| First Author | Tulone C | Year | 2011 |
| Journal | PLoS One | Volume | 6 |
| Issue | 10 | Pages | e24886 |
| PubMed ID | 22053177 | Mgi Jnum | J:179691 |
| Mgi Id | MGI:5302900 | Doi | 10.1371/journal.pone.0024886 |
| Citation | Tulone C, et al. (2011) Differential requirement for cathepsin D for processing of the full length and C-terminal fragment of the malaria antigen MSP1. PLoS One 6(10):e24886 |
| abstractText | Merozoite Surface Protein 1 is expressed on the surface of malaria merozoites and is important for invasion of the malaria parasite into erythrocytes. MSP1-specific CD4 T cell responses and antibody can confer protective immunity in experimental models of malaria. In this study we explore the contributions of cathepsins D and E, two aspartic proteinases previously implicated in antigen processing, to generating MSP1 CD4 T-cell epitopes for presentation. The absence of cathepsin D, a late endosome/lysosomal enzyme, is associated with a reduced presentation of MSP1 both following in vitro processing of the epitope MSP1 from infected erythrocytes by bone marrow-derived dendritic cells, and following in vivo processing by splenic CD11c+ dendritic cells. By contrast, processing and presentation of the soluble recombinant protein fragment of MSP1 is unaffected by the absence of cathepsin D, but is inhibited when both cathepsin D and E are absent. The role of different proteinases in generating the CD4 T cell repertoire, therefore, depends on the context in which an antigen is introduced to the immune system. |
