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1

The cross-reactivity of Shewanella fidelis lipopolysaccharide with anti-Proteus antibodies

100%
Kwinkowski M., Grabowski S., Konieczna I., Nazarenko E. L., Kaca W.
Polish Journal of Microbiology
|
2009
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tom 58
|
nr 3
275-278
The serological cross-reactivity between lipopolysaccharides (LPS) of S.fidelis KMM3582Τ and rabbit anti-O P. mirabilis antibodies was tested. Using ELISA and Western blot cross-reactivity between S.fidelis LPS and antisera against P. mirabilis O14, O3 LPSs was found. The observed cross-reaction may suggest that anti-E mirabilis S1959 (03) antibodies may bind to the internal part of S. fidelis O-polysaccharides. A weak interaction between S. fidelis LPS and antiserum against P. mirabilis O13 in Western blot suggests that the absolute configuration of non-sugar "AlaLys" component (Nε-[(S)-l-carboxyethyl]-Nα-(D-galacturonoyl)-L-lysine) may influence the affinity of antibodies for S. fidelis LPS.
2

Cross-recognition of Fagaceae pollen allergen by IgE raised against allergen of Cupressus arizonica pollen

100%
Mazzitelli A., Caiola M. G.
Acta Biologica Cracoviensia. Series Botanica
|
2003
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tom 45
|
nr 1
This study investigated cross-reactivity between allergens of Cupressaceae and Fagaceae pollen. Human IgE raised against Cupressus arizonica pollen allergen was used to demonstrate the presence of related allergens on ultrathin sections of Fagaceae pollen (Quercus ilex, Castanea sativa, Fagus sylvatica). Tissue localization of the cross-reactive allergen was investigated by immunogold electron microscopy. TEM observations showed that IgE raised against C. arizonica allergen recognizes epitopes on Fagaceae pollen. The cross-reactive allergens can be found on the wall and in the cytoplasm.
3
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Peanut allergenicity and cross-reactivity with pea proteins in the in vivo model

80%
Szymkiewicz A., Chudzik-Kozlowska J.
Polish Journal of Food and Nutrition Sciences
|
2013
|
tom 63
|
nr 1
The aim of the study was to analyse the potential pea-peanut cross-reactivity using the mice BALB/c as a biological in vivo model in the research on immune response to peanut proteins (PnE). BALB/c mice were three-fold sensitised (on days 1, 7, and 21) by oral or intraperitoneal (IP) administration of PnE in 0.5 mg or 1 mg dose, with or without adjuvant – aluminum hydroxide gel (Alum). Serum immunoglobulins (IgE, IgG, IgG1 and IgG2a) and level of cytokines (IL-4, IL-10, IFN- γ), secreted by the isolated lymphocytes were examined. The highest increase in total IgE and peanut-specific IgG1 was noted in the group sensitised by IP administration of PnE in the presence of Alum. Lymphocytes from peanut-sensitised (with and without Alum) mice showed a significantly high level of IL-4 and this cytokine was secreted to a much higher extent as compared to IFN-γ. Stimulation of a culture of lymphocytes with pea proteins resulted in high IFN-γ secretion. A weak reaction of peanut-specific IgG1 present in mice serum with pea globulins (vicilin – PV and legumin – PL) can suggest that the cross-reactivity between peanut and pea proteins results from the presence of proteins other than 7S and 11S globulins. Due to the demonstrated low cross-reactivity between peanut proteins and pea globulins, the possibility of applying pea proteins in peanut-allergy immunotherapy may be suggested.
4
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Characterisation of pollen allergens

80%
Puc M.
Annals of Agricultural and Environmental Medicine
|
2003
|
tom 10
|
nr 2
5

Antigenic relationships between Aggregata octopiana and A. eberthi two parasites of cephalopods

80%
Rodriguez H., Crespo C., Soto M., Arias C., Iglesias R., Garcia-Estevez M.
Acta Protozoologica
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2003
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tom 42
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nr 3
6
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Allergenicity of lupine proteins - a review

80%
Loza A., Lampart-Szczapa E.
Polish Journal of Food and Nutrition Sciences
|
2008
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tom 58
|
nr 3
In Europe, the application of lupine seeds to produce food has increased significantly in recent years. Lupine (flour, seeds or dust) can induce different allergic responses. Consumption of lupine-fortified products may also provoke allergy syndromes. This article reviews the adverse reactions to lupine, after various contacts with this plant, including eating lupine products and seeds. It discusses cases which confirm properties of lupine protein as a primary allergen. It describes lupine protein cross-reactivity and the modifying effect of thermal processes on lupine protein.
7
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Aeroallergens in clinical practice of allergy in India. An overview

80%
Singh A. B., Kumar P.
Annals of Agricultural and Environmental Medicine
|
2003
|
tom 10
|
nr 2
8
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Antigenic relationship between four airborne palm pollen grains from Calcutta, India

80%
Chowdhury I., Chakraborty P., Gupta-Bhattacharya S., Chanda S.
Annals of Agricultural and Environmental Medicine
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1999
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tom 06
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nr 1
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