References/Publications for Mass spectrometry (MS) of Ara h 2

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12759484 Int Arch Allergy Immunol. 2003 May;131(1):14-8.

Isolation and characterization of two complete Ara h 2 isoforms cDNA.

Chatel JM(1), Bernard H, Orson FM.

17474754 J Agric Food Chem. 2007 May 30;55(11):4461-73. Epub 2007 May 3.

Proteomics-based approach to detect and identify major allergens in processed
peanuts by capillary LC-Q-TOF (MS/MS).

Chassaigne H(1), Nĝrgaard JV, Hengel AJ.

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, Nĝrgaard JV, Maleki SJ, van Hengel AJ.

Two doublets on two different mass lines at ca. 16 and 18 kDa matched with
purified allergen Ara h 2. The basic and acidic sub-units of Ara h 3/4 were
observed at masses of ca. 25 kDa and 40-45 kDa, respectively. Subsequently the
antibody-binding capacity of spots corresponding to peanut allergens was
investigated by Western blotting of 2D gels using antibodies (IgY) raised against
Ara h 1, Ara h 2 and the recombinant 40 kDa sub-unit of Ara h 3/4. Final
confirmation of the identity of the protein spots matched after 2D
electrophoresis and identified by Western blotting was obtained by in-gel
digestion of protein spots and analysis by quadrupole time-of-flight mass
spectrometry. By using the method developed in our work, the location and
identification of two different isoforms of the allergen Ara h 1, the allergen
Ara h 2 and six isoforms of the allergen Ara h 3/4 in 2D peanut protein maps was

DOI: 10.1016/j.jprot.2009.02.002
PMID: 19223023 [Indexed for MEDLINE]
Protein Sci. 2010 Jan;19(1):174-82. doi: 10.1002/pro.295.

Primary sequence and site-selective hydroxylation of prolines in isoforms of a
major peanut allergen protein Ara h 2.

Li J(1), Shefcheck K, Callahan J, Fenselau C.

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

26920311 Food Chem. 2016 Jul 1;202:404-8. doi: 10.1016/j.foodchem.2016.02.004. Epub 2016
Feb 2.

Influence of heat treatment on the structure and core IgE-binding epitopes of
rAra h 2.02.

Cai Q(1), Zhang WJ(2), Zhu QQ(2), Chen Q(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).

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).

31525267 J Sci Food Agric. 2020 Jan 15;100(1):308-314. doi: 10.1002/jsfa.10040. Epub 2019
Nov 6.

Polyphenol-oxidase-catalyzed cross-linking of Ara h 2: reaction sites and effect
on structure and allergenicity.

Ren L(1)(2), Wu Z(1)(3), Zhang Y(1)(4), Li K(1)(5), Yuan J(1)(6), Li X(1), Yang
A(1)(3), Tong P(1), Chen H(1)(3).

31584695 Allergy. 2020 Mar;75(3):709-712. doi: 10.1111/all.14070. Epub 2019 Oct 28.

Mass spectrometry confirmation that clinically important peanut protein allergens
are present in household dust.

Brough HA(1)(2)(3), Mills ENC(4), Richards K(1)(2), Lack G(1)(2)(3), Johnson

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).

32125467 Anal Bioanal Chem. 2020 May;412(12):2815-2827. doi: 10.1007/s00216-020-02508-9.
Epub 2020 Mar 3.

A multiple reaction monitoring method for determining peanut (Arachis hypogea)
allergens in serum using quadrupole and time-of-flight mass spectrometry.

Hands CM(1), Sayers RL(1), Nitride C(1), Gethings LA(2), Mills ENC(3).

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).

34671372 Front Plant Sci. 2021 Oct 4;12:723363. doi: 10.3389/fpls.2021.723363. eCollection

The Major Peanut Allergen Ara h 2 Produced in Nicotiana benthamiana Contains
Hydroxyprolines and Is a Viable Alternative to the E. Coli Product in Allergy

Üzülmez Ö(1), Kalic T(1)(2), Mayr V(1), Lengger N(1), Tscheppe A(1), Radauer
C(1), Hafner C(2)(3), Hemmer W(4), Breiteneder H(1).

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).