Molecular and immunological characterization of wheat <scp>S</scp>erpin (<scp>T</scp>ri a 33)

Mameri, Hamza; Denery-Papini, Sandra; Pietri, Mathéa; Tranquet, Olivier; Larré, Colette; Drouet, M.; Paty, E.; Jonathan, Anne-Marie; Beaudouin, É.; Moneret‐Vautrin, D.A.; Moreau, Thierry; Briozzo, Pierre; Gaudin, Jean-Charles

doi:10.1002/mnfr.201200244

Cited by 21 publications

(18 citation statements)

References 31 publications

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“…Additionally, our efforts to use an in vitro refolded r Aam S6 were unsuccessful in that the refolded protein was digested by the test protease (unpublished data). There are reported studies where serpins expressed as soluble fractions in E. coli showed inhibitory functions (An et al ., ; Mameri et al ., ), which may suggest that glycosylation may not be important to serpin function. In conclusion, data reported in the present study advance our knowledge of the understanding of tick feeding physiology regulation, and provide some insight into the putative roles of Aam S6 at the tick feeding site.…”

Section: Discussionmentioning

confidence: 99%

Amblyomma americanum tick saliva serine protease inhibitor 6 is a cross‐class inhibitor of serine proteases and papain‐like cysteine proteases that delays plasma clotting and inhibits platelet aggregation

Mulenga

Kim

Ibelli

2013

Insect Molecular Biology

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We previously demonstrated that Amblyomma americanum tick serine protease inhibitor 6 (AamS6) was secreted into the host during tick feeding and that both its mRNA and protein were ubiquitously and highly expressed during the first 3 days of tick feeding. This study demonstrates that AamS6 is a cross-class inhibitor of both serine- and papain-like cysteine proteases that has apparent antihaemostatic functions. Consistent with the typical inhibitory serpin characteristics, enzyme kinetics analyses revealed that Pichia pastoris-expressed recombinant (r) AamS6 reduced initial velocities of substrate hydrolysis (V0) and/or maximum enzyme velocity (Vmax) of trypsin, chymotrypsin, elastase, chymase, and papain in a dose–response manner. We speculate that rAamS6 inhibited plasmin in a temporary fashion in that while rAamS6 reduced V0 of plasmin by up to ~53%, it had no effect on Vmax. Our data also suggest that rAmS6 has minimal or no apparent effect on V0 or Vmax of thrombin, factor Xa, and kallikrein. We speculate that AamS6 is apparently involved in facilitating blood meal feeding in that various amounts of rAamS6 reduced platelet aggregation by up to ~47% and delayed plasma clotting time in the recalcification time assay by up to ~210 s. AamS6 is most likely not involved with the tick’s evasion of the host’s complement defense mechanism, in that rAamS6 did not interfere with the complement activation pathway. Findings in this study are discussed in the context of expanding our understanding of tick proteins that control bloodmeal feeding and hence tick-borne disease transmission by ticks.

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Section: Discussionmentioning

confidence: 99%

Amblyomma americanum tick saliva serine protease inhibitor 6 is a cross‐class inhibitor of serine proteases and papain‐like cysteine proteases that delays plasma clotting and inhibits platelet aggregation

Mulenga

Kim

Ibelli

2013

Insect Molecular Biology

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“…No differences were identified in the IgE-binding epitope peptides associated with food allergy and baker's asthma. 105 Tri a 27 was identified as an allergen that causes wheat protein contact dermatitis and wheat food allergy. 114,134,135 It is considered that the N-linked glycan moieties with fucose residues contained in this allergen are involved in IgE-binding.…”

Section: Water/salt-soluble Wheat Allergensmentioning

confidence: 99%

Common food allergens and their IgE-binding epitopes

Matsuo

Yokooji

Taogoshi

2015

Allergology International

196

135

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Food allergy is an adverse immune response to certain kinds of food. Although any food can cause allergic reactions, chicken egg, cow's milk, wheat, shellfish, fruit, and buckwheat account for 75% of food allergies in Japan. Allergen-specific immunoglobulin E (IgE) antibodies play a pivotal role in the development of food allergy. Recent advances in molecular biological techniques have enabled the efficient analysis of food allergens. As a result, many food allergens have been identified, and their molecular structure and IgE-binding epitopes have also been identified. Studies of allergens have demonstrated that IgE antibodies specific to allergen components and/or the peptide epitopes are good indicators for the identification of patients with food allergy, prediction of clinical severity and development of tolerance. In this review, we summarize our current knowledge regarding the allergens and IgE epitopes in the well-researched allergies to chicken egg, cow's milk, wheat, shrimp, and peanut.

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“…The present study was particularly successful in the detection of wheat grain allergens associated with Baker’s asthma (Salcedo et al, 2011; Olivieri et al, 2013). Five 2-DE spots were identified as serpin ( Table 1 ; Figure 3 ), which are involved in food allergy and Baker’s asthma (Salcedo et al, 2011; Mameri et al, 2012). Three 2-DE spots were identified as an α-amylase inhibitor, important contributors to Baker’s asthma (Tatham and Shewry, 2008; Salcedo et al, 2011), food allergies (James et al, 1997), and WDEIA (Hofmann et al, 2012).…”

Section: Discussionmentioning

confidence: 99%

Using 7 cm immobilized pH gradient strips to determine levels of clinically relevant proteins in wheat grain extracts

et al. 2015

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The aim of the work was to test a relatively simple proteomics approach based on phenol extraction and two-dimensional gel electrophoresis (2-DE) with 7 cm immobilized pH gradient strips for the determination of clinically relevant proteins in wheat grain. Using this approach, 157 2-DE spots were quantified in biological triplicate, out of which 55 were identified by matrix-assisted laser desorption/ionization – time of flight tandem mass spectrometry. Clinically relevant proteins associated with celiac disease, wheat dependent exercise induced anaphylaxis, baker’s asthma, and food allergy, were detected in 24 2-DE spots. However, alcohol-soluble gliadins were not detected with this approach. The comparison with a recent quantitative study suggested that gel-based and gel-free proteomics approaches are complementary for the detection and quantification of clinically relevant proteins in wheat grain.

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Molecular and immunological characterization of wheat Serpin (Tri a 33)

Abstract: This study confirms wheat serpin allergenicity and shows that recombinant serpin may be a marker of a broad spectrum of sensitization to wheat proteins.

Cited by 21 publications

References 31 publications

Amblyomma americanum tick saliva serine protease inhibitor 6 is a cross‐class inhibitor of serine proteases and papain‐like cysteine proteases that delays plasma clotting and inhibits platelet aggregation

Amblyomma americanum tick saliva serine protease inhibitor 6 is a cross‐class inhibitor of serine proteases and papain‐like cysteine proteases that delays plasma clotting and inhibits platelet aggregation

Common food allergens and their IgE-binding epitopes

Using 7 cm immobilized pH gradient strips to determine levels of clinically relevant proteins in wheat grain extracts

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