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

doi:10.1107/S1744309113001917

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

Toegepaste Biologische Wetenschappen

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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.

Originele taal-2	English
Pagina's (van-tot)	270-274
Aantal pagina's	5
Tijdschrift	Acta Crystallogr F Struct Biol Commun
Volume	69
DOI's	https://doi.org/10.1107/S1744309113001917
Status	Published - 2013

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FWOAL699: ESRF and DUBBLE: Synchrotron X-rays for revealing the structure and function of molecules and materials
Loris, R. (Administrative Promotor), Remaut, H. K. (Co-Promoter), Goderis, B. (Coördinator), Janssens, K. (Co-Promoter), Kirschhock, C. E. A. (Co-Promoter), Van Bael, M. (Co-Promoter), Poelman, D. (Co-Promoter), Temst, K. (Co-Promoter), Adriaens, A. (Co-Promoter) & Laszlo, V. (Co-Promoter)
1/01/13 → 31/12/17
Project: Fundamenteel
SRP13: Structuur en dynamiek van macromoleculaire complexen in gezondheid en ziekte
Steyaert, J. (Administrative Promotor), Remaut, H. K. (Co-Promoter), Loris, R. (Co-Promoter), Efremov, R. (Co-Promoter), Steyaert, J. (Administrative Promotor), Loris, R. (Co-Promoter) & Remaut, H. K. (Co-Promoter)
1/11/12 → 31/10/24
Project: Fundamenteel

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@article{c29c78afd7384ec7a2b134605e7f943d,

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

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.",

keywords = "Structural Biology, X-ray crystallography, Nanobody",

author = "Anneleen Vuchelen and Els Pardon and Jan Steyaert and Benoit Gamain and Remy Loris and \{Van Nuland\}, Nico and Stephanie Ramboarina",

year = "2013",

doi = "10.1107/S1744309113001917",

language = "English",

volume = "69",

pages = "270--274",

journal = "Acta Crystallogr F Struct Biol Commun",

issn = "1744-3091",

publisher = "Wiley-Blackwell",

}

Vuchelen, A, Pardon, E , Steyaert, J, Gamain, B, Loris, R, Van Nuland, N & Ramboarina, S 2013, 'Production, crystallisation and X-ray diffraction analysis of two nanobodies against the Duffy Binding like domain DBL6e-FCR3 of the Plasmodium falciparum VAR2CSA protein', Acta Crystallogr F Struct Biol Commun, vol. 69, blz. 270-274. https://doi.org/10.1107/S1744309113001917

TY - JOUR

T1 - Production, crystallisation and X-ray diffraction analysis of two nanobodies against the Duffy Binding like domain DBL6e-FCR3 of the Plasmodium falciparum VAR2CSA protein

AU - Vuchelen, Anneleen

AU - Pardon, Els

AU - Steyaert, Jan

AU - Gamain, Benoit

AU - Loris, Remy

AU - Van Nuland, Nico

AU - Ramboarina, Stephanie

PY - 2013

Y1 - 2013

N2 - 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.

AB - 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.

KW - Structural Biology

KW - X-ray crystallography

KW - Nanobody

U2 - 10.1107/S1744309113001917

DO - 10.1107/S1744309113001917

M3 - Article

SN - 1744-3091

VL - 69

SP - 270

EP - 274

JO - Acta Crystallogr F Struct Biol Commun

JF - Acta Crystallogr F Struct Biol Commun

ER -

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

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Projecten

FWOAL699: ESRF and DUBBLE: Synchrotron X-rays for revealing the structure and function of molecules and materials

SRP13: Structuur en dynamiek van macromoleculaire complexen in gezondheid en ziekte

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