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