References/Publications for Western/Immunoblot of Ara h 2

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1460200 J Allergy Clin Immunol. 1992 Dec;90(6 Pt 1):962-9.

Identification and characterization of a second major peanut allergen, Ara h II,
with use of the sera of patients with atopic dermatitis and positive peanut
challenge.

Burks AW(1), Williams LW, Connaughton C, Cockrell G, O'Brien TJ, Helm RM.


9186485 Arch Biochem Biophys. 1997 Jun 15;342(2):244-53.

Identification and mutational analysis of the immunodominant IgE binding epitopes
of the major peanut allergen Ara h 2.

Stanley JS(1), King N, Burks AW, Huang SK, Sampson H, Cockrell G, Helm RM, West
CM, Bannon GA.


10474031 Int Arch Allergy Immunol. 1999 Aug;119(4):265-74.

Selective cloning of peanut allergens, including profilin and 2S albumins, by
phage display technology.

Kleber-Janke T(1), Crameri R, Appenzeller U, Schlaak M, Becker WM.


11398088 J Allergy Clin Immunol. 2001 Jun;107(6):1077-81.

Effects of cooking methods on peanut allergenicity.

Beyer K(1), Morrow E, Li XM, Bardina L, Bannon GA, Burks AW, Sampson HA.


12097392 J Immunol. 2002 Jul 15;169(2):882-7.

Protein structure plays a critical role in peanut allergen stability and may
determine immunodominant IgE-binding epitopes.

Sen M(1), Kopper R, Pons L, Abraham EC, Burks AW, Bannon GA.


15080811 Clin Exp Allergy. 2004 Apr;34(4):583-90.

Relevance of Ara h1, Ara h2 and Ara h3 in peanut-allergic patients, as determined
by immunoglobulin E Western blotting, basophil-histamine release and
intracutaneous testing: Ara h2 is the most important peanut allergen.

Koppelman SJ(1), Wensing M, Ertmann M, Knulst AC, Knol EF.


15237964 J Agric Food Chem. 2004 Jul 14;52(14):4541-5.

Allergenic properties of roasted peanut allergens may be reduced by peroxidase.

Chung SY(1), Maleki SJ, Champagne ET.


15836759 Clin Exp Allergy. 2005 Apr;35(4):490-7.

Purification and immunoglobulin E-binding properties of peanut allergen Ara h 6:
evidence for cross-reactivity with Ara h 2.

Koppelman SJ(1), de Jong GA, Laaper-Ertmann M, Peeters KA, Knulst AC, Hefle SL,
Knol EF.


15893698 Clin Immunol. 2005 Jun;115(3):302-12.

Comparative potency of Ara h 1 and Ara h 2 in immunochemical and functional
assays of allergenicity.

Palmer GW(1), Dibbern DA Jr, Burks AW, Bannon GA, Bock SA, Porterfield HS,
McDermott RA, Dreskin SC.


16189800 Mol Nutr Food Res. 2005 Oct;49(10):963-71.

Allergenic characteristics of a modified peanut allergen.

King N(1), Helm R, Stanley JS, Vieths S, Lüttkopf D, Hatahet L, Sampson H, Pons
L, Burks W, Bannon GA.


16580071 Mol Immunol. 2007 Jan;44(4):463-71. Epub 2006 Mar 31.

IgE cross-reactivity between the major peanut allergen Ara h 2 and tree nut
allergens.

de Leon MP(1), Drew AC, Glaspole IN, Suphioglu C, O'Hehir RE, Rolland JM.


17210048 Clin Exp Allergy. 2007 Jan;37(1):108-15.

Does skin prick test reactivity to purified allergens correlate with clinical
severity of peanut allergy?

Peeters KA(1), Koppelman SJ, van Hoffen E, van der Tas CW, den Hartog Jager CF,
Penninks AH, Hefle SL, Bruijnzeel-Koomen CA, Knol EF, Knulst AC.


17651153 Clin Exp Allergy. 2007 Aug;37(8):1221-8.

Children with peanut allergy recognize predominantly Ara h2 and Ara h6, which
remains stable over time.

Flinterman AE(1), van Hoffen E, den Hartog Jager CF, Koppelman S, Pasmans SG,
Hoekstra MO, Bruijnzeel-Koomen CA, Knulst AC, Knol EF.


18680451 Protein Pept Lett. 2008;15(6):567-77.

Proteomic analysis of peanut seed storage proteins and genetic variation in a
potential peanut allergen.

Guo B(1), Liang X, Chung SY, Holbrook CC, Maleki SJ.


19007236 J Agric Food Chem. 2008 Dec 10;56(23):11225-33. doi: 10.1021/jf802600r.

Reduction of IgE binding and nonpromotion of Aspergillus flavus fungal growth by
simultaneously silencing Ara h 2 and Ara h 6 in peanut.

Chu Y(1), Faustinelli P, Ramos ML, Hajduch M, Stevenson S, Thelen JJ, Maleki SJ,
Cheng H, Ozias-Akins P.


19223023 J Proteomics. 2009 Apr 13;72(3):511-26. doi: 10.1016/j.jprot.2009.02.002. Epub
2009 Feb 15.

Resolution and identification of major peanut allergens using a combination of
fluorescence two-dimensional differential gel electrophoresis, Western blotting
and Q-TOF mass spectrometry.

Chassaigne H(1), Trégoat V, Nřrgaard JV, Maleki SJ, van Hengel AJ.


19609960
Proteomics. 2009 Jul;9(13):3507-21. doi: 10.1002/pmic.200800938.

2-D DIGE analysis of the proteome of extracts from peanut variants reveals
striking differences in major allergen contents.

Schmidt H(1), Gelhaus C, Latendorf T, Nebendahl M, Petersen A, Krause S, Leippe
M, Becker WM, Janssen O.


19639724 J Investig Allergol Clin Immunol. 2009;19(4):283-91.

Immunoglobulin E cross-reactivity between lupine conglutins and peanut allergens
in serum of lupine-allergic individuals.

Dooper MM(1), Plassen C, Holden L, Lindvik H, Faeste CK.


21130383 Ann Allergy Asthma Immunol. 2010 Dec;105(6):451-7. doi:
1016/j.anai.2010.09.025.

Differences among heat-treated, raw, and commercial peanut extracts by skin
testing and immunoblotting.

Maleki SJ(1), Casillas AM, Kaza U, Wilson BA, Nesbit JB, Reimoneqnue C, Cheng H,
Bahna SL.


21883278 Allergy. 2011 Dec;66(12):1522-9. doi: 10.1111/j.1398-9995.2011.02692.x. Epub 2011
Aug 23.

Computationally predicted IgE epitopes of walnut allergens contribute to
cross-reactivity with peanuts.

Maleki SJ(1), Teuber SS, Cheng H, Chen D, Comstock SS, Ruan S, Schein CH.


21912172 Int Arch Allergy Immunol. 2012;157(1):41-50. doi: 10.1159/000324681. Epub 2011
Sep 6.

Influence of enzymatic hydrolysis on the allergenicity of roasted peanut protein
extract.

Cabanillas B(1), Pedrosa MM, Rodríguez J, Muzquiz M, Maleki SJ, Cuadrado C,
Burbano C, Crespo JF.


23181796 Clin Exp Allergy. 2012 Dec;42(12):1801-12. doi: 10.1111/cea.12031.

An unfolded variant of the major peanut allergen Ara h 2 with decreased
anaphylactic potential.

Starkl P(1), Felix F, Krishnamurthy D, Stremnitzer C, Roth-Walter F, Prickett SR,
Voskamp AL, Willensdorfer A, Szalai K, Weichselbaumer M, O'Hehir RE,
Jensen-Jarolim E.


23921317 Int Arch Allergy Immunol. 2013;162(2):123-30. doi: 10.1159/000351920. Epub 2013
Jul 31.

Allergenic properties of enzymatically hydrolyzed peanut flour extracts.

Shi X(1), Guo R, White BL, Yancey A, Sanders TH, Davis JP, Burks AW, Kulis M.


24266677 Allergy. 2013 Dec;68(12):1546-54. doi: 10.1111/all.12261. Epub 2013 Nov 23.

Identification of Maillard reaction products on peanut allergens that influence
binding to the receptor for advanced glycation end products.

Mueller GA(1), Maleki SJ, Johnson K, Hurlburt BK, Cheng H, Ruan S, Nesbit JB,
Pomés A, Edwards LL, Schorzman A, Deterding LJ, Park H, Tomer KB, London RE,
Williams JG.


23889250 Clin Exp Allergy. 2013 Aug;43(8):967-74. doi: 10.1111/cea.12136.

IgE binding to peanut components by four different techniques: Ara h 2 is the
most relevant in peanut allergic children and adults.

Klemans RJ(1), Liu X, Knulst AC, Knol MJ, Gmelig-Meyling F, Borst E, Pasmans SG,
Knol EF.


25483599 J Allergy Clin Immunol. 2015 May;135(5):1267-74.e1-8. doi:
1016/j.jaci.2014.10.025. Epub 2014 Dec 4.

Allergenicity of peanut component Ara h 2: Contribution of conformational versus
linear hydroxyproline-containing epitopes.

Bernard H(1), Guillon B(1), Drumare MF(1), Paty E(2), Dreskin SC(3), Wal JM(1),
Adel-Patient K(1), Hazebrouck S(4).


26411458 Appl Microbiol Biotechnol. 2016 Jan;100(2):661-71. doi:
1007/s00253-015-6953-y. Epub 2015 Sep 28.

Expression of a codon-optimised recombinant Ara h 2.02 peanut allergen in
Escherichia coli.

Lew MH(1), Lim RL(2).


26842773 Pediatr Allergy Immunol. 2016 Jun;27(4):348-55. doi: 10.1111/pai.12533.

Prospective investigation on the transfer of Ara h 2, the most potent peanut
allergen, in human breast milk.

Schocker F(1), Baumert J(2), Kull S(1), Petersen A(1), Becker WM(1), Jappe
U(1)(3).


27377129 Sci Rep. 2016 Jul 5;6:29249. doi: 10.1038/srep29249.

Conformational stability of digestion-resistant peptides of peanut conglutins
reveals the molecular basis of their allergenicity.

Apostolovic D(1), Stanic-Vucinic D(1), de Jongh HH(2), de Jong GA(3), Mihailovic
J(1), Radosavljevic J(1), Radibratovic M(4), Nordlee JA(5), Baumert JL(5), Milcic
M(1), Taylor SL(5), Garrido Clua N(2), Cirkovic Velickovic T(1), Koppelman SJ(5).


27979211 Food Chem. 2017 Apr 15;221:335-344. doi: 10.1016/j.foodchem.2016.10.063. Epub
2016 Oct 14.

Peanut protein extraction conditions strongly influence yield of allergens Ara h
1 and 2 and sensitivity of immunoassays.

Walczyk NE(1), Smith PMC(2), Tovey ER(3), Roberts TH(4).


28441989 Allergy Asthma Proc. 2017 May 1;38(3):192-196. doi: 10.2500/aap.2017.38.4049.

Ara h2 levels in dust from homes of individuals with peanut allergy and
individuals with peanut tolerance.

Shroba J, Barnes C, Nanda M, Dinakar C, Ciaccio C.

28634114
Food Chem Toxicol. 2017 Sep;107(Pt A):88-98. doi: 10.1016/j.fct.2017.06.029. Epub
2017 Jun 17.

Peanut digestome: Identification of digestion resistant IgE binding peptides.

Di Stasio L(1), Picariello G(2), Mongiello M(2), Nocerino R(3), Berni Canani
R(3), Bavaro S(4), Monaci L(4), Ferranti P(5), Mamone G(6).


28638052 Sci Rep. 2017 Jun 21;7(1):3981. doi: 10.1038/s41598-017-04268-6.

Determination of Crucial Immunogenic Epitopes in Major Peanut Allergy Protein,
Ara h2, via Novel Nanoallergen Platform.

Deak PE(1), Vrabel MR(1), Kiziltepe T(1)(2), Bilgicer B(3)(4)(5).


29188033 Food Sci Nutr. 2017 Jul 25;5(6):1065-1071. doi: 10.1002/fsn3.491. eCollection
2017 Nov.

Simple methods to reduce major allergens Ara h 1 and Ana o 1/2 in peanut and
cashew extracts.

Chung SY(1), Mattison CP(1), Grimm CC(1), Reed S(1).


29542223
Clin Exp Allergy. 2018 Jul;48(7):890-897. doi: 10.1111/cea.13134. Epub 2018 Apr


2S protein Ara h 7.0201 has unique epitopes compared to other Ara h 7 isoforms
and is comparable to 2S proteins Ara h 2 and 6 in basophil degranulation
capacity.

Hayen SM(1)(2), Ehlers AM(1)(2), den Hartog Jager CF(1), Garssen J(3)(4), Knol
EF(1)(2), Knulst AC(1)(2), Suer W(5), Willemsen LEM(3), Otten HG(2).


30744860 Food Chem. 2019 Jun 30;284:287-295. doi: 10.1016/j.foodchem.2019.01.081. Epub
2019 Jan 18.

Binding of peanut allergen Ara h 2 with Vaccinium fruit polyphenols.

Plundrich NJ(1), Cook BT(2), Maleki SJ(3), Fourches D(2), Lila MA(4).


31758869 J Appl Microbiol. 2020 Mar;128(3):862-874. doi: 10.1111/jam.14524. Epub 2019 Dec


Lactococcus lactis harbouring Ara h 2.02 alleviates allergen-specific
Th2-associated responses in sensitized mice.

Chan CJ(1), Yong YS(1), Song AAL(2), Abdul Rahim R(3), In LLA(1), Lim RLH(1).


33046788 Sci Rep. 2020 Oct 12;10(1):17038. doi: 10.1038/s41598-020-72636-w.

Impact of cold plasma processing on major peanut allergens.

Venkataratnam H(1), Cahill O(2), Sarangapani C(2), Cullen PJ(2)(3)(4), Barry-Ryan
C(2).


33217527 Food Chem Toxicol. 2021 Jan;147:111866. doi: 10.1016/j.fct.2020.111866. Epub 2020
Nov 17.

Purification of soybean cupins and comparison of IgE binding with peanut
allergens in a population of allergic subjects.

Ramadan S(1), Marsh J(2), El-Sherbeny GA(1), El-Halawany EF(1), Luan F(3),
Baumert JL(2), Johnson P(2), Osman Y(1), Goodman RE(4).


33854954 Toxicol Rep. 2021 Mar 31;8:767-773. doi: 10.1016/j.toxrep.2021.03.027.
eCollection 2021.

Ranking of 10 legumes according to the prevalence of sensitization as a parameter
to characterize allergenic proteins.

Smits M(1)(2)(3), Verhoeckx K(1)(2), Knulst A(1)(2), Welsing P(1)(4), de Jong
A(5)(6), Houben G(1)(2)(3), Le TM(1)(2).


34118511 Food Chem. 2021 Nov 15;362:129879. doi: 10.1016/j.foodchem.2021.129879. Epub 2021
Apr 20.

The impact of a baked muffin matrix on the bioaccessibility and IgE reactivity of
egg and peanut allergens.

Mattar H(1), Padfield P(1), Simpson A(2), Mills ENC(3).


35000380 J Agric Food Chem. 2022 Jan 19;70(2):626-633. doi: 10.1021/acs.jafc.1c06828. Epub
2022 Jan 8.

Effect of Processing on the Structure and Allergenicity of Peanut Allergen Ara h
2 Roasted in a Matrix.

Chang X(1)(2), Zhou X(1)(2), Tang Y(1)(2), Zhang Y(1)(2), Yuan J(1)(3), Li
X(1)(2), Yang A(1)(4), Tong P(1)(2), Wu Z(1)(4), Chen H(1)(4).