Molecular analysis of the coronavirus-receptor function of aminopeptidase N

Andreas Kolb, A Hegyi, J Maile, A Heister, M Hagemann, S G Siddell

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    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.

    Original languageEnglish
    Pages (from-to)61-67
    Number of pages7
    JournalAdvances in Experimental Medicine and Biology
    Volume440
    Publication statusPublished - 1998

    Keywords

    • TRANSMISSIBLE GASTROENTERITIS VIRUS
    • CANINE
    • FELINE

    Cite this

    Kolb, A., Hegyi, A., Maile, J., Heister, A., Hagemann, M., & Siddell, S. G. (1998). Molecular analysis of the coronavirus-receptor function of aminopeptidase N. Advances in Experimental Medicine and Biology, 440, 61-67.