Large-Scale expression and purification of mumps virus hemagglutinin-neuraminidase for structural analyses and glycan-binding assays

Marie Kubota, Takao Hashiguchi

Research output: Chapter in Book/Report/Conference proceedingChapter

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
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Pages641-652
Number of pages12
DOIs
Publication statusPublished - 2020

Publication series

NameMethods in Molecular Biology
Volume2132
ISSN (Print)1064-3745
ISSN (Electronic)1940-6029

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Genetics

Fingerprint Dive into the research topics of 'Large-Scale expression and purification of mumps virus hemagglutinin-neuraminidase for structural analyses and glycan-binding assays'. Together they form a unique fingerprint.

Cite this