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...
Saved in:
| Main Authors: | , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2011-01-01
|
| Series: | PLoS ONE |
| Online Access: | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0024886&type=printable |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1849333856908345344 |
|---|---|
| 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. |
| format | Article |
| id | doaj-art-7b58bf8ea2bf4d40afa15c700c3a164a |
| institution | Kabale University |
| issn | 1932-6203 |
| language | English |
| publishDate | 2011-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj-art-7b58bf8ea2bf4d40afa15c700c3a164a2025-08-20T03:45:44ZengPublic 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.https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0024886&type=printable |
| 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 | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0024886&type=printable |
| work_keys_str_mv | AT calogerotulone differentialrequirementforcathepsindforprocessingofthefulllengthandcterminalfragmentofthemalariaantigenmsp1 AT annemaritsponaas differentialrequirementforcathepsindforprocessingofthefulllengthandcterminalfragmentofthemalariaantigenmsp1 AT eunangraiber differentialrequirementforcathepsindforprocessingofthefulllengthandcterminalfragmentofthemalariaantigenmsp1 AT aletheabtabor differentialrequirementforcathepsindforprocessingofthefulllengthandcterminalfragmentofthemalariaantigenmsp1 AT jeanlanghorne differentialrequirementforcathepsindforprocessingofthefulllengthandcterminalfragmentofthemalariaantigenmsp1 AT bennymchain differentialrequirementforcathepsindforprocessingofthefulllengthandcterminalfragmentofthemalariaantigenmsp1 |