The receptor binding domain of the new Middle East respiratory syndrome coronavirus maps to a 231-residue region in the spike protein that efficiently elicits neutralizing antibodies

J Virol. 2013 Aug;87(16):9379-83. doi: 10.1128/JVI.01277-13. Epub 2013 Jun 19.

Abstract

The spike (S) protein of the recently emerged human Middle East respiratory syndrome coronavirus (MERS-CoV) mediates infection by binding to the cellular receptor dipeptidyl peptidase 4 (DPP4). Here we mapped the receptor binding domain in the S protein to a 231-amino-acid fragment (residues 358 to 588) by evaluating the interaction of spike truncation variants with receptor-expressing cells and soluble DPP4. Antibodies to this domain--much less so those to the preceding N-terminal region--efficiently neutralize MERS-CoV infection.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antibodies, Neutralizing / immunology*
  • Antibodies, Viral / immunology
  • Binding Sites
  • Cell Line
  • Coronavirus / immunology*
  • Coronavirus / physiology*
  • Dipeptidyl Peptidase 4 / metabolism
  • Epitopes, B-Lymphocyte / genetics
  • Epitopes, B-Lymphocyte / immunology*
  • Humans
  • Membrane Glycoproteins / immunology*
  • Membrane Glycoproteins / metabolism*
  • Receptors, Virus / metabolism
  • Spike Glycoprotein, Coronavirus
  • Viral Envelope Proteins / immunology*
  • Viral Envelope Proteins / metabolism*
  • Virus Attachment*

Substances

  • Antibodies, Neutralizing
  • Antibodies, Viral
  • Epitopes, B-Lymphocyte
  • Membrane Glycoproteins
  • Receptors, Virus
  • Spike Glycoprotein, Coronavirus
  • Viral Envelope Proteins
  • spike glycoprotein, SARS-CoV
  • spike protein, mouse hepatitis virus
  • DPP4 protein, human
  • Dipeptidyl Peptidase 4