Bet v 1 potential allergens are involved in anthracnose resistance of strawberry varieties

2021 ◽  
pp. 1-12
Author(s):  
Jing Yang ◽  
Zhiwen Ding ◽  
Jing Wang ◽  
Shuhua Tian ◽  
Ke Duan ◽  
...  
Keyword(s):  
Large Scale ◽  
Mrna Level ◽  
Major Allergen ◽  
Resistant Variety ◽  
Igg Antibody ◽  
Homologous Proteins ◽  
Anthracnose Resistance ◽  
Bet V 1 ◽  
Pathogenesis Related Protein ◽  
Bet V 1 Allergen

BACKGROUND: Bet v 1 family identified as one major plant food allergen class, is highly homologous to pathogenesis-related protein 10 (PR-10), but its biological function involved in disease resistance is still unclear. OBJECTIVE: This study aims to investigate whether Bet v 1 potential allergens participate in the resistance of berry crops against fungal pathogen. METHODS: Allergenicity of Bet v 1 proteins in strawberry (Fragaria) was evaluated by bioinformatics methods. Their expression in response to anthracnose and between susceptible and resistance varieties was analyzed. RESULTS: 19 Bet v 1 homologous proteins were identified and 15 of them were considered as allergen candidates. RNA-seq analysis indicated most of these Fra a 1s expressed in fruits could be largely induced by the invasion of anthracnose pathogen Colletotrichum. The mRNA level of fruit major allergen Fra a 1.05 in the resistant variety Shenyang (SY) was 20∼50 fold higher compared with those in the susceptible cultivar and two diploid wild species. Immunoblotting using Birch (Betula pendula) Bet v 1 allergen-specific IgG antibody confirmed the large-scale accumulation of potential cross-reactive antigens in SY fruit. CONCLUSIONS: Strawberry Bet v 1 potential allergens exhibit their correspondence with anthracnose resistance that might be instructive to future breeding strategies.

scholarly journals Dominant Epitopes and Allergic Cross-Reactivity: Complex Formation Between a Fab Fragment of a Monoclonal Murine IgG Antibody and the Major Allergen from Birch Pollen Bet v 1

2000 ◽  
Vol 165 (1) ◽  
pp. 331-338 ◽  
Author(s):  
Osman Mirza ◽  
Anette Henriksen ◽  
Henrik Ipsen ◽  
Jørgen N. Larsen ◽  
Margit Wissenbach ◽  
...  
Keyword(s):  
Complex Formation ◽  
Birch Pollen ◽  
Major Allergen ◽  
Cross Reactivity ◽  
Igg Antibody ◽  
Fab Fragment ◽  
Bet V 1

Pyr c 1, the major allergen from pear (Pyrus communis), is a new member of the Bet v 1 allergen family

2001 ◽  
Vol 756 (1-2) ◽  
pp. 281-293 ◽  
Author(s):  
Fariba Karamloo ◽  
Stephan Scheurer ◽  
Andrea Wangorsch ◽  
Sibylle May ◽  
Dieter Haustein ◽  
...  
Keyword(s):  
Major Allergen ◽  
Pyrus Communis ◽  
Bet V 1 ◽  
Bet V 1 Allergen

Expanded bed adsorption as a fast technique for the large-scale purification of the complete isoform pool of Ber e 1, the major allergen from Brazil nuts

2006 ◽  
Vol 50 (3) ◽  
pp. 275-281 ◽  
Author(s):  
Evelien L. van Boxtel ◽  
Gerrit A. van Koningsveld ◽  
Stef J. Koppelman ◽  
Lambertus A. M. van den Broek ◽  
Alfons G. J. Voragen ◽  
...  
Keyword(s):  
Large Scale ◽  
Major Allergen ◽  
Expanded Bed Adsorption ◽  
Expanded Bed ◽  
Brazil Nuts

scholarly journals Analysis of Epitope-Specific Immune Responses Induced by Vaccination with Structurally Folded and Unfolded Recombinant Bet v 1 Allergen Derivatives in Man

2007 ◽  
Vol 179 (8) ◽  
pp. 5309-5316 ◽  
Author(s):  
Ines Pree ◽  
Jürgen Reisinger ◽  
Margit Focke ◽  
Susanne Vrtala ◽  
Gabrielle Pauli ◽  
...  
Keyword(s):  
Immune Responses ◽  
Bet V 1 ◽  
Bet V 1 Allergen

scholarly journals In SilicoIdentification of Functional Protein Interfaces

2003 ◽  
Vol 4 (4) ◽  
pp. 420-423 ◽  
Author(s):  
Rachel E. Bell ◽  
Nir Ben-Tal
Keyword(s):  
Phylogenetic Trees ◽  
Large Scale ◽  
Hypothetical Protein ◽  
Evolutionary Information ◽  
Structural Constraints ◽  
Functional Protein ◽  
Homologous Proteins ◽  
Geometrical Properties ◽  
Protein Interfaces ◽  
Branch Lengths

Proteins perform many of their biological roles through protein–protein, protein–DNA or protein–ligand interfaces. The identification of the amino acids comprising these interfaces often enhances our understanding of the biological function of the proteins. Many methods for the detection of functional interfaces have been developed, and large-scale analyses have provided assessments of their accuracy. Among them are those that consider the size of the protein interface, its amino acid composition and its physicochemical and geometrical properties. Other methods to this effect use statistical potential functions of pairwise interactions, and evolutionary information. The rationale of the evolutionary approach is that functional and structural constraints impose selective pressure; hence, biologically important interfaces often evolve at a slower pace than do other external regions of the protein. Recently, an algorithm, Rate4Site, and a web-server, ConSurf (http://consurf.tau.ac.il/), for the identification of functional interfaces based on the evolutionary relations among homologous proteins as reflected in phylogenetic trees, were developed in our laboratory. The explicit use of the tree topology and branch lengths makes the method remarkably accurate and sensitive. Here we demonstrate its potency in the identification of the functional interfaces of a hypothetical protein, the structure of which was determined as part of the international structural genomics effort. Finally, we propose to combine complementary procedures, in order to enhance the overall performance of methods for the identification of functional interfaces in proteins.

scholarly journals In Vivo HP1 Targeting Causes Large-Scale Chromatin Condensation and Enhanced Histone Lysine Methylation

2005 ◽  
Vol 25 (11) ◽  
pp. 4552-4564 ◽  
Author(s):  
Pernette J. Verschure ◽  
Ineke van der Kraan ◽  
Wim de Leeuw ◽  
Johan van der Vlag ◽  
Anne E. Carpenter ◽  
...  
Keyword(s):  
Chromatin Structure ◽  
Mammalian Cells ◽  
Large Scale ◽  
Chromosome Region ◽  
Chromatin Condensation ◽  
Regulation Of Gene Expression ◽  
Lac Repressor ◽  
Homologous Proteins ◽  
Lac Operator

ABSTRACT Changes in chromatin structure are a key aspect in the epigenetic regulation of gene expression. We have used a lac operator array system to visualize by light microscopy the effect of heterochromatin protein 1 (HP1) α (HP1α) and HP1β on large-scale chromatin structure in living mammalian cells. The structure of HP1, containing a chromodomain, a chromoshadow domain, and a hinge domain, allows it to bind to a variety of proteins. In vivo targeting of an enhanced green fluorescent protein-tagged HP1-lac repressor fusion to a lac operator-containing, gene-amplified chromosome region causes local condensation of the higher-order chromatin structure, recruitment of the histone methyltransferase SETDB1, and enhanced trimethylation of histone H3 lysine 9. Polycomb group proteins of both the HPC/HPH and the EED/EZH2 complexes, which are involved in the heritable repression of gene activity, are not recruited to the amplified chromosome region by HP1α and HP1β in vivo targeting. HP1α targeting causes the recruitment of endogenous HP1β to the chromatin region and vice versa, indicating a direct interaction between the two HP1 homologous proteins. Our findings indicate that HP1α and HP1β targeting is sufficient to induce heterochromatin formation.

Ara h 8, a Bet v 1–homologous allergen from peanut, is a major allergen in patients with combined birch pollen and peanut allergy

2004 ◽  
Vol 114 (6) ◽  
pp. 1410-1417 ◽  
Author(s):  
Diana Mittag ◽  
Jaap Akkerdaas ◽  
Barbara K. Ballmer-Weber ◽  
Lothar Vogel ◽  
Marjolein Wensing ◽  
...  
Keyword(s):  
Peanut Allergy ◽  
Birch Pollen ◽  
Major Allergen ◽  
Bet V 1

scholarly journals Bet v 1 allergen is the driver of food allergy in both birch and grass pollen allergic patients

2020 ◽  
Author(s):  
Fran oise Pirson ◽  
Esmeralda Fraille Lopez ◽  
Clo Hupin ◽  
Carine Sohy ◽  
Bertrand Bearzatto ◽  
...  
Keyword(s):  
Food Allergy ◽  
Grass Pollen ◽  
Bet V 1 ◽  
Bet V 1 Allergen

scholarly journals Disease Severity, Resistance Analysis, and Expression Profiling of Pathogenesis-Related Protein Genes after the Inoculation of Fusarium equiseti in Wheat

Agronomy ◽  
2021 ◽  
Vol 11 (11) ◽  
pp. 2124
Author(s):  
Hakim Manghwar ◽  
Amjad Hussain ◽  
Qurban Ali ◽  
Muhammad Hamzah Saleem ◽  
Muyassar H. Abualreesh ◽  
...  
Keyword(s):  
Disease Severity ◽  
Defense Mechanism ◽  
Abiotic Factors ◽  
Wheat Variety ◽  
Resistant Variety ◽  
Pr Genes ◽  
Wheat Varieties ◽  
Fusarium Equiseti ◽  
Resistance Analysis ◽  
Pathogenesis Related Protein

Wheat (Triticum aestivum) is an important cereal crop, grown throughout the temperate and in some tropical and sub-tropical zones, at higher elevations. Several biotic and abiotic factors influence the production of wheat. In the present study, two wheat varieties have been subjected to disease severity and resistance analysis against Fusarium equiseti. Disease severity analysis revealed Shafaq-2006 to be more resistant than Sahar-2006. Both varieties were further subjected to the expression analysis of six important defense-related genes by RT-PCR and quantitative real-time PCR. This analysis revealed that PR-1, TLP, Chitinase, and β-1,3-glucanase genes were highly expressed in Shafaq-2006 and possibly play a significant role in its defense mechanism. In addition, biochemical and physiochemical parameters were also studied to further explore the difference between resistant and susceptible varieties. With total proline and protein contents, sugar and chlorophyll contents also increased significantly in resistant variety. Likewise, higher relative water content, total plant length, and the high root–shoot ratio was observed in resistant plants, compared to susceptible wheat plants. These increases in chemical and physiological parameters might be related to the activation of the defense mechanism due to the higher expression of PR genes in the resistant wheat variety. These genes can further be employed for cloning into wheat and other transgenic crops to develop resistance against F. equiseti.

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