@article{fdi:010049685,
  title = {{F}unctional and immunological characterization of the var2{CSA}-{DBL}5 epsilon domain of a placental {P}lasmodium falciparum isolate},
  author = {{G}angnard, {S}. and {T}uikue {N}dam, {N}icaise and {G}nidehou, {S}{\'e}dami and {Q}uiviger, {M}ichael and {J}uillerat, {A}. and {F}aure, {G}. and {B}aron, {B}. and {V}iwami, {F}irmine and {D}eloron, {P}hilippe and {B}entley, {G}. {A}.},
  editor = {},
  language = {{ENG}},
  abstract = {{P}regnancy-associated malaria ({PAM}) arises from sequestration of {P}lasmodium falciparum-parasitized erythrocytes ({PE}) in the placenta, leading to chronic symptoms in the expectant mother and serious consequences for fetal development. {P}lacental sequestration has been linked to binding of chondroitin sulphate {A} ({CSA}) by the var2{CSA} variant of {P}f{EMP}1 expressed on the {PE} surface, and a substantial body of evidence shows that the immune response to var2{CSA} gives an effective protection against {PAM}. {W}e have expressed the var2{CSA}-{DBL}5 epsilon domain, derived from a placental isolate from {S}enegal, as soluble product in {E}scherichia coil and have shown using different criteria that the recombinant protein is obtained with the native conformation. {U}sing surface plasmon resonance techniques, we have examined binding of {DBL}5 epsilon to placental chondroitin sulphate proteoglyan and {CSA}; however, the recombinant protein also binds to other sulphated oligosaccharides, with higher affinity in some cases, indicating that the single domain lacks the specificity for {CSA} shown by the complete extra-cellular region of var2{CSA} and placental parasites. {R}ecombinant {DBL}5 epsilon was specifically recognized by sera from malaria-exposed {S}enegalese women in a parity-dependent manner but by sera not from children or males from the same endemic region. {C}onversely, {DBL}5 epsilon induced antibodies in mice that recognized placental isolates from {B}enin but not isolates from children. {T}he presence of universal epitopes thus supports {DBL}5 epsilon as an interesting component of var2{CSA} to be considered for vaccine development.},
  keywords = {{P}regnancy-associated malaria ; {P}f{EMP}1 ; var2{CSA} ; {DBL} domain ; {R}ecombinant protein},
  booktitle = {},
  journal = {{M}olecular and {B}iochemical {P}arasitology},
  volume = {173},
  numero = {2},
  pages = {115--122},
  ISSN = {0166-6851},
  year = {2010},
  DOI = {10.1016/j.molbiopara.2010.05.014},
  URL = {https://www.documentation.ird.fr/hor/fdi:010049685},
}