Open AccessProduction, crystallization and X‐ray diffraction analysis of two nanobodies against the Duffy binding‐like (DBL) domain DBL6ɛ‐FCR3 of the Plasmodium falciparum VAR2CSA protein
Author(s) -
Vuchelen Anneleen,
Pardon Els,
Steyaert Jan,
Gamain Benoît,
Loris Remy,
van Nuland Nico A. J.,
Ramboarina Stéphanie
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113001917
Subject(s) - plasmodium falciparum , bacterial adhesin , resolution (logic) , crystallization , biology , antibody , crystallography , microbiology and biotechnology , chemistry , malaria , biochemistry , immunology , gene , escherichia coli , organic chemistry , artificial intelligence , computer science
The VAR2CSA protein has been closely associated with pregnancy‐associated malaria and is recognized as the main adhesin exposed on the surface of Plasmodium falciparum ‐infected erythrocytes. Chondroitin sulfate A was identified as the main host receptor in the placenta. Single‐domain heavy‐chain camelid antibodies, more commonly called nanobodies, were selected and produced against the DBL6ɛ‐FCR3 domain of VAR2CSA. Crystals of two specific nanobodies, Nb2907 and Nb2919, identified as strong binders to DBL6ɛ‐FCR3 and the full‐length VAR2CSA exposed on the surface of FCR3 P. falciparum ‐infected erythrocytes, were obtained. Crystals of Nb2907 diffract to 2.45 Å resolution and belong to space group C 2 with unit‐cell parameters a = 136.1, b = 78.5, c = 103.4 Å, β = 118.8°, whereas Nb2919 crystals diffract to 2.15 Å resolution and belong to space group P 4 3 2 1 2 with unit‐cell parameters a = b = 62.7, c = 167.2 Å.