Biological activity of hamster interferon-gamma is modulated by the carboxyl-terminal tail

Weiguo Zhao, Anais Z. Valencia, Peter C. Melby

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

The Syrian golden hamster (Mesocricetus auratus) is highly susceptible to a number of intracellular pathogens. Interferon-gamma (IFN-γ), the primary macrophage-activating cytokine, plays a key role in the host defense against intracellular pathogens. The hamster IFN-γ cDNA encodes a 174 amino acid protein that has an additional 17 amino acids at the carboxyl-terminus compared to IFN-γ of mice and rats. A homologous C-terminal tail is also found in other non-murine rodents. The biological activity of hamster IFN-γ had not been investigated previously so we first demonstrated the activity of native IFN-γ in assays of IFN-γ-induced receptor signaling and antiviral activity against vesicular stomatitis virus. We then tested the hypothesis that the C-terminal tail of hamster IFN-γ could influence its biological activity. A truncated hamster IFN-γ, in which the C-terminal 17 aa were removed by insertion of a stop codon at the position corresponding to the stop codon in the mouse sequence, had approximately 10-fold greater activity than the full length protein when measured in the two bioassays. Polyclonal and monoclonal anti-hamster IFN-γ antibodies specifically inhibited this biological activity. Collectively, these data indicate that this unique structural feature influences the biological activity of hamster IFN-γ.

Original languageEnglish (US)
Pages (from-to)243-251
Number of pages9
JournalCytokine
Volume34
Issue number5-6
DOIs
StatePublished - Jun 1 2006
Externally publishedYes

Keywords

  • Antiviral
  • Hamster
  • Interferon-gamma
  • Mesocricetus auratus

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology
  • Biochemistry
  • Hematology
  • Molecular Biology

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