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Benoit Gamain

Researcher at University of Paris

Publications -  74
Citations -  3137

Benoit Gamain is an academic researcher from University of Paris. The author has contributed to research in topics: Plasmodium falciparum & Malaria. The author has an hindex of 27, co-authored 63 publications receiving 2796 citations. Previous affiliations of Benoit Gamain include National Institutes of Health & Paris Diderot University.

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Classification of adhesive domains in the Plasmodium falciparum erythrocyte membrane protein 1 family.

TL;DR: The sequence classification of DBL and CIDR types may have predictive value for identifying PfEMP1 domains with a particular binding property, and this information might be used to develop interventions targeting parasite binding variants that cause disease.
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Plasmodium falciparum domain mediating adhesion to chondroitin sulfate A: A receptor for human placental infection

TL;DR: Because protective antibodies present after pregnancy block binding to CSA of parasites from different parts of the world, DBL-3, although variant, may induce cross-reactive immunity that will protect pregnant women and their fetuses.
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A single member of the Plasmodium falciparum var multigene family determines cytoadhesion to the placental receptor chondroitin sulphate A

TL;DR: It is shown that disruption of the var2csa gene of P. falciparum results in the inability of parasites to recover the CSA‐binding phenotype, which supports var2CSA as a leading vaccine candidate aimed at protecting pregnant women and their fetuses.
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Identification of Multiple Chondroitin Sulfate A (CSA)–Binding Domains in the var2CSA Gene Transcribed in CSA-Binding Parasites

TL;DR: The identification of multiple binding domains in var2CSA strengthens the evidence for their involvement in malaria during pregnancy and may have applications for the development of a vaccine against malaria in pregnancy.
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Full-length extracellular region of the var2CSA variant of PfEMP1 is required for specific, high-affinity binding to CSA

TL;DR: It is suggested that a high-affinity, CSA-specific binding site is formed by the higher-order structure of the var2CSA extracellular region, which has important consequences for the development of an effective vaccine and therapeutic inhibitors.