Abstract
Recently, combined nuclear magnetic resonance (NMR), native mass spectrometry (MS) and X-ray crystallographic studies have demonstrated that binding of histo-blood group antigens (HBGAs) to norovirus capsid protein (P-dimers) is a cooperative process involving four binding pockets. Here, we show that binding to norovirus virus-like particles (VLPs) is even more complex. We performed saturation transfer difference (STD) NMR titration experiments with two representative genotypes of norovirus VLPs using L-fucose as a minimal HBGA. Compared to titrations with P-dimers, the corresponding binding isotherms reflect at least six distinct binding events.
| Original language | English |
|---|---|
| Journal | Glycobiology |
| Volume | 27 |
| Issue number | 1 |
| Pages (from-to) | 80-86 |
| Number of pages | 7 |
| ISSN | 0959-6658 |
| DOIs | |
| Publication status | Published - 01.2017 |
Funding
The German Research Council (DFG) (Grants DFG-PE494/8-1 and DFGPE494/ 12-1 as part of the research unit ViroCarb (FOR 2327) to T.P.). Marie Curie fellowship within the 7th Framework Programme of the EU (Grant Agreement No. 329485, NoroCarb to A.M.). A.M. also thanks the University of Lubeck for financial support. Work at F.P. laboratory has been supported by grant GRUPIN 14-099 from Consejeria de Economia y Empleo of Principado de Asturias and the European Union FEDER program.
Research Areas and Centers
- Academic Focus: Center for Infection and Inflammation Research (ZIEL)
