Journal article
Interaction between two domains of the P. yoelii MSP-1 protein detected using the yeast two-hybrid system
Molecular and biochemical parasitology, Vol.117(1), pp.27-35
2001
PMID: 11551629
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Several model systems of plasmodia have demonstrated the potential of the merozoite surface protein, MSP-1, to induce protective immunity. However, little is known about the function of this protein or its interaction with other surface molecules that may also serve as immunological targets. To identify potentially significant inter- and intra-molecular interactions involving MSP-1, we have utilized the yeast two-hybrid system. A cDNA activation domain library was constructed from the erythrocytic stages of the murine malarial parasite
Plasmodium yoelii yoelii 17XL. A 795 bp region of Py17XL MSP-1 (bait), homologous to the
Plasmodium falciparum MSP1
33 fragment, was inserted into a Gal4p DNA binding domain vector and used to screen the activation domain library (target). Several randomly selected clones that demonstrated bait-target interaction were found to express overlapping regions of Py17XL MSP-1. Deletion constructs further localized the peptide fragments retaining interaction indicating that a region within the MSP-1
38 fragment interacts with the MSP-1 bait domain. Subsequent studies confirmed this interaction, as both peptides were co-precipitated from cell lysate by a peptide tag-specific antibody. It was observed that the interaction of these two fragments significantly increased the half-life of the MSP-1
38 within yeast cells. The specific interaction described here demonstrates the potential of this approach to elucidate additional inter- or intra-molecular interactions of Py17XL MSP1 and other malarial proteins.
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Details
- Title
- Interaction between two domains of the P. yoelii MSP-1 protein detected using the yeast two-hybrid system
- Creators
- Thomas M DalyCarole A LongLawrence W Bergman
- Publication Details
- Molecular and biochemical parasitology, Vol.117(1), pp.27-35
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- [Retired Faculty]; Microbiology and Immunology
- Identifiers
- 991014878512104721
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- Web of Science research areas
- Biochemistry & Molecular Biology
- Parasitology