Post-translational signal peptide cleavage controls differential epitope recognition in the QP-rich domain of recombinant Theileria parva PIM
The presence of the schizont stage of the obligate intracellular parasites Theileria parva or T. annulata in the cytoplasm of an infected leukocyte results in host cell transformation via a mechanism that has not yet been elucidated. Proteins, secreted by the schizont, or expressed on its surface, a...
| Main Authors: | , , , |
|---|---|
| Format: | Journal Article |
| Language: | Inglés |
| Published: |
Elsevier
2006
|
| Subjects: | |
| Online Access: | https://hdl.handle.net/10568/33057 |
Similar Items: Post-translational signal peptide cleavage controls differential epitope recognition in the QP-rich domain of recombinant Theileria parva PIM
- Fusion of a cell penetrating peptide from HIV-1 TAT to the Theileria parva antigen Tp2 enhances the stimulation of bovine CD8+ T cell responses
- A membrane-anchored Theileria parva cyclophilin with a non-cleaved amino-terminal signal peptide for entry into the endoplasmic reticulum
- Impaired expressions of the beta and delta isoforms of vacuolar processing enzymes compromise the basal defenses of Arabidopsis thaliana against the phloem-feeding insect Myzus persicae
- Evaluation of T cell recognition of theileria parva homologs of apicomplexan antigens.
- Potato Snakin-1 Gene Silencing Affects Cell Division, Primary Metabolism, and Cell Wall Composition
- Blood parasitic diseases and specific immune responses