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The Capital Region of Denmark - a part of Copenhagen University Hospital
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A Plasmodium falciparum 48/45 single epitope R0.6C subunit protein elicits high levels of transmission blocking antibodies

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The sexual stage Pfs48/45 antigen is a well-established lead candidate for a transmission blocking (TB) vaccine because of its critical role in parasite fertilization. We have recently produced the carboxy-terminal 10C-fragment of Pfs48/45 containing three known epitopes for TB antibodies as a chimera with the N-terminal region of GLURP (R0). The resulting fusion protein elicited high titer TB antibodies in rodents. To increase the relatively low yield of correctly folded Pfs48/45 we have generated a series of novel chimera truncating the 10C-fragments to 6 cysteine residues containing sub-units (6C). All constructs harbor the major epitope I for TB antibodies. One of these sub-units (R0.6Cc), produced high yields of correctly folded conformers, which could be purified by a simple 2-step procedure. Purified R0.6Cc was stable and elicits high titer TB antibodies in rats. The yield, purity and stability of R0.6Cc allows for further clinical development.

Original languageEnglish
JournalVaccine
Volume33
Issue number16
Pages (from-to)1981-6
Number of pages6
ISSN0264-410X
DOIs
Publication statusPublished - 15 Apr 2015

    Research areas

  • Animals, Antibodies, Blocking, Antibodies, Protozoan, Antigens, Protozoan, Epitopes, Gene Expression, Malaria, Falciparum, Plasmodium falciparum, Protozoan Proteins, Rats, Recombinant Fusion Proteins

ID: 45923781