Molecular characterization of interleukin-1Beta in the tammar wallaby (Macropus eugenii).
Interleukin-1beta (IL-1β) plays a significant role in the onset and pathogenesis of inflammation in mammalian hosts. Although well characterized in a range of vertebrate species, little is known about this important cytokine in marsupial mammals. We report here the molecular cloning and characterization of IL-1β in the tammar wallaby (Macropus eugenii). M. eugenii IL-1β has an open-reading frame of 813 nucleotides, coding for a putative protein of 270 amino acids to the termination codon. The IL-1 family motif and potential caspase cleavage site (necessary for production of the mature protein) is also present in the sequence. Molecular characterization of tammar wallaby IL-1β provides fundamental information necessary to progress the study of functional immune responses in this unique group of mammals.
Young
Lauren J
LJ
Marsupial Immunology Research Laboratory, Centre for Environmental Management CQUniversity Australia, New South Wale, Australia. l.young@cqu.edu.au
Harrison
Gavan A
GA
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003062:Codon / Q000235:genetics; D006801:Humans; D053583:Interleukin-1beta / Q000737:chemistry / Q000235:genetics* / Q000276:immunology; D007614:Macropodidae / Q000235:genetics* / Q000276:immunology; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D009893:Opossums / Q000235:genetics; D010987:Platypus / Q000235:genetics; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity
D003062:Codon; D053583:Interleukin-1beta