A post-translational modification of human Norovirus capsid protein attenuates glycan binding.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 30899001.
- Also identified by DOI 10.1038/s41467-019-09251-5 and PMC identifier 6428809.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
Attachment of human noroviruses to histo blood group antigens (HBGAs) is essential for infection, but how this binding event promotes the infection of host cells is unknown. Here, we employ protein NMR experiments supported by mass spectrometry and crystallography to study HBGA binding to the P-domain of a prevalent virus strain (GII.4). We report a highly selective transformation of asparagine 373, located in an antigenic loop adjoining the HBGA binding site, into an iso-aspartate residue. This spontaneous post-translational modification (PTM) proceeds with an estimated half-life of a few days at physiological temperatures, independent of the presence of HBGAs but dramatically affecting HBGA recognition. Sequence conservation and the surface-exposed position of this PTM suggest an important role in infection and immune recognition for many norovirus strains.
Medical subject headings
- Asparagine
- Blood Group Antigens
- Capsid Proteins
- Isoaspartic Acid
- Norovirus
- Polysaccharides
- Protein Processing, Post-Translational