Major Allergen and Its IgE Cross-Reactivity among Salmonid Fish Roe Allergy

2009 ◽  
Vol 57 (6) ◽  
pp. 2314-2319 ◽  
Author(s):  
Yutaka Shimizu ◽  
Atsushi Nakamura ◽  
Hideki Kishimura ◽  
Akihiko Hara ◽  
Kazuhiko Watanabe ◽  
...  
Keyword(s):  
Major Allergen ◽  
Cross Reactivity ◽  
Salmonid Fish ◽  
Fish Roe

scholarly journals Novel Allergen Discovery through Comprehensive De Novo Transcriptomic Analyses of Five Shrimp Species

2020 ◽  
Vol 22 (1) ◽  
pp. 32
Author(s):  
Shaymaviswanathan Karnaneedi ◽  
Roger Huerlimann ◽  
Elecia B. Johnston ◽  
Roni Nugraha ◽  
Thimo Ruethers ◽  
...  
Keyword(s):  
De Novo ◽  
Penaeus Monodon ◽  
Clinical Importance ◽  
Major Allergen ◽  
Cross Reactivity ◽  
Multiple Sequence ◽  
Alpha Tubulin ◽  
Shrimp Species ◽  
Allergen Sources ◽  
Shellfish Allergy

Shellfish allergy affects 2% of the world’s population and persists for life in most patients. The diagnosis of shellfish allergy, in particular shrimp, is challenging due to the similarity of allergenic proteins from other invertebrates. Despite the clinical importance of immunological cross-reactivity among shellfish species and between allergenic invertebrates such as dust mites, the underlying molecular basis is not well understood. Here we mine the complete transcriptome of five frequently consumed shrimp species to identify and compare allergens with all known allergen sources. The transcriptomes were assembled de novo, using Trinity, from raw RNA-Seq data of the whiteleg shrimp (Litopenaeus vannamei), black tiger shrimp (Penaeus monodon), banana shrimp (Fenneropenaeus merguiensis), king shrimp (Melicertus latisulcatus), and endeavour shrimp (Metapenaeus endeavouri). BLAST searching using the two major allergen databases, WHO/IUIS Allergen Nomenclature and AllergenOnline, successfully identified all seven known crustacean allergens. The analyses revealed up to 39 unreported allergens in the different shrimp species, including heat shock protein (HSP), alpha-tubulin, chymotrypsin, cyclophilin, beta-enolase, aldolase A, and glyceraldehyde-3-phosphate dehydrogenase (G3PD). Multiple sequence alignment (Clustal Omega) demonstrated high homology with allergens from other invertebrates including mites and cockroaches. This first transcriptomic analyses of allergens in a major food source provides a valuable resource for investigating shellfish allergens, comparing invertebrate allergens and future development of improved diagnostics for food allergy.

Identification of sole parvalbumin as a major allergen: study of cross-reactivity between parvalbumins in a Spanish fish-allergic population

2011 ◽  
Vol 41 (5) ◽  
pp. 750-758 ◽  
Author(s):  
M. Perez-Gordo ◽  
J. Cuesta-Herranz ◽  
A. S. Maroto ◽  
B. Cases ◽  
M. D. Ibáñez ◽  
...  
Keyword(s):  
Major Allergen ◽  
Cross Reactivity

Cockroach allergens and asthma in Brazil: Identification of tropomyosin as a major allergen with potential cross-reactivity with mite and shrimp allergens☆☆☆★

1999 ◽  
Vol 104 (2) ◽  
pp. 329-337 ◽  
Author(s):  
Ana Beatriz R. Santos ◽  
Martin D. Chapman ◽  
Rob C. Aalberse ◽  
Lisa D. Vailes ◽  
Virginia P.L. Ferriani ◽  
...  
Keyword(s):  
Major Allergen ◽  
Cross Reactivity

The IgE-Binding Regions of the Major Allergen Pen a 1: Multiple Epitopes or Intramolecular Cross-Reactivity?

2001 ◽  
Vol 124 (1-3) ◽  
pp. 103-106 ◽  
Author(s):  
G. Reese ◽  
R. Ayuso ◽  
S.M. Leong-Kee ◽  
M. Plante ◽  
S.B. Lehrer
Keyword(s):  
Major Allergen ◽  
Cross Reactivity ◽  
Ige Binding ◽  
Binding Regions ◽  
Pen A 1

Identification of Linear IgE Epitopes for a Major Allergen–Type I Collagen in Fish (Rainbow Trout)

2018 ◽  
Vol 17 (2) ◽  
pp. 206-213
Author(s):  
Wang Yan-Bo ◽  
Li Xiao-Hui ◽  
Zhou Jin-Ru ◽  
Zhang Yan ◽  
Ma Ai-Jin ◽  
...  
Keyword(s):  
Rainbow Trout ◽  
Type I Collagen ◽  
Solid Phase ◽  
Strong Support ◽  
Major Allergen ◽  
Cross Reactivity ◽  
Type I ◽  
Linear Epitope ◽  
Fish Collagen ◽  
P Type

Type I collagen was described as a major allergen in fish. The purpose of this study was to screen and identify the linear IgE epitopes of type I collagen α1 and α2 subunits in rainbow trout. Five bioinformatics tools were used to predict the potential epitopes and the resultant epitopes were confirmed by LAD2 cells degranulation assay with sera from fish allergic patients. As the result, 10 peptides of α1 and α2 subunits were predicted, respectively, and these peptides were assembled by solid-phase synthesis. 14 epitopes were identified by LAD2 cells degranulation assay, among which, peptide 2, 5–7 were identified as linear epitope of α1 and peptide 11–20 were identified as linear epitope of α2. Moreover, for α1 and α2 subunits, the similarity of sequences was greater than 79%, suggesting the cross-reactivity of fish collagen. The findings of this study provided a strong support for further research of reduction of the collagen allergenicity.

scholarly journals Identification of Allergenic Component Tyr p 8 from Tyrophagus putrescentiae and Cross-Reactivity with Der p 8

2013 ◽  
Vol 20 (4) ◽  
pp. 506-512 ◽  
Author(s):  
En-Chih Liao ◽  
Yi-Hsueh Lin ◽  
Chih-Liang Chiu ◽  
Ting-Chu Lin ◽  
Jaw-Ji Tsai
Keyword(s):  
Sequence Homology ◽  
Positive Response ◽  
Specific Binding ◽  
Major Allergen ◽  
Specific Ige ◽  
Cross Reactivity ◽  
House Dust Mites ◽  
Tyrophagus Putrescentiae ◽  
Serum Samples ◽  
Content Type

ABSTRACTGroup 8 mite allergens exhibit sequence homology to glutathioneS-transferases (GSTs), such as that fromDermatophagoides pteronyssinus(Der p 8). GSTs have been identified as important allergens in studies of allergens from house dust mites, cockroaches, and fungi. Our objective was to purify the native group 8 allergen fromTyrophagus putrescentiae(nTyr p 8) and generate recombinant Tyr p 8 (rTyr p 8) for immunological characterization. The allergenicity was determined by antibody recognition, IgE inhibition, and triggering of the basophil-sensitized release of histamine, usingT. putrescentiaehypersensitivity sera. The results showed that the mRNA transcript of nTyr p 8 is 657 bp long, contains 218 amino acids with a molecular mass of 26 kDa, and exhibits 83% sequence homology to Der p 8. Serum samples from the allergic patients with an IgE-positive response toT. putrescentiaewere analyzed to determine their IgE response to rTyr p 8. The results showed that the sera of 48 subjects (45.3%) had specific IgE against rTyr p 8. However, sera of only 19 subjects (17.9%) had specific IgE against rTyr p 8 afterD. pteronyssinusabsorption. Histamine release was observed fromT. putrescentiae-allergic subjects in the presence of rTyr p 8. Both the nTyr p 8 andT. putrescentiaecrude extract had been demonstrated to possess GST enzymatic activity. Although the specific binding of serum IgE to rTyr p 8 was only 17.9%, which indicates that rTyr p 8 was not a major allergen, the positive response to rTyr p 8 was due to the cross-reactivity with Der p 8. The group 8 mite allergen might be of use in the design of a suitable allergen for diagnosis and for the development of novel immunotherapies.

Pho d 2, a major allergen from date palm pollen, is a profilin: cloning, sequencing, and immunoglobulin E cross-reactivity with other profilins

2005 ◽  
Vol 35 (3) ◽  
pp. 374-381 ◽  
Author(s):  
J. A. Asturias ◽  
I. Ibarrola ◽  
J. Fernandez ◽  
M. C. Arilla ◽  
R. Gonzalez-Rioja ◽  
...  
Keyword(s):  
Date Palm ◽  
Immunoglobulin E ◽  
Major Allergen ◽  
Cross Reactivity ◽  
Date Palm Pollen
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