Solution structure of the immunodominant region of protein G of bovine respiratory syncytial virus

Biochemistry
J F DoreleijersR Kaptein

Abstract

The three-dimensional solution structure of the immunodominant central conserved region of the attachment protein G (BRSV-G) of bovine respiratory syncytial virus has been determined by nuclear magnetic resonance (NMR) spectroscopy. In the 32-residue peptide studied, 19 residues form a small rigid core composed of two short helices, connected by a type I' turn, and linked by two disulfide bridges. This unique fold is among the smallest stable tertiary structures known and could therefore serve as an ideal building block for the design of de novo proteins and as a test case for modeling studies. A characteristic hydrophobic pocket, lined by conserved residues, lies at the surface of the peptide and may play a role in receptor binding. This work provides a structural basis for further peptide vaccine development against the severe diseases associated with the respiratory syncytial viruses in both cattle and man.

References

Mar 5, 1985·Journal of Molecular Biology·R KapteinW F van Gunsteren
May 1, 1994·Journal of Biomolecular NMR·A M Gronenborn, G M Clore
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Citations

Oct 24, 2000·Journal of Virology·J F ValarcherH Bourhy
Oct 18, 2002·The Journal of Peptide Research : Official Journal of the American Peptide Society·M SugawaraA Milton
Aug 15, 1998·Archives of Biochemistry and Biophysics·J HughesM A Hughes
Mar 11, 2018·Science Immunology·Stanislav O FedechkinRebecca M DuBois
Feb 7, 2019·Nature Reviews. Microbiology·Michael B Battles, Jason S McLellan
Oct 20, 2000·The Journal of General Virology·I Martínez, J A Melero
Dec 20, 2019·Journal of Virology·Stanislav O FedechkinRebecca M DuBois
Nov 26, 2020·Journal of Veterinary Diagnostic Investigation : Official Publication of the American Association of Veterinary Laboratory Diagnosticians, Inc·Asuka KumagaiShinichi Hatama

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