1995
DOI: 10.1016/s0091-6749(95)70318-7
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Allergy to latex, avocado pear, and banana: Evidence for a 30 kd antigen in immunoblotting

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Cited by 134 publications
(50 citation statements)
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“…First, there could be a cross-reaction between latex and mountain cedar in which similar or identical proteins are found in both allergen sources. Cross-reactivity has already been demonstrated between latex and banana, kiwi, chestnut, avocado, and peanut (29,30). Our results using IgG from rabbits specifically immunized with latex glove extract showed the presence of cross-reactive material in mountain cedar extracts in the Western blots.…”
Section: Resultssupporting
confidence: 72%
See 1 more Smart Citation
“…First, there could be a cross-reaction between latex and mountain cedar in which similar or identical proteins are found in both allergen sources. Cross-reactivity has already been demonstrated between latex and banana, kiwi, chestnut, avocado, and peanut (29,30). Our results using IgG from rabbits specifically immunized with latex glove extract showed the presence of cross-reactive material in mountain cedar extracts in the Western blots.…”
Section: Resultssupporting
confidence: 72%
“…By using Western blot analyses to identify human IgE bound to electrophoresis proteins, well over 50 allergenic bands have been reported, with major bands occurring in the 14 and 30 kDa regions (39). Recent studies have shown that the sera of several food-sensitive and latex-sensitive patients recognize a 30 kDa allergen (30). Furthermore, a 36 kDa allergen, frequently encountered by sera of patients with latex allergy (40), has been purified and shows homology to plant endo 1,3-0-glucosidases (41).…”
Section: Resultsmentioning
confidence: 99%
“…Several reports indicate that NRL allergens may crossreact with latex from the weeping fig (Ficus benjamina) [39], and various fruits (banana, avocado, passion fruit, kiwi and chestnut) [40][41][42][43][44]. A recent study suggests that NRL and fruits have common epitopes on 30 kDa proteins [45].…”
Section: Nrl Allergensmentioning
confidence: 99%
“…It is a lectin that belongs to the defense related family of proteins [10,11]. This polypeptide chain is present as a chitin-binding domain in several plant proteins, such as multi-hevein domain lectins and class I chitinases [12,13], which have been associated with cross-reactivity between latex and some fruits [14,15]. Recently, information regarding conformational epitopes of this allergen has been described: Karisola et al [16,17], using, chimeric-hevein, hevein mutants and molecular modeling suggested that the N-terminal and C-terminal regions essentially determined the IgE binding activity.…”
Section: Introductionmentioning
confidence: 99%