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Biochim Biophys Acta. 1996 Feb 7;1305(1-2):87-97.

Molecular cloning and characterization of the major allergen Myr p II from the venom of the jumper ant Myrmecia pilosula: Myr p I and Myr p II share a common protein leader sequence.

Author information

1
Molecular Immunology Unit, Kolling Institute of Medical Research, Royal North Shore Hospital of Sydney, St. Leoonards, NSW, Australia.

Erratum in

  • Biochim Biophys Acta 1996 Jul 15;1307(3):351.

Abstract

A major allergen Myr p II of the Australian jumper ant Myrmecia pilosula has been cloned, immunocharacterized and nucleotide sequenced. An open reading frame of 225 bases was identified and found to encode a deduced amino acid sequence of 75 residues which contained a typical hydrophobic peptide leader sequence. Expressed fusion proteins of Myr p II in both phage and plasmid vectors bind high levels of ant venom-specific IgE and the expressed clones are recognised by 35% of ant venom-allergic individuals. IgE antibodies that recognise the expressed clone have been shown to recognise IgE-binding bands in blots of native venom after separation by SDS-PAGE. The amino acid sequence of Myr p II shares close structural homology with the other major jumper ant allergen Myr p I, differing by only three amino acids in the first 47 residues of both sequences. However, N-terminal analysis of IgE-binding bands derived from Tricine-SDS-PAGE gel blots indicates that both Myr p I and Myr p II undergo extensive post-translational proteolytic processing to unique peptides of 45 and 27 residues, respectively.

PMID:
8605256
[Indexed for MEDLINE]

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