Production, crystallisation and X-ray diffraction analysis of two nanobodies against the Duffy Binding like domain DBL6e-FCR3 of the Plasmodium falciparum VAR2CSA protein

Anneleen Vuchelen, Els Pardon, Jan Steyaert, Benoit Gamain, Remy Loris, Nico Van Nuland, Stephanie Ramboarina

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)
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Abstract

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 DBL6"-FCR3 domain of VAR2CSA. Crystals of two specific nanobodies, Nb2907 and Nb2919, identified as strong binders to DBL6e-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 A resolution and belong to space group C2 with unit-cell parameters a = 136.1, b = 78.5, c = 103.4 A, beta = 118.8°, whereas Nb2919 crystals diffract to 2.15 A resolution and belong to space group P4(3)2(1)2 with unit-cell parameters a = b = 62.7, c = 167.2 A.
Original languageEnglish
Pages (from-to)270-274
Number of pages5
JournalActa Crystallogr F Struct Biol Commun
Volume69
DOIs
Publication statusPublished - 2013

Keywords

  • Structural Biology
  • X-ray crystallography
  • Nanobody

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