A Plasmodium falciparum 48/45 single epitope R0.6C subunit protein elicits high levels of transmission blocking antibodies

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A Plasmodium falciparum 48/45 single epitope R0.6C subunit protein elicits high levels of transmission blocking antibodies. / Singh, Susheel K; Roeffen, Will; Andersen, Gorm; Bousema, Teun; Christiansen, Michael; Sauerwein, Robert; Theisen, Michael.

In: Vaccine, Vol. 33, No. 16, 15.04.2015, p. 1981-6.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Singh, SK, Roeffen, W, Andersen, G, Bousema, T, Christiansen, M, Sauerwein, R & Theisen, M 2015, 'A Plasmodium falciparum 48/45 single epitope R0.6C subunit protein elicits high levels of transmission blocking antibodies', Vaccine, vol. 33, no. 16, pp. 1981-6. https://doi.org/10.1016/j.vaccine.2015.02.040

APA

Singh, S. K., Roeffen, W., Andersen, G., Bousema, T., Christiansen, M., Sauerwein, R., & Theisen, M. (2015). A Plasmodium falciparum 48/45 single epitope R0.6C subunit protein elicits high levels of transmission blocking antibodies. Vaccine, 33(16), 1981-6. https://doi.org/10.1016/j.vaccine.2015.02.040

Vancouver

Singh SK, Roeffen W, Andersen G, Bousema T, Christiansen M, Sauerwein R et al. A Plasmodium falciparum 48/45 single epitope R0.6C subunit protein elicits high levels of transmission blocking antibodies. Vaccine. 2015 Apr 15;33(16):1981-6. https://doi.org/10.1016/j.vaccine.2015.02.040

Author

Singh, Susheel K ; Roeffen, Will ; Andersen, Gorm ; Bousema, Teun ; Christiansen, Michael ; Sauerwein, Robert ; Theisen, Michael. / A Plasmodium falciparum 48/45 single epitope R0.6C subunit protein elicits high levels of transmission blocking antibodies. In: Vaccine. 2015 ; Vol. 33, No. 16. pp. 1981-6.

Bibtex

@article{f343309a557541d7bfb146d2b4a7c92e,
title = "A Plasmodium falciparum 48/45 single epitope R0.6C subunit protein elicits high levels of transmission blocking antibodies",
abstract = "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.",
author = "Singh, {Susheel K} and Will Roeffen and Gorm Andersen and Teun Bousema and Michael Christiansen and Robert Sauerwein and Michael Theisen",
note = "Copyright {\textcopyright} 2015 Elsevier Ltd. All rights reserved.",
year = "2015",
month = apr,
day = "15",
doi = "10.1016/j.vaccine.2015.02.040",
language = "English",
volume = "33",
pages = "1981--6",
journal = "Vaccine",
issn = "0264-410X",
publisher = "Elsevier",
number = "16",

}

RIS

TY - JOUR

T1 - A Plasmodium falciparum 48/45 single epitope R0.6C subunit protein elicits high levels of transmission blocking antibodies

AU - Singh, Susheel K

AU - Roeffen, Will

AU - Andersen, Gorm

AU - Bousema, Teun

AU - Christiansen, Michael

AU - Sauerwein, Robert

AU - Theisen, Michael

N1 - Copyright © 2015 Elsevier Ltd. All rights reserved.

PY - 2015/4/15

Y1 - 2015/4/15

N2 - 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.

AB - 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.

U2 - 10.1016/j.vaccine.2015.02.040

DO - 10.1016/j.vaccine.2015.02.040

M3 - Journal article

C2 - 25728318

VL - 33

SP - 1981

EP - 1986

JO - Vaccine

JF - Vaccine

SN - 0264-410X

IS - 16

ER -

ID: 134916379