Differential requirement for cathepsin D for processing of the full length and C-terminal fragment of the malaria antigen MSP1.
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 contri...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2011-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3203867?pdf=render |
| _version_ | 1818244976446799872 |
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| author | Calogero Tulone Anne-Marit Sponaas Eun-Ang Raiber Alethea B Tabor Jean Langhorne Benny M Chain |
| author_facet | Calogero Tulone Anne-Marit Sponaas Eun-Ang Raiber Alethea B Tabor Jean Langhorne Benny M Chain |
| author_sort | Calogero Tulone |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-12T14:25:34Z |
| format | Article |
| id | doaj.art-7b58bf8ea2bf4d40afa15c700c3a164a |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-12T14:25:34Z |
| publishDate | 2011-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-7b58bf8ea2bf4d40afa15c700c3a164a2022-12-22T00:21:41ZengPublic Library of Science (PLoS)PLoS ONE1932-62032011-01-01610e2488610.1371/journal.pone.0024886Differential requirement for cathepsin D for processing of the full length and C-terminal fragment of the malaria antigen MSP1.Calogero TuloneAnne-Marit SponaasEun-Ang RaiberAlethea B TaborJean LanghorneBenny M ChainMerozoite 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.http://europepmc.org/articles/PMC3203867?pdf=render |
| spellingShingle | Calogero Tulone Anne-Marit Sponaas Eun-Ang Raiber Alethea B Tabor Jean Langhorne Benny M Chain Differential requirement for cathepsin D for processing of the full length and C-terminal fragment of the malaria antigen MSP1. PLoS ONE |
| title | Differential requirement for cathepsin D for processing of the full length and C-terminal fragment of the malaria antigen MSP1. |
| title_full | Differential requirement for cathepsin D for processing of the full length and C-terminal fragment of the malaria antigen MSP1. |
| title_fullStr | Differential requirement for cathepsin D for processing of the full length and C-terminal fragment of the malaria antigen MSP1. |
| title_full_unstemmed | Differential requirement for cathepsin D for processing of the full length and C-terminal fragment of the malaria antigen MSP1. |
| title_short | Differential requirement for cathepsin D for processing of the full length and C-terminal fragment of the malaria antigen MSP1. |
| title_sort | differential requirement for cathepsin d for processing of the full length and c terminal fragment of the malaria antigen msp1 |
| url | http://europepmc.org/articles/PMC3203867?pdf=render |
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