Assignment of Ala, Ile, LeuproS, Met, and ValproS methyl groups of the protruding domain of murine norovirus capsid protein VP1 using methyl–methyl NOEs, site directed mutagenesis, and pseudocontact shifts

Thorben Maass, Leon Torben Westermann, Robert Creutznacher, Alvaro Mallagaray, Jasmin Dülfer, Charlotte Uetrecht, Thomas Peters*

*Korrespondierende/r Autor/-in für diese Arbeit

Abstract

The protruding domain (P-domain) of the murine norovirus (MNV) capsid protein VP1 is essential for infection. It mediates receptor binding and attachment of neutralizing antibodies. Protein NMR studies into interactions of the P-domain with ligands will yield insights not easily available from other biophysical techniques and will extend our understanding of MNV attachment to host cells. Such studies require at least partial NMR assignments. Here, we describe the assignment of about 70% of the Ala, Ile, LeuproS, Met, and ValproS methyl groups. An unfavorable distribution of methyl group resonance signals prevents complete assignment based exclusively on 4D HMQC-NOESY-HMQC experiments, yielding assignment of only 55 out of 100 methyl groups. Therefore, we created point mutants and measured pseudo contact shifts, extending and validating assignments based on methyl-methyl NOEs. Of note, the P-domains are present in two different forms caused by an approximate equal distribution of trans- and cis-configured proline residues in position 361.

OriginalspracheEnglisch
ZeitschriftBiomolecular NMR Assignments
Jahrgang16
Ausgabenummer1
Seiten (von - bis)97-107
Seitenumfang11
ISSN1874-2718
DOIs
PublikationsstatusVeröffentlicht - 04.2022

Strategische Forschungsbereiche und Zentren

  • Forschungsschwerpunkt: Infektion und Entzündung - Zentrum für Infektions- und Entzündungsforschung Lübeck (ZIEL)
  • Zentren: Zentrum für Medizinische Struktur- und Zellbiologie (ZMSZ)

DFG-Fachsystematik

  • 204-04 Virologie

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