A B-lymphocyte binding peptide from BNRF1 induced antibodies inhibiting EBV-invasion of B-lymphocytes

Epstein-Barr virus is a herpesvirus that causes infectious mononucleosis, carcinomas and immunoproliferative disease. Its genome encodes 86 proteins, which provided targets for a structural genomics project. After updating the annotation of the genome, 23 open reading frames were chosen for expression in Escherichia coli, initially selecting for those with known enzyme activity and then supplementing this set based on a series of predicted properties, in particular secondary structure. The major obstacle turned out to be poor expression and low solubility. Surprisingly, this could not be overcome by modifications of the constructs, changes of expression temperature or strain or renaturation. Of the eight soluble proteins, five were crystallized using robotic nanolitredrop crystallization trials, which led to four solved structures. Although these results depended on individual treatment rather than standardized protocols, a high-throughput miniaturized crystallization screening protocol was a key component of success with these difficult proteins.

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Structural genomics of the Epstein–Barr virus

Tarbouriech

Buisson

Géoui

et al. 2006

Acta Crystallogr D Biol Crystallogr

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A B-lymphocyte binding peptide from BNRF1 induced antibodies inhibiting EBV-invasion of B-lymphocytes

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References 31 publications

Structural genomics of the Epstein–Barr virus

Structural genomics of the Epstein–Barr virus

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