Molecular cloning and sequencing of interleukin 6 cDNA fragments from the harbor seal (Phoca vitulina), killer whale (Orcinus orca), and Southern sea otter (Enhydra lutris nereis)

Donald P. King, Mark D. Schrenzel, Mark L. McKnight, Thomas H. Reidarson, Krista D. Hanni, Jeffrey L Stott, David A. Ferrick

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

Using polymerase chain reaction, interleukin-6 (IL-6) cDNA fragments from harbor seal (Phoca vitulina), killer whale (Orcinus orca), and Southern sea otter (Enhydra lutris nereis) were cloned and sequenced. For all three species, a continuous open reading frame encoding 203 residues for harbor seal, 199 residues for killer whale, and 201 residues for sea otter with stop codons located at analogous positions were identified. These fragments correspond to nucleotides 71-753 of the human IL-6 transcript and represent 96% of the complete coding nucleotides. Comparison of these marine mammal sequences with other published mammalian IL-6 cDNA demonstrated that both harbor seal and sea otter IL-6 had most similarity to that of other terrestrial carnivores (Mustelidae and Canidae), while killer whale had highest identity with ruminants (Bovidae and Ovidae). Among the three marine mammal species characterized, as well as cDNA sequences from nine other species, 40 invariant amino acids, including a number of residues situated at the putative gp80 and gp130 receptor binding sites, were identified. The presence of invariant amino acids within the receptor-binding portion of IL-6 for twelve different species suggests these positions are essential for biological activity of IL-6 and, moreover, likely account for the cross-reactivity among different mammalian IL-6-like activities in mouse bioassays. An additional significant finding was the presence of several variant residues only within the mouse putative IL-6 receptor binding region, which may account for observations of restricted cross-reactivity of mouse IL-6-like activity in human bioassays. Together, these findings provide insights into the evolution of the mammalian IL-6 gene and additional valuable information regarding amino acid residues essential for the biological activity of mammalian IL-6.

Original languageEnglish (US)
Pages (from-to)190-195
Number of pages6
JournalImmunogenetics
Volume43
Issue number4
DOIs
StatePublished - 1996

Fingerprint

Killer Whale
Otters
Phoca
Molecular Cloning
Interleukin-6
Complementary DNA
Biological Assay
Mammals
Nucleotides
Amino Acid Receptors
Mustelidae
Interleukin-6 Receptors
Essential Amino Acids
Terminator Codon
Ruminants
Human Activities
Open Reading Frames
Canidae

ASJC Scopus subject areas

  • Immunology
  • Genetics

Cite this

Molecular cloning and sequencing of interleukin 6 cDNA fragments from the harbor seal (Phoca vitulina), killer whale (Orcinus orca), and Southern sea otter (Enhydra lutris nereis). / King, Donald P.; Schrenzel, Mark D.; McKnight, Mark L.; Reidarson, Thomas H.; Hanni, Krista D.; Stott, Jeffrey L; Ferrick, David A.

In: Immunogenetics, Vol. 43, No. 4, 1996, p. 190-195.

Research output: Contribution to journalArticle

King, Donald P. ; Schrenzel, Mark D. ; McKnight, Mark L. ; Reidarson, Thomas H. ; Hanni, Krista D. ; Stott, Jeffrey L ; Ferrick, David A. / Molecular cloning and sequencing of interleukin 6 cDNA fragments from the harbor seal (Phoca vitulina), killer whale (Orcinus orca), and Southern sea otter (Enhydra lutris nereis). In: Immunogenetics. 1996 ; Vol. 43, No. 4. pp. 190-195.
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abstract = "Using polymerase chain reaction, interleukin-6 (IL-6) cDNA fragments from harbor seal (Phoca vitulina), killer whale (Orcinus orca), and Southern sea otter (Enhydra lutris nereis) were cloned and sequenced. For all three species, a continuous open reading frame encoding 203 residues for harbor seal, 199 residues for killer whale, and 201 residues for sea otter with stop codons located at analogous positions were identified. These fragments correspond to nucleotides 71-753 of the human IL-6 transcript and represent 96{\%} of the complete coding nucleotides. Comparison of these marine mammal sequences with other published mammalian IL-6 cDNA demonstrated that both harbor seal and sea otter IL-6 had most similarity to that of other terrestrial carnivores (Mustelidae and Canidae), while killer whale had highest identity with ruminants (Bovidae and Ovidae). Among the three marine mammal species characterized, as well as cDNA sequences from nine other species, 40 invariant amino acids, including a number of residues situated at the putative gp80 and gp130 receptor binding sites, were identified. The presence of invariant amino acids within the receptor-binding portion of IL-6 for twelve different species suggests these positions are essential for biological activity of IL-6 and, moreover, likely account for the cross-reactivity among different mammalian IL-6-like activities in mouse bioassays. An additional significant finding was the presence of several variant residues only within the mouse putative IL-6 receptor binding region, which may account for observations of restricted cross-reactivity of mouse IL-6-like activity in human bioassays. Together, these findings provide insights into the evolution of the mammalian IL-6 gene and additional valuable information regarding amino acid residues essential for the biological activity of mammalian IL-6.",
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AU - Ferrick, David A.

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