Multilaboratory approach to preclinical evaluation of vaccine immunogens for placental malaria
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Multilaboratory approach to preclinical evaluation of vaccine immunogens for placental malaria. / Fried, Michal; Avril, Marion; Chaturvedi, Richa; Fernandez, Pablo; Lograsso, Joseph; Narum, David; Nielsen, Morten A; Oleinikov, Andrew V; Resende, Mafalda; Salanti, Ali; Saveria, Tracy; Williamson, Kathryn; Dicko, Alassane; Scherf, Artur; Smith, Joseph D; Theander, Thor G; Duffy, Patrick E.
In: Infect Immun, Vol. 81, No. 2, 2013, p. 487-95.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Multilaboratory approach to preclinical evaluation of vaccine immunogens for placental malaria
AU - Fried, Michal
AU - Avril, Marion
AU - Chaturvedi, Richa
AU - Fernandez, Pablo
AU - Lograsso, Joseph
AU - Narum, David
AU - Nielsen, Morten A
AU - Oleinikov, Andrew V
AU - Resende, Mafalda
AU - Salanti, Ali
AU - Saveria, Tracy
AU - Williamson, Kathryn
AU - Dicko, Alassane
AU - Scherf, Artur
AU - Smith, Joseph D
AU - Theander, Thor G
AU - Duffy, Patrick E
PY - 2013
Y1 - 2013
N2 - Pregnancy malaria is caused by Plasmodium falciparum-infected erythrocytes that adhere to the placental receptor chondroitin sulfate A (CSA) and sequester in the placenta; women become resistant to pregnancy malaria as they acquire antiadhesion antibodies that target surface proteins of placental parasites. VAR2CSA, a member of the P. falciparum EMP1 variant surface antigen family, is the leading candidate for a pregnancy malaria vaccine. Because VAR2CSA is a high-molecular-weight protein, a vaccine based on the full-length protein may not be feasible. An alternative approach has been to develop a vaccine targeting individual Duffy binding-like (DBL) domains. In this study, a consortium of laboratories under the Pregnancy Malaria Initiative compared the functional activity of antiadhesion antibodies elicited by different VAR2CSA domains and variants produced in prokaryotic and eukaryotic expression systems. Antisera were initially tested against laboratory lines of maternal parasites, and the most promising reagents were evaluated in the field against fresh placental parasite samples. Recombinant proteins expressed in Escherichia coli elicited antibody levels similar to those expressed in eukaryotic systems, as did the two allelic forms of the DBL4 and DBL5 domains. The procedures developed for this head-to-head comparison will be useful for future evaluation and down-selection of malaria vaccine immunogens.
AB - Pregnancy malaria is caused by Plasmodium falciparum-infected erythrocytes that adhere to the placental receptor chondroitin sulfate A (CSA) and sequester in the placenta; women become resistant to pregnancy malaria as they acquire antiadhesion antibodies that target surface proteins of placental parasites. VAR2CSA, a member of the P. falciparum EMP1 variant surface antigen family, is the leading candidate for a pregnancy malaria vaccine. Because VAR2CSA is a high-molecular-weight protein, a vaccine based on the full-length protein may not be feasible. An alternative approach has been to develop a vaccine targeting individual Duffy binding-like (DBL) domains. In this study, a consortium of laboratories under the Pregnancy Malaria Initiative compared the functional activity of antiadhesion antibodies elicited by different VAR2CSA domains and variants produced in prokaryotic and eukaryotic expression systems. Antisera were initially tested against laboratory lines of maternal parasites, and the most promising reagents were evaluated in the field against fresh placental parasite samples. Recombinant proteins expressed in Escherichia coli elicited antibody levels similar to those expressed in eukaryotic systems, as did the two allelic forms of the DBL4 and DBL5 domains. The procedures developed for this head-to-head comparison will be useful for future evaluation and down-selection of malaria vaccine immunogens.
U2 - 10.1128/IAI.01106-12
DO - 10.1128/IAI.01106-12
M3 - Journal article
C2 - 23208604
VL - 81
SP - 487
EP - 495
JO - Infection and Immunity
JF - Infection and Immunity
SN - 0019-9567
IS - 2
ER -
ID: 44049729