@article{fdi:010037748,
  title = {{R}eceptor-binding studies of the {DBL} gamma domain of {P}lasmodium falciparum erythrocyte membrane protein 1 from a placental isolate},
  author = {{B}adaut, {C}. and {F}aure, {G}. and {T}uikue {N}dam, {N}icaise and {B}ertin, {G}wladys and {C}haffotte, {A}. and {K}hattab, {A}. and {K}linkert, {M}.{Q}. and {D}eloron, {P}hilippe and {B}entley, {G}.{A}.},
  editor = {},
  language = {{ENG}},
  abstract = {{W}e have previously identified a number of {DBL} gamma domains in {P}lasmodium falciparum erythrocyte membrane protein 1 ({P}f{EMP}1) transcripts obtained from placental parasite isolates, showing that they bind specifically to chondroitin sulfate {A} ({CSA}) ({K}hattab {A}, {K}un {J}, {D}eloron {P}, {K}remsner {PG}, {K}linkert {MQ}. {V}ariants of {P}lasmodium falciparum erythrocyte membrane protein {I} expressed by different placental parasites are closely related and adhere to chondroitin sulfate {A}. {J} {I}nfect {D}is 2001;183:1165-9). {H}ere we give a more detailed physico-chemical and binding characterisation of the soluble, recombinant {DBL} gamma domain derived from one of these isolates. {R}esults from circular dichroism and limited proteolysis experiments are consistent with the recombinant domain being expressed with the native fold. {S}pecific binding of {DBL} gamma to placental cryosections was demonstrated by labeling with antibodies raised against the recombinant domain; binding was diminished after treatment of the cryosections with chondroitinase or by blocking with anti-{CSA} antibody, showing that {CSA} mediates the interaction. {B}inding of the {DBL} gamma domain to purified placental chondroitin sulfate proteoglycan ({CSPG}) was also studied using surface plasmon resonance techniques, with {DBL} gamma as analyte and {CSPG} immobilised on the sensor chip; these quantitative measurements gave an affinity constant in the mu-molar range under the conditions used. {T}he native conformation of the {DBL} gamma domain is essential for {CSPG} recognition since binding to the sensor chip is abolished when the protein is irreversibly reduced. {A}s with the placental cryosections, association was significantly reduced after treating the immobilised {CSPG} with chondroitinase. {T}ogether, these results demonstrate specific interaction between the {DBL} gamma domain and the placental receptor.},
  keywords = {{P}lasmodium falciparum ; erythrocyte membrane protein 1 ; duffy binding like domain ; placental malaria ; receptor binding ; surface plasmon resonance ; circular dichroism},
  booktitle = {},
  journal = {{M}olecular and {B}iochemical {P}arasitology},
  volume = {151},
  numero = {1},
  pages = {89--99},
  ISSN = {0166-6851},
  year = {2007},
  DOI = {10.1016/j.molbiopara.2006.10.010},
  URL = {https://www.documentation.ird.fr/hor/fdi:010037748},
}