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Structural basis for Glycan-receptor binding by mumps virus hemagglutinin-neuraminidase

Rosa Ester Forgione1, Cristina Di Carluccio1, Marie Kubota2

  • 1Department of Chemical Sciences, Complesso Universitario Monte Sant'Angelo, University of Naples Federico II, Via Cintia 4, I-80126, Napoli, Italy.

Scientific Reports
|February 2, 2020
PubMed

Insights

Mumps virus hemagglutinin-neuraminidase (MuV-HN) binds to sialylated glycans on host cells. Understanding this interaction aids in developing new drugs against mumps virus infections.

Area of Science:

  • Virology
  • Structural Biology
  • Biochemistry

Background:

  • Mumps virus causes respiratory illnesses, particularly in children.
  • The viral hemagglutinin-neuraminidase (MuV-HN) glycoprotein is crucial for mumps virus entry and infectivity.
  • MuV-HN is an attractive target for antiviral drug development.

Purpose of the Study:

  • To analyze the molecular recognition of host cell sialylated glycans by MuV-HN.
  • To elucidate the structural basis of sialoglycan/MuV-HN complex formation.
  • To investigate the enzymatic activity of MuV-HN on different glycan substrates.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy
  • Molecular docking and modeling
  • CORCEMA-ST analysis
  • NMR-based kinetic analysis

Main Results:

  • Detailed structural features of sialoglycan/MuV-HN complexes were revealed.
  • MuV-HN exhibits distinct enzymatic activity towards complex sialoglycans compared to simpler ligands.
  • The study provides insights into the binding mechanism and enzymatic properties of MuV-HN.

Conclusions:

  • The findings provide a structural foundation for designing inhibitors targeting MuV-HN.
  • This research paves the way for developing novel therapeutics against mumps virus.
  • Understanding MuV-HN-glycan interactions is key to combating mumps-related diseases.

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