A correlation between symptom severity and unbalanced reactive IgA production in Japanese cedar pollinosis patients.

To better understand the unbalanced immunoglobulin production that occurs in pollinosis, we measured the levels of IgG, IgA, and IgE reactive to either Japanese cedar pollen, Cry j 1 protein, or Cry j 2 protein in the sera of pollinosis patients. As expected, the levels of these immunoglobulins (Igs) reactive to the three antigens were significantly higher in the patients than in the controls, and the RAST scores correlated with the levels of these Igs. Only the levels of IgA reactive to the Cry j 2 protein and IgG reactive to the Japanese cedar pollen antigen did not correlate with the RAST scores. We classified the patients into mild and severe, based on the severity of their allergic symptoms, and compared their levels of Igs. As expected, the levels of IgE reactive to Japanese cedar pollen and Cry j 1 of the severe group were significantly higher than those of the mild group. It is of note that the ratio of anti-Cry j 1 IgE to anti-Japanese cedar pollen IgA was significantly higher in the patients with severe symptoms suggesting that decreased IgA production could be responsible for the severity of pollinosis.

Hydrophobic allergens from the bottom fraction membrane of Hevea brasiliensis.

Several proteins of rubber latex have been recognized as allergens causing immediate hypersensitivity in humans. In this study, a bottom fraction membrane (BFM) protein preparation from Hevea brasiliensis trees grown in southern Thailand was used to detect specific IgE in four groups of serum samples. The first group included 170 samples of latex glove factory workers (LGWs); group 2 consisted of the sera of 35 health care workers (HCWs) who were repeatedly exposed to powdered latex gloves; groups 3 and 4 were 31 positive and 22 negative sera, respectively, obtained from Johns Hopkins University School of Medicine, Baltimore, USA, tested for IgE to latex allergen. It was found that 56/170 (33%), 5/35 (14%), 11/31 (35.5%) and 1/22 (4.5%) samples of the LGWs, HCWs, CAP+ and CAP- groups had significant IgE to the BFM proteins, respectively. However, of all subjects only one subject of group 1 had experienced allergic morbidity consisting of eczema, conjunctivitis and asthma. The IgE of this subject bound to a 55 kDa component in the rubber latex BFM preparation. Thus, this protein may be regarded as a novel, although minor, latex allergen. Further investigation is needed to characterize the component and to pinpoint its allergenic role.

A comparison study on allergen components between Korean (Arachis fastigiata Shinpung) and American peanut (Arachis hypogaea Runner)

The prevalence of peanut allergy in Korea is lower than in America. Peanut extract allergens between the two countries have not been standardized. This study was performed to compare the allergenicity of raw Korean and American peanuts with that of roasted peanuts. We prepared the peanut extracts in Korean raw (KP) and roasted peanuts (KRP), and also in American raw (AP) and roasted (ARP) peanuts. We compared the peanut extract allergens of KP, KRP, AP and ARP in vitro with sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) followed by immunoblotting, T-cell proliferation assay and skin prick test with sera from peanut-allergic patients. SDS-PAGE and Western blotting demonstrated four allergenic extracts, numerous bands that displayed a high prevalence of IgE binding. IgE-binding bands were at 64, 36 and 17 kDa. Western blot inhibition revealed that either KP or AP could almost completely inhibit the reactivity of the other extract. There were no differences between T-cell proliferation assay and skin prick test. In conclusion, this investigation showed no different allergic components in both raw and roast extracts of Korean and American peanuts.

Isolation of rice allergenic cDNA clones from a rice cDNA library by immunoscreening with a polyclonal antibody specific to 16 kD rice allergenic protein

Clinical cases of type-1 hypersensitive reaction to rice (Oryza sativa) have been reported in western countries as well as in Japan. Among rice proteins, 14-16 kD globulin proteins encoded by multiple gene family have been identified as major rice allergens. In this study, a rice cDNA library was constructed using lambda UniZap vector and screened with a rat anti-16 kD globulin protein polyclonal antibody in order to isolate Korean rice allergenic cDNA clones. Five independent cDNA clones, termed RAK1-5, were obtained after second rounds of plaque assay and immunoblot analysis. These clones encoded 13-19 kD recombinant proteins upon IPTG induction, which were identified by the polyclonal antibody in immunoblot analysis. DNA sequencing analysis showed that RAK1-4 have 99% sequence homology with RA5b, and RAK5 is closely related with RA14c. This result indicated that RA5b gene is widely distributed in our cDNA library among other possible rice allergenic genes, and more study is needed to isolate heterogeneous or novel rice allergen genes. Copyright 2000 Academic Press.

Efecto de la combustión del tabaco en la propiedad inmunoquímicas de la albúmina / Effect of tobacco smoke in the immunochemistry properties of albumin

Las condiciones en que se realiza la combustión del tabaco durante el acto de fumar favorecen el arrastre de diferentes componentes del cigarrillo, incluyéndose los que se generan en la ignición y que llegan al aparato respiratorio del sujeto que aspira el humo del tabaco. En el extremo de la combustión del cagarrillo la temperatura alcanza 600ºC pero en el punto opuesto, que se pone en contacto con los labios del fumador, la temperatura es menor; por lo anterior se considera que en el cigarrillo se forma un gradiente de temperatura que puede ser capaz de transportar los productos del tabaco. Para demostrar que sí es posible encontrar componentes inmunorreactivos en el humo del tabaco se diseñó un modelo en el cual se usaron dos series de cigarrillos. La serie experimental de cigarrillos fue inyectada con distintas concentraciones de una solución de albúmina sérica bovina (albúmina sérica bovina) y la control recibió salina-fosfato (SSF) sin ninguna proteína. Ambos grupos de cigarrillos permanecieron a 20ºC durante 48 horas para permitir su secado. Posteriormente, se procedió a la combustión de cada serie por separado y el condensado del humo del tabaco producido se dejó en solución salina-fosfato. Los condensados de humo del tabaco derivados de los cigarrillos con mayor concentración de albúmina sérica bovina presentaron más proteína total que los cigarrillos controles. La identificación de la albúmina sérica bovina, que previamente se había colocado en los cigarrillos, se realizó con técnicas inmunoserológicas en las cuales se demostró una banda correspondiente a la albumina sérica bovina, la cual fue revelada con los anticuerpos policlonales anti-albúmina sérica bovina. Los condensados de humo del tabaco producidos con cigarrillos sin albúmina sérica bovina no reaccionaron con los anticuerpos anti-albúmina sérica bovina. La cuantificación de la albvúmina sérica bovina en cada conjunto de cigarrillos mostró de 15 a 601 mcg por cada cigarrillo, de acuerdo con la dosis de albúmina sérica bovina aplicada inicialmente. Se concluye que una fracción de la proteína puesta a los cigarrillos conserva su inmunorreactividad en el condensado del humo del tabaco; por lo cual es posible que los sujetos fumadores al aspirar el humo se pongan en contacto con estructuras del tabaco que desencadenan una respuesta inmunitaria anti-tabaco

Cocos nucifera pollen inducing allergy: sensitivity test and immunological study.

Among the heterogeneous population (n = 975) in greater Calutta, sensitization to Cocos nucifera pollen accounts to be 2.65% and for atopic patients (n = 204) 47.06%. Out of 24 patients who had C. nucifera pollen sensitivity and suffered from asthma and allergic rhinitis, 16 showed sensitivity also to other allergens. All were skin test positive and 19 of them were phadezym RAST positive to C. nucifera pollen extract. Bronchial provocation test appeared to be positive in 7 out of 8 patients included in the test and no late response or non-specific reactions were observed. C. nucifera pollen extract on fractionation by ion-exchange chromatography following gel filtration yielded two major allergenic protein fractions, CnII (M(r) 158,000) and CnVII (M(r) 2900) as evidenced by skin prick test, ELISA-inhibition and immunoblot analysis. Hence, C. nucifera pollen should be considered to be a relevant allergen and thus included in the panel of allergens for routine clinical use.