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Molecular Analysis of the Coronavirus-Receptor Function of Aminopeptidase N

  • Andreas F. Kolb
  • Annette Hegyi
  • Julia Maile
  • Angelien Heister
  • Margitta Hagemann
  • Stuart G. Siddell
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 440)

Abstract

Aminopeptidase N (APN) is a major cell surface for coronaviruses of the serogroup I. By using chimeric APN proteins assembled from human, porcine and feline APN we have identified determinants which are critically involved in the Coronavirus-APN interaction. Our results indicate that human coronavirus 229E (HCV 229E) is distinct from the other serogroup I coronaviruses in that determinants located within the N-terminal parts of the human and feline APN proteins mediate the infection of HCV 229E, whereas determinants located within the C-terminal parts of porcine, feline and canine APN mediate the infection of transmissible gastro-enteritis virus (TGEV), feline infectious peritonitis virus (FIPV) and canine coronavirus (CCV), respectively. A further analysis of the mapped amino acid segments by site directed mutagenesis revealed that a short stretch of 8 amino acids in the hAPN protein plays a decisive role in mediating HCV 229E reception.

Keywords

Chimeric Protein MegAlign Program Feline Infectious Peritonitis Virus Amino Acid Segment CRFK Cell 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1998

Authors and Affiliations

  • Andreas F. Kolb
    • 1
  • Annette Hegyi
    • 1
  • Julia Maile
    • 1
  • Angelien Heister
    • 1
  • Margitta Hagemann
    • 1
  • Stuart G. Siddell
    • 1
  1. 1.Institute of Virology and ImmunologyUniversity of WürzburgWürzburgGermany

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