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(Received for publication, April 5, 1996, and in revised form, July 24, 1996)
From the Division of Allergenic Products and Parasitology, Center
for Biologics Evaluation and Research, Food and Drug Administration,
Rockville, Maryland 20852 and the ¶ Unit on Molecular Structures,
Clinical Neuroscience Branch, National Institute of Mental Health,
Bethesda, Maryland 20892
Latex allergy is recognized as a serious health
problem among health care workers and children with spina bifida. A
number of IgE-reactive proteins have been identified in natural and
processed latex products. One of the most acidic proteins in the
cytoplasm of lacticifer cells of rubber trees (Hevea
brasiliensis) is demonstrated to be a potent allergen in
eliciting allergic reactions in humans. This protein, with pI = 3.5, has a molecular mass of 16 kDa with a blocked N terminus and an
unusual amino acid composition. This acidic protein was found in
extracts prepared from latex gloves, which were shown to be allergenic.
The purified protein elicits histamine release from human basophils
passively sensitized with serum from latex-allergic individuals in a
dose-dependent manner.
From a latex cDNA library, the cDNA coding for this protein was
isolated and sequenced. The deduced amino acid sequence shows a high
degree of homology to another acidic protein identified in kiwifruit
(Actinidia deliciosa var. deliciosa). The
sequence homology (47% sequence identity) between these two acidic
proteins suggests a molecular explanation for the high frequency of
fruit hypersensitivity in latex-allergic patients.
Volume 271, Number 41,
Issue of October 11, 1996
pp. 25389-25393
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
PURIFICATION, CLONING AND CHARACTERIZATION
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