Journal
PLOS ONE
Volume 6, Issue 10, Pages -Publisher
PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pone.0024886
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Funding
- Biotechnology and Biological Sciences Research Council under the Selective Chemical Intervention in Biological Systems initiative [BB/D005469/1]
- Medical Research Council, United Kingdom [U117584248]
- Biotechnology and Biological Sciences Research Council [BB/D005469/1] Funding Source: researchfish
- Medical Research Council [G9721629, G0900950, G9721629B, MC_U117584248, G0900950B] Funding Source: researchfish
- BBSRC [BB/D005469/1] Funding Source: UKRI
- MRC [G9721629, G0900950, MC_U117584248] Funding Source: UKRI
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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.
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