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 ◽  
...  
2021 ◽  
Vol 42 (5) ◽  
pp. e145-e151
Author(s):  
Francesco Papia ◽  
Chiara Bellia ◽  
Carina Gabriela Uasuf

Background: Panallergens are proteins that take part in key processes of organisms and, therefore, are ubiquitously distributed with highly conserved sequences and structures. One class of these panallergens is composed of the tropomyosins. The highly heat-stable tropomyosins comprise the major allergens in crustaceans and mollusks, which make them important food allergens in exposed populations. Tropomyosins are responsible for a widespread immunoglobulin E cross-reactivity among allergens from different sources. Allergic tropomyosins are expressed in many species, including parasites and insects. Methods: This panallergen class is divided, according to it capacity of induced allergic symptoms, into allergenic or nonallergenic tropomyosin. Although vertebrate tropomyosins share ∼55% of sequence homology with invertebrate tropomyosins, it has been thought that the invertebrate tropomyosins would not have allergic properties. Nevertheless, in recent years, this opinion has been changed. In particular, tropomyosin has been recognized as a major allergen in many insects. Results: A high grade of homology has been shown among tropomyosins from different species, such as crustaceans and insects, which supports the hypothesis of cross-reactivity among tropomyosins from divergent species. Moreover, the emerging habit of consuming edible insects has drawn the attention of allergists to invertebrate tropomyosin protein due to its potential allergenic risk. Nevertheless, evidence about tropomyosin involvement in clinical allergic response is still scarce and deserves more investigation. Conclusion: This review intended to report allergic reactions associated with different tropomyosins when considering house dust mites, parasites, seafood, and insects, and to summarize our current knowledge about its cross-reactivity because this could help physicians to accurately diagnose patients with food allergy.


2020 ◽  
Vol 22 (1) ◽  
pp. 32
Author(s):  
Shaymaviswanathan Karnaneedi ◽  
Roger Huerlimann ◽  
Elecia B. Johnston ◽  
Roni Nugraha ◽  
Thimo Ruethers ◽  
...  

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.


Animals ◽  
2021 ◽  
Vol 11 (3) ◽  
pp. 886
Author(s):  
Samar S. Elblehi ◽  
Yasser S. El-Sayed ◽  
Mohamed Mohamed Soliman ◽  
Mustafa Shukry

Doxorubicin (DOX) has a potent antineoplastic efficacy and is considered a cornerstone of chemotherapy. However, it causes several dose-dependent cardiotoxic results, which has substantially restricted its clinical application. This study was intended to explore the potential ameliorative effect of date palm pollen ethanolic extract (DPPE) against DOX-induced cardiotoxicity and the mechanisms underlying it. Forty male Wistar albino rats were equally allocated into Control (CTR), DPPE (500 mg/kg bw for 4 weeks), DOX (2.5 mg/kg bw, intraperitoneally six times over 2 weeks), and DPPE + DOX-treated groups. Pre-coadministration of DPPE with DOX partially ameliorated DOX-induced cardiotoxicity as DPPE improved DOX-induced body and heart weight changes and mitigated the elevated cardiac injury markers activities of serum aminotransferases, lactate dehydrogenase, creatine kinase, and creatine kinase-cardiac type isoenzyme. Additionally, the concentration of serum cardiac troponin I (cTnI), troponin T (cTnT), N-terminal pro-brain natriuretic peptide (NT-pro BNP), and cytosolic calcium (Ca+2) were amplified. DPPE also alleviated nitrosative status (nitric oxide) in DOX-treated animals, lipid peroxidation and antioxidant molecules as glutathione content, and glutathione peroxidase, catalase, and superoxide dismutase activities and inflammatory markers levels; NF-κB p65, TNF-α, IL-1β, and IL-6. As well, it ameliorated the severity of histopathological lesions, histomorphometric alteration and improved the immune-staining of the pro-fibrotic (TGF-β1), pro-apoptotic (caspase-3 and Bax), and anti-apoptotic (Bcl-2) proteins in cardiac tissues. Collectively, pre-coadministration of DPPE partially mitigated DOX-induced cardiac injuries via its antioxidant, anti-inflammatory, anti-fibrotic, and anti-apoptotic potential.


Italus Hortus ◽  
2020 ◽  
Vol 27 (3) ◽  
pp. 64-71
Author(s):  
Mohammed Mesnoua ◽  
Messaoud Roumani ◽  
Ouahiba Mizab ◽  
Reguia Zeguerrou

2014 ◽  
Vol 38 (2) ◽  
pp. 41-47
Author(s):  
Salah M. M. AL-Chalabi

     The present study was undertaken to evaluate the effect of aqueous extract of Date Palm Pollen DPP on the testicular function and serum testosterone, FSH and LH hormones value. Thirty five male rats were divided randomly into five equal groups. Group 1: received 0.5 ml of distilled water (control group), group 2: was treated orally 0.250 p.p.m of sodium florid (NaF) (with volume of 0.5 ml / rat), Group 3: was treated with 0.250 p.p.m of NaF and 50 mg/kg. B.W. of DPP extract (0.5ml D.W \rat), Group 4: was treated with 0.250 p.p.m of NaF and 100 mg/kg. B.W. of DPP extract and Group 5: was treated with 0.250 p.p.m of NaF and 150 mg/kg. B.W. of DPP extract. The results showed  significant (P< 0.05) decrease in sperm concentration, motility and significant (P< 0.05) increases in dead and abnormal sperm in the group 2 in comparison to control, while all groups of  DPP extract showed significant (P< 0.05) increase in  sperm concentration, motility and decrease in dead and abnormal sperm. Maximum effect was observed in animals treated with a dose of 150 mg/kg of DPP extract, also the results revealed significant (P< 0.05) increase in testosterone, FSH and LH hormones in groups treated with DDP in comparison to G1andG2. Male rats received DPP for 50 days showed significant (P< 0.05) increases in body and testes weight as compared to G1andG2. In conclusion the results revealed that the aqueous extract of DPP pollen can be used as a sex enhancer and seems to cure male infertility.


Biomolecules ◽  
2019 ◽  
Vol 9 (9) ◽  
pp. 489 ◽  
Author(s):  
L’Hocine ◽  
Pitre ◽  
Achouri

Currently, information on the allergens profiles of different mustard varieties is rather scarce. Therefore, the objective of this study was to assess protein profiles and immunoglobulin E (IgE)-binding patterns of selected Canadian mustard varieties. Optimization of a non-denaturing protein extraction from the seeds of selected mustard varieties was first undertaken, and the various extracts were quantitatively and qualitatively analyzed by means of protein recovery determination and protein profiling. The IgE-binding patterns of selected mustard seeds extracts were assessed by immunoblotting using sera from mustard sensitized and allergic individuals. In addition to the known mustard allergens—Sin a 2 (11S globulins), Sin a 1, and Bra j 1 (2S albumins)—the presence of other new IgE-binding protein bands was revealed from both Sinapis alba and Brassica juncea varieties. Mass spectrometry (MS) analysis of the in-gel digested IgE-reactive bands identified the unknown ones as being oleosin, β-glucosidase, enolase, and glutathione-S transferase proteins. A bioinformatic comparison of the amino acid sequence of the new IgE-binding mustard proteins with those of know allergens revealed a number of strong homologies that are highly relevant for potential allergic cross-reactivity. Moreover, it was found that Sin a 1, Bra j 1, and cruciferin polypeptides exhibited a stronger IgE reactivity under non-reducing conditions in comparison to reducing conditions, demonstrating the recognition of conformational epitopes. These results further support the utilization of non-denaturing extraction and analysis conditions, as denaturing conditions may lead to failure in the detection of important immunoreactive epitopes.


2004 ◽  
Vol 34 (11) ◽  
pp. 1762-1767 ◽  
Author(s):  
F. C. Yi ◽  
K. Y. Chua ◽  
N. Cheong ◽  
L. P. Shek ◽  
B. W. Lee

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