2017
DOI: 10.1080/09540105.2017.1306493
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Expression of recombinant parvalbumin from wolf-herring fish and determination of its IgE-binding capability

Abstract: In this study, we produced the recombinant form of parvalbumin from wolf-herring fish and determined its IgE reactivity. Parvalbumin cDNA was sub-cloned into pET28 and expressed in Escherichia coli BL-21. The immunoreactivities of the recombinant and native parvalbumins were compared, and the effect of calcium binding was determined by sera from 25 fish-allergic patients. ELISA and Western blotting confirmed similar IgEreactivities of the recombinant and native proteins and confirmed that this phenomenon is hi… Show more

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Cited by 9 publications
(5 citation statements)
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“…Splenocytes of mice immunized with HBc VLPs alone or HBc VLP mixed with allergen induced a high level of IFN-g when only stimulated with HBc VLPs (no with rChe a 3), while splenocytes of mice immunized with chimeric HBc VLPs produced high IFN-g when stimulated with either HBc VLPs or rChe a 3. p values less than 0.05 were regarded as statistically significant that were calculated by multiple t test and one-way ANOVA polcalcins) depends on their three-dimensional structure (Mohammadi et al 2017;Swoboda et al 2007;Westritschnig et al 2004). These studies indicated that a disruption or alteration in the three-dimensional structures of two EF-hand calcium-binding allergens, by mutations in the calcium-binding site or fragmentation, led to the generation of a hypoallergenic variant (Mohammadi et al 2017;Swoboda et al 2007;Westritschnig et al 2004). Consistent with these results, the basophil activation test demonstrated that chimeric HBc VLP and C. Che a 3 peptide at same the level exhibited very low basophil degranulationtriggering ability compared to that triggered by rChe a 3.…”
Section: Discussionmentioning
confidence: 99%
“…Splenocytes of mice immunized with HBc VLPs alone or HBc VLP mixed with allergen induced a high level of IFN-g when only stimulated with HBc VLPs (no with rChe a 3), while splenocytes of mice immunized with chimeric HBc VLPs produced high IFN-g when stimulated with either HBc VLPs or rChe a 3. p values less than 0.05 were regarded as statistically significant that were calculated by multiple t test and one-way ANOVA polcalcins) depends on their three-dimensional structure (Mohammadi et al 2017;Swoboda et al 2007;Westritschnig et al 2004). These studies indicated that a disruption or alteration in the three-dimensional structures of two EF-hand calcium-binding allergens, by mutations in the calcium-binding site or fragmentation, led to the generation of a hypoallergenic variant (Mohammadi et al 2017;Swoboda et al 2007;Westritschnig et al 2004). Consistent with these results, the basophil activation test demonstrated that chimeric HBc VLP and C. Che a 3 peptide at same the level exhibited very low basophil degranulationtriggering ability compared to that triggered by rChe a 3.…”
Section: Discussionmentioning
confidence: 99%
“…This host has been used to express a variety of food allergens, including allergens from peanut (Ara 62], pistachio nut (MnSOD) [63], hazelnut (Cor a 8) [64] and wolf herring (parvalbumin) [65]. Most studies do not explicitly describe the reason for choosing E. coli as the host organism, but most likely this is due to the ease of engineering, the high growth rate, low maintenance, and ability to produce proteins on a large scale [66].…”
Section: The Most Widely Used Expression Host For Recombinant Proteins Is Escherichia Coli (E Coli)mentioning
confidence: 99%
“…These conditions have been used for production of major allergens from fish [60,81,82], shellfish [83,84], hen's egg [67,85], peanut [47,49,50,72] and tree nuts [86][87][88][89][90][91][92][93]. Some studies reported increased yield and solubility of recombinant food allergens by lowering expression temperature [48,65,[94][95][96][97] or inducer concentration [63,95,98].…”
Section: Production Recovery and Purification Of Recombinant Food Allergensmentioning
confidence: 99%
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“…The authors reported that this allergen form, devoid of Ca 2+ , showed a IgE-reactivity reduction of around 30% ( Apold and Elsayed, 1979 ). More recently, Mohammadi et al (2017) showed a significantly decreased IgE-reactivity of the EDTA-treated wolf-herring parvalbumin, compared to the native protein. Additionally, other authors using a different chelating agent, the ethyleneglycoltetraacetic acid (EGTA), achieved similar results and conclusions regarding parvalbumin’s stability and immunoreactivity ( Bugajska-Schretter et al, 1998 ; Tomura et al, 2008 ; Kobayashi et al, 2016a ).…”
Section: Introductionmentioning
confidence: 99%