Abstract
Recurring reports of a highly allergenic 42-46-kDa protein in Hevea brasiliensis latex appeared to have been resolved with the discovery of a 43-kDa allergenic latex protein that was a homologue to patatin. However, the low to moderate prevalence of sensitization to the protein, designated Hev b 7, among latex-allergic patients could not adequately explain the frequent observations of the 42-46-kDa allergen. This led to the hypothesis that another, more allergenic protein of a similar molecular mass existed in Hevea latex. We report the isolation and purification of a 42.98-kDa latex glycoprotein showing homology to the early nodule-specific protein (ENSP) of the legumes Medicago sativa, Medicago truncatula, and Glycine max. The protein is allergenic, being recognized by immunoglobulin E (IgE) in sera from latex-allergic patients. The IgE epitope resides on the carbohydrate moiety of the protein, and the presence of a similar carbohydrate component on potato tuber patatin enables the latter to inhibit IgE binding to the ENSP homologue. The cDNA encoding the ENSP homologue was isolated by reverse transcription-PCR and cloned. The protein predicted from the cDNA sequence has 391 amino acids, the first 26 of which constitute a putative signal peptide. The deduced molecular mass of the mature protein is 40.40 kDa, while its isoelectric point is estimated at 5.0. The discrepancy between the predicted and observed molecular mass might be due to glycosylation, for which three N-sites on the protein are predicted. The purified protein showed lipase and esterase activities and may be involved in plant defense.
Highlights
Latex exudes from the bark of the commercial rubber tree, Hevea brasiliensis, when the tree is tapped
We report the isolation and purification of a 42.98-kDa latex glycoprotein showing homology to the early nodule-specific protein (ENSP) of the legumes Medicago sativa, Medicago truncatula, and Glycine max
When the proteins that were independently isolated were all shown to be allergenic, they were classified as Hev b 7, with the protein originating from the latex C-serum designated Hev b 7.01 and that from the latex B-serum designated Hev b 7.02
Summary
Latex exudes from the bark of the commercial rubber tree, Hevea brasiliensis, when the tree is tapped. Originating from the latex bottom fraction, the protein did not show structural features expected of a vacuolar protein, and there is no explanation yet for its presence in the latex B-serum [12] About this time, researchers in England were investigating a 44-kDa proteinaceous rubber biosynthesis inhibitor isolated from the latex C-serum [13, 14]. This deduction received further support when the recombinant protein produced from the DNA was shown to be allergenic [15, 16] These developments notwithstanding, one discrepancy that surfaced was the observation that the numbers of patients who were sensitized to native or recombinant Hev b 7 were far fewer than expected, and this did not reflect the frequent observation of 42– 46-kDa IgE-reactive protein. This paper is available on line at http://www.jbc.org
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