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Purified hevamine demonstrated IgE reactivity with only 1 in 29 latex-allergic sera tested and hence are not considered as an important allergen in inducing latex allergy ( 83) cheap lady era 100mg line womens health resource center lebanon nh. The lack of a hevein-like domain near the N-terminal region of the protein may be responsible for its minimal allergenicity in latex-allergic patients cheap lady era 100mg with visa breast cancer young women statistics. Several other latex allergens have been identified by two-dimensional immunoblotting and microsequencing ( 75) discount lady era 100 mg online womens health daily magazine. These proteins with sequence similarities to spinach order extra super viagra with a mastercard, rice order 400 mg levitra plus with visa, and tomato triose phosphate isomerases and several proteosane subunits are yet to be purified and characterized for their role in latex allergy buy cialis extra dosage toronto. Two-dimensional immunoblot demonstrates more than 200 peptides, with more than 50 spots demonstrating immune reactivity with IgE. This widespread cross-reactivity among various plant proteins may be due to the presence of common T- and B-cell epitopes in them. Although extensive work has been carried out to identify the proteins involved in latex allergy, not much information is available on the cross-reactivity of latex allergens with proteins from other sources. In a recent study, Beezhold and associates demonstrated the co-sensitization between latex and various foods by skin-prick testing ( 120). Cross-reactive allergens in banana appear in several molecular weight ranges between 23 and 47 kDa and in avocado between 27 and 91 kDa ( 121,122 and 123). Akasawa and colleagues identified an avocado chitinase as one of the cross-reacting proteins using sera from latex-allergic patients ( 124). Yagami and co-workers proposed that the pathogenesis-related latex proteins such as chitinase and b-1,3-glucanase are potential cross-reacting proteins because they are common in different plant families and have comparable amino acid sequences and immunologic properties (91). In a recent study, Blanco and colleagues showed that chestnut and avocado type 1 chitinases with N-terminal hevein-like domain are the major allergens that cross-react with latex and suggested that type 1 chitinases are the pan allergens responsible for the latex-fruit syndrome ( 119). The cross-reactivity between fruits, pollen, and latex is also attributed to the highly conserved plant allergen profilin identified in all these different species ( 30). These results demonstrated a mutual boosting effect of pollen and latex sensitization in vivo, which may be seen also in polysensitized plant allergic patients. This study confirmed that mice stimulated with latex proteins develop a predominantly T H2 cytokine response. The results indicated that eosinophils and IgE antibodies play a major role in the immunopathogenesis of latex-induced allergy and anaphylaxis. In another study, latex-immunized mice evaluated by body plethysmography exhibited a significant change in pulmonary conductance (G L) and compliance (Cdyn) consistent with an asthma-like response. The latex-allergic response in this study is unique in that the direct challenge with latex antigen itself resulted in a significant airway response (128). The accumulated data from animal models suggest that the nature of sensitization in patients may be solely dependent on the type of antibody production and the pattern of cytokine expression by allergen-specific T lymphocytes ( 126,127,128 and 129). The studies using crude ammoniated latex, nonammoniated latex cytosol, and extracts demonstrated enhanced lymphoproliferative responses in latex sensitized patients ( 130). The distinct serologic patterns of patients against purified allergens were also reflected in their cell-mediated immune responses against these allergens. The monoclonal antibody affinity purified Hev b 3 exhibited proliferative responses in spina bifida patients, but not in health care workers ( 81).

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