Correspondence to H. Breiteneder, Department of General and Experimental Pathology, University Hospital, AKH-EBO-3Q, Waehringer Guertel 18−20, A-1090 Vienna, Austria
cDNA cloning of the 43-kDa latex allergen Hev b 7 with sequence similarity to patatins and its expression in the yeast Pichia pastoris
Article first published online: 25 DEC 2001
European Journal of Biochemistry
Volume 255, Issue 1, pages 213–219, July (I) 1998
How to Cite
Sowka, S., Wagner, S., Krebitz, M., Arija-Mad-Arif, S., Yusof, F., Kinaciyan, T., Brehler, R., Scheiner, O. and Breiteneder, H. (1998), cDNA cloning of the 43-kDa latex allergen Hev b 7 with sequence similarity to patatins and its expression in the yeast Pichia pastoris. European Journal of Biochemistry, 255: 213–219. doi: 10.1046/j.1432-1327.1998.2550213.x
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Abbreviations. RAST, radioallergosorbent test; NRL, natural rubber latex; PNGase F, peptide N-glycosidase F; pfu, plaque-forming units.
Enzyme. Peptide N-glycosidase F ( EC126.96.36.199).
Note. The nucleotide sequence reported in this paper has been submitted to the EMBL database and assigned the accession number AJ223038.
- Issue published online: 25 DEC 2001
- Article first published online: 25 DEC 2001
- (Received 13 March/21 April 1998)
- Cited By
- latex allergy;
- Hev b 7;
- Pichia pastoris;
- type-I allergy.
IgE-mediated hypersensitivity to latex proteins present in health care products, particularly in latex gloves, has become an important public health problem in recent years. We purified natural Hev b 7, a 43-kDa patatin-like allergen from the latex of Hevea brasiliensis and determined several internal peptide sequences. A heterologous hybridization probe of a patatin gene of potato, to which these peptides could be aligned best, was used to screen a latex cDNA library. The cDNA encoded an acidic protein of 388 amino acids with a molecular mass of 42.9 kDa. The deduced amino acid sequence had 39−42 % identity to patatins from Solanum tuberosum. The purified recombinant Hev b 7 expressed in the yeast Pichia pastoris displayed, similarly to patatins from S. tuberosum, esterase activity. Both natural and recombinant Hev b 7 were recognized by IgE from sera of latex-sensitized allergic individuals. In contrast to patatins from S. tuberosum and Nicotiana tabacum, natural Hev b 7 lacked an N-terminal leader peptide for targeting to the endoplasmatic reticulum and was not glycosylated. These results establish the 43-kDa patatin-like protein as a latex allergen and raise the possibility of different cellular localization and function compared to S. tuberosum patatins.