org/citations/25359607 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
| http://purl.uniprot.org/citations/25359607 | http://purl.uniprot.org/core/name | "Scand. J. Immunol."xsd:string |
| http://purl.uniprot.org/citations/25359607 | http://purl.uniprot.org/core/name | "Scand. J. Immunol."xsd:string |
| http://purl.uniprot.org/citations/25359607 | http://purl.uniprot.org/core/pages | "46-55"xsd:string |
| http://purl.uniprot.org/citations/25359607 | http://purl.uniprot.org/core/pages | "46-55"xsd:string |
| http://purl.uniprot.org/citations/25359607 | http://purl.uniprot.org/core/title | "PstS-1, the 38-kDa Mycobacterium tuberculosis glycoprotein, is an adhesin, which binds the macrophage mannose receptor and promotes phagocytosis."xsd:string |
| http://purl.uniprot.org/citations/25359607 | http://purl.uniprot.org/core/title | "PstS-1, the 38-kDa Mycobacterium tuberculosis glycoprotein, is an adhesin, which binds the macrophage mannose receptor and promotes phagocytosis."xsd:string |