Human coronavirus 229E: receptor binding domain and neutralization by soluble receptor at 37 degrees C

J Virol. 2003 Apr;77(7):4435-8. doi: 10.1128/jvi.77.7.4435-4438.2003.

Abstract

Truncated human coronavirus HCoV-229E spike glycoproteins containing amino acids 407 to 547 bound to purified, soluble virus receptor, human aminopeptidase N (hAPN). Soluble hAPN neutralized the infectivity of HCoV-229E virions at 37 degrees C, but not 4 degrees C. Binding of hAPN may therefore trigger conformational changes in the viral spike protein at 37 degrees C that facilitate virus entry.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • CD13 Antigens / chemistry
  • CD13 Antigens / genetics
  • CD13 Antigens / physiology*
  • Cell Line
  • Coronavirus 229E, Human / genetics
  • Coronavirus 229E, Human / pathogenicity*
  • Coronavirus 229E, Human / physiology*
  • Humans
  • Membrane Glycoproteins / chemistry
  • Membrane Glycoproteins / genetics
  • Membrane Glycoproteins / physiology
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Tertiary
  • Receptors, Coronavirus
  • Receptors, Virus / chemistry
  • Receptors, Virus / genetics
  • Receptors, Virus / physiology*
  • Sequence Deletion
  • Solubility
  • Spike Glycoprotein, Coronavirus
  • Viral Envelope Proteins / chemistry
  • Viral Envelope Proteins / genetics
  • Viral Envelope Proteins / physiology

Substances

  • Membrane Glycoproteins
  • Receptors, Coronavirus
  • Receptors, Virus
  • Spike Glycoprotein, Coronavirus
  • Viral Envelope Proteins
  • CD13 Antigens