Title | Production, crystallization and X-ray diffraction analysis of two nanobodies against the Duffy binding-like (DBL) domain DBL6ℇ-FCR3 of the Plasmodium falciparum VAR2CSA protein. |
Publication Type | Journal Article |
Year of Publication | 2013 |
Authors | Vuchelen, A., E. Pardon, J. Steyaert, B. Gamain, R. Loris, N. A. J. van Nuland, and S. Ramboarina |
Journal | Acta Crystallogr Sect F Struct Biol Cryst Commun |
Volume | 69 |
Issue | Pt 3 |
Pagination | 270-4 |
Date Published | 2013 Mar 1 |
ISSN | 1744-3091 |
Keywords | Amino Acid Sequence, Animals, Antibodies, Protozoan, Antigens, Protozoan, Binding Sites, Camelids, New World, Crystallography, X-Ray, Erythrocytes, Escherichia coli, Models, Molecular, Molecular Sequence Data, Plasmodium falciparum, Protein Structure, Secondary, Protein Structure, Tertiary, Recombinant Proteins, Sequence Alignment, Sequence Homology, Amino Acid, Single-Domain Antibodies |
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 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 C2 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 P4₃2₁2 with unit-cell parameters a=b=62.7, c=167.2 Å. |
DOI | 10.1107/S1744309113001917 |
Alternate Journal | Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. |
PubMed ID | 23519802 |
PubMed Central ID | PMC3606572 |
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