Structural insights into the human metapneumovirus glycoprotein ectodomain

J Virol. 2014 Oct;88(19):11611-6. doi: 10.1128/JVI.01726-14. Epub 2014 Jul 16.

Abstract

Human metapneumovirus is a major cause of respiratory tract infections worldwide. Previous reports have shown that the viral attachment glycoprotein (G) modulates innate and adaptive immune responses, leading to incomplete immunity and promoting reinfection. Using bioinformatics analyses, static light scattering, and small-angle X-ray scattering, we show that the extracellular region of G behaves as a heavily glycosylated, intrinsically disordered polymer. We discuss potential implications of these findings for the modulation of immune responses by G.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Glycoproteins / chemistry*
  • Glycoproteins / immunology
  • Glycoproteins / metabolism
  • Glycosylation
  • Humans
  • Immunity, Innate
  • Metapneumovirus / chemistry*
  • Metapneumovirus / immunology
  • Metapneumovirus / metabolism
  • Models, Molecular
  • Protein Structure, Tertiary
  • Viral Proteins / chemistry*
  • Viral Proteins / immunology
  • Viral Proteins / metabolism

Substances

  • G glycoprotein, human metapneumovirus
  • Glycoproteins
  • Viral Proteins

Associated data

  • PDB/3FXI
  • PDB/4DAG