Large-Scale Expression and Purification of Mumps Virus Hemagglutinin-Neuraminidase for Structural Analyses and Glycan-Binding Assays

Marie Kubota, Takao Hashiguchi

Research output: Contribution to journalArticle

Abstract

Many viruses utilize cell-surface glycans as receptors for host cell entry. Viral surface glycoproteins specifically interact with glycan motifs, which strongly contributes to viral tropism. Recently, the interactions between host cell glycan receptors and the mumps virus (MuV) hemagglutinin-neuraminidase (MuV-HN) protein were characterized by determining the co-crystal structure of MuV-HN in complex with glycan receptors. Here, we describe protocols for large-scale expression, purification and crystallization of MuV-HN proteins for structural analyses and glycan-binding assays with the overarching goal of investigating glycan-protein interactions.

Original languageEnglish
Pages (from-to)641-652
Number of pages12
JournalMethods in molecular biology (Clifton, N.J.)
Volume2132
DOIs
Publication statusPublished - Jan 1 2020

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All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Genetics

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