Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0024530 (malaria)
 44,886 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The HAINAN isolate of Plasmodium falciparum FCC1/HN was cultured in vitro in large quantities. The total parasite mRNA was purified and reverse transcribed into cDNA. The cDNA fragments were inserted into lambda gt11 to construct a P. falciparum FCC1/HN erythrocytic stage cDNA library. Inhibitory monoclonal antibodies (McAbs) M26-32, F6-C2, and F6-D3 were used to screen the cDNA library expressed in E. coli. A total of 27 positive clones were found to react with M26-32 alone and 34 clones with both M26-32 and F6-C2. These expressed proteins may be candidates for use in malaria vaccine.
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PMID:Construction and screening of Plasmodium falciparum cDNA library. 249 16

A DNA fragment, designated as P190TR, encoding amino acid residues of the tripeptide region of the P190 antigen was amplified by polymerase chain reaction from genomic DNA of FCC1/HN Plasmodium falciparum isolated from Hainan Province, China. Upon comparison with the nucleotide sequences of MAD20 allele, it was found that there were five bases substitution in the P190TR which cause amino acid changes. The DNA fragment sequenced were ligated to BamHI and XbaI-digested pGEX-2T vector. Competent E. coli JM109 (DE3) were transformed with either parental or recombinant pGEX-2T for expression. Analysis of soluble cellular proteins revealed the high level expression of GST-P190TR as fusion proteins. Affinity purification of the fusion protein under nondenaturing condition resulted in the removal of almost all other E. coli proteins. The purified P190TR protein was highly immunogenic in rabbits. The antibodies against the recombinant protein recognized the malaria parasite with the titers at 1:320 measured by IFA and antisera from malarial patients reacted with the expressed protein in Western Blot.
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PMID:Expression and immunogenicity of tripeptide repeat region on P190 of Plasmodium falciparum. 778 21

A Plasmodium falciparum chimeric protein 2.9 (PfCP-2.9) was constructed consisting of the C-terminal regions of two leading malaria vaccine candidates, domain III of apical membrane ag-1 (AMA-1) and 19-kDa C-terminal fragment of the merozoite surface protein 1 (MSP1). The PfCP-2.9 was produced by Pichia pastoris in secreted form with a yield of 2600 mg/L and approximately 1 g/L of final product was obtained from a three-step purification process. Analysis of conformational properties of the chimeric protein showed that all six conformational mAbs interacted with the recombinant protein were reduction-sensitive, indicating that fusion of the two cysteine-rich proteins retains critical conformational epitopes. PfCP-2.9 was found to be highly immunogenic in rabbits as well as in rhesus monkeys (Macaca mulatta). The chimeric protein induced both anti-MSP1-19 and anti-AMA-1(III) Abs at levels 11- and 18-fold higher, respectively, than individual components did. Anti-PfCP-2.9 sera from both rabbits and rhesus monkeys almost completely inhibited in vitro growth of the P. falciparum FCC1/HN and 3D7 lines when tested at a 6.7-fold dilution. It was shown that the inhibition is dependent on the presence of Abs to the chimeric protein and their disulfide bond-dependent conformations. Moreover, the activity was mediated by a combination of growth-inhibitory Abs generated by the individual MSP1-19 and AMA-1(III) of PfCP-2.9. The combination of the extremely high yield of the protein and enhancement of its immune response provides a basis to develop an effective and affordable malaria vaccine.
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PMID:Fusion of two malaria vaccine candidate antigens enhances product yield, immunogenicity, and antibody-mediated inhibition of parasite growth in vitro. 1512 4