Disease relevance of MSP1

• MATERIALS AND METHODS: Two recombinant proteins from the carboxy-terminus of MSP1, the 42 kD fused to GST (bMSP1(42)) and the 19 kD (yMSP1(19)), were expressed in Escherichia coli and secreted from Saccharomyces cerevisiae, respectively [1].

High impact information on MSP1

• The mechanism of immunity is unclear, although data show that cell-mediated immunity plays a critical role following immunization with the larger mature MSP1 protein [2].
• The MSP1 gene is not essential for the cell growth either on fermentable or nonfermentable carbon sources [3].
• Intramitochondrial protein sorting. Isolation and characterization of the yeast MSP1 gene which belongs to a novel family of putative ATPases [3].
• MSP1 was found to be an intrinsic mitochondrial outer membrane protein of an apparent molecular mass of 40 kDa with a large domain facing to the cytosol [3].
• Further sequence analyses revealed that MSP1 is a member of a novel family of putative ATPases which share a highly conserved domain of about 185 amino acid residues, including a consensus motif for a nucleotide binding site [3].

Biological context of MSP1

• The MSP-1 gene was identified using universal genome walking [4].
• A multigene family that interacts with the amino terminus of plasmodium MSP-1 identified using the yeast two-hybrid system [5].

Anatomical context of MSP1

• P30P2MSP1(19) consists of two universal T-cell epitopes fused to the most C-terminal 19-kDa portion of MSP1, and this protein has previously shown promising potential as a vaccine for malaria [6].

Associations of MSP1 with chemical compounds

• We isolated a novel yeast gene MSP1 (mitochondrial sorting of proteins) whose overexpression causes mislocalization of the 61mC1 fusion protein to the inner membrane, probably via the intermembrane space, and thereby allows the host cells to grow on glycerol [3].
• Four antigenic variants of the 19-kDa carboxy terminal fragment of Plasmodium falciparum merozoite surface protein, MSP1 (MSP1(19)), were expressed in Saccharomyces cerevisiae as a histidine-tagged, secreted polypeptides (rMSP1(19)s) [7].

Other interactions of MSP1

• 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) [8].
• In vitro binding experiments confirmed the interaction between MSRP-1, MSRP-2, and the amino-terminal region of P. falciparum MSP-1 [5].

Analytical, diagnostic and therapeutic context of MSP1

• In the MSP1 and control groups, protection correlated with antibody to MSP3 raised by challenge infection [9].
• Immunofluorescence studies colocalized P. yoelii MSP-7 and P. yoelii MSRP-2 with the amino-terminal portion of MSP-1 and with each other on the surface of schizonts [10].

References