Evaluation of physiological and molecular effect of variable virulence of Alternaria brassicae isolates in Brassica juncea, Sinapis alba and Camelina sativa

AbstractTo determine resistance of Brassicaceae field crops to Contarinia Róndani (Diptera: Cecidomyiidae) midge complex (Contarinia nasturtii Kieffer and Contarinia undescribed species), field trials of two different host assemblages were undertaken near Melfort, Saskatchewan, Canada in 2014 and repeated in 2015. In both years the first midge adults appeared in early July, when most plants were starting to flower, and a second generation occurred in mid-August, past the period of crop susceptibility. In a trial studying 18 lines of six brassicaceous species, the lowest probability of midge injury was found on Camelina sativa (Linnaeus) Crantz lines in both years. No differences were found in the probability of midge injury among any of the 13 Brassica Linnaeus species lines tested, including commercial glyphosate-resistant and glufosinate-resistant Brassica napus Linnaeus canola lines, Ethiopian mustard (Brassica carinata Braun), brown or oriental mustard (Brassica juncea (Linnaeus) Czernajew), or Polish canola (Brassica rapa Linnaeus) lines. Probability of midge injury on Sinapis alba Linnaeus yellow mustard lines reached levels between those on Camelina sativa lines and those on Brassica lines. A second trial examining 14 current commercial glyphosate-resistant Brassica napus canola cultivars found no differences in susceptibility to midge feeding among any cultivars tested. More plants were damaged in 2015 in both studies, and damage reached maximum levels earlier in 2015 than in 2014.

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Detection and identification of allergens from Canadian mustard varieties of Sinapis alba and Brassica juncea

Biomolecules ◽

10.3390/biom9090489 ◽

2019 ◽

Vol 9 (9) ◽

pp. 489 ◽

Cited By ~ 5

Author(s):

L’Hocine ◽

Pitre ◽

Achouri

Keyword(s):

Brassica Juncea ◽

Protein Extraction ◽

Immunoglobulin E ◽

Sinapis Alba ◽

Cross Reactivity ◽

Protein Profiling ◽

Ige Reactivity ◽

Ige Binding ◽

Reducing Conditions ◽

Detection And Identification

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.

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