PMID- 33439436
OWN - NLM
STAT- MEDLINE
DCOM- 20220128
LR  - 20220128
IS  - 1573-4986 (Electronic)
IS  - 0282-0080 (Linking)
VI  - 38
IP  - 1
DP  - 2021 Feb
TI  - Purification and molecular characterization of a truncated-type Ara h 1, a major 
      peanut allergen: oligomer structure, antigenicity, and glycoform.
PG  - 67-76
LID - 10.1007/s10719-020-09969-1 [doi]
AB  - Peanut allergies are among the most severe food allergies, and several allergenic 
      proteins referred to as Ara h 1-Ara h 17 have been identified from peanut seeds. 
      The molecular characterization of Ara h 1 (63 kDa), a glycosylated allergen, has 
      almost been completed, and the occurrence of two homologous genes (clone 41B and 
      clone P17) has been identified. In this study, we found a new variant of Ara h 1 
      i.e. 54 kDa, in which the N-terminal amino acid sequence was EGREGEQ-, indicating 
      that the N-terminal domain of 63 kDa Ara h 1 had been removed. This new isoform 
      was obtained from the run-through fraction of hydrophobic interaction 
      chromatography while 63 kDa Ara h 1 was tightly bound to the hydrophobic resins, 
      suggesting that the removal of the N-terminal domain resulted in extreme 
      hydrophilic properties. We found that 63 kDa Ara h 1 occurs as higher order 
      homo-oligomeric conformations such as decamer or nonamer, while 54 kDa Ara h 1 
      occurs exclusively as a homotrimer, indicating that the N-terminal domain of the 
      63 kDa molecule may be involved in higher order oligomerization. When antisera 
      from peanut-allergic patients were treated with both the Ara h 1 molecules, the 
      immunoglobulin E (IgE) antibodies in these sera reacted with each Ara h 1 
      molecule, suggesting that the C-terminal as well as the N-terminal domains of Ara 
      h 1 contribute significantly to the epitope formations of this peanut 
      glycoallergen. Furthermore, the glycoform analyses of N-glycans linked to 63 kDa 
      and 54 kDa Ara h 1 subunits revealed that both typical high-mannose type and 
      beta-xylosylated type N-glycans are linked to the molecules. The cross-reactivity of 
      IgE against Ara h 1 in the serum of one peanut allergy patient was completely 
      lost by de-N-glycosylation, indicating the N-glycan of Ara h 1 was the sole 
      epitope for the Ara h 1- specific IgE in the patient.
FAU - Md, Asaduzzaman
AU  - Md A
AD  - Department of Biofunctional Chemistry, Graduate School of Environmental and Life 
      Science, Okayama University, 1-1-1 Tsushima-Naka, Okayama, 700-8530, Japan.
FAU - Maeda, Megumi
AU  - Maeda M
AD  - Department of Biofunctional Chemistry, Graduate School of Environmental and Life 
      Science, Okayama University, 1-1-1 Tsushima-Naka, Okayama, 700-8530, Japan.
FAU - Matsui, Teruaki
AU  - Matsui T
AD  - Department of Allergy, Aichi Children's Health and Medical Center, 7-426, Obu, 
      Morioka, Aichi, 474-8710, Japan.
FAU - Takasato, Yoshihiro
AU  - Takasato Y
AD  - Department of Allergy, Aichi Children's Health and Medical Center, 7-426, Obu, 
      Morioka, Aichi, 474-8710, Japan.
FAU - Ito, Komei
AU  - Ito K
AD  - Department of Allergy, Aichi Children's Health and Medical Center, 7-426, Obu, 
      Morioka, Aichi, 474-8710, Japan.
FAU - Kimura, Yoshinobu
AU  - Kimura Y
AUID- ORCID: 0000-0003-0329-1168
AD  - Department of Biofunctional Chemistry, Graduate School of Environmental and Life 
      Science, Okayama University, 1-1-1 Tsushima-Naka, Okayama, 700-8530, Japan. 
      yosh8mar@okayama-u.ac.jp.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20210113
PL  - United States
TA  - Glycoconj J
JT  - Glycoconjugate journal
JID - 8603310
RN  - 0 (Antigens, Plant)
RN  - 0 (Ara h 1 protein, Arachis hypogaea)
RN  - 0 (Epitopes)
RN  - 0 (Membrane Proteins)
RN  - 0 (Plant Proteins)
RN  - 0 (Polysaccharides)
RN  - 0 (Protein Subunits)
RN  - 37341-29-0 (Immunoglobulin E)
SB  - IM
MH  - Antigens, Plant/*chemistry/*immunology/isolation & purification/metabolism
MH  - Arachis/chemistry
MH  - Cross Reactions
MH  - Epitopes/immunology/metabolism
MH  - Golgi Apparatus/metabolism
MH  - Immunoblotting
MH  - Immunoglobulin E/immunology
MH  - Membrane Proteins/*chemistry/*immunology/isolation & purification/metabolism
MH  - Molecular Weight
MH  - Peanut Hypersensitivity/blood/*immunology
MH  - Plant Proteins/*chemistry/*immunology/isolation & purification/metabolism
MH  - Polysaccharides/chemistry/metabolism
MH  - Protein Subunits
OTO - NOTNLM
OT  - Ara h 1
OT  - Glycoallergen
OT  - Immunogenic N-glycan
OT  - Peanut allergy
EDAT- 2021/01/14 06:00
MHDA- 2022/01/29 06:00
CRDT- 2021/01/13 12:13
PHST- 2020/07/26 00:00 [received]
PHST- 2020/12/23 00:00 [accepted]
PHST- 2020/12/11 00:00 [revised]
PHST- 2021/01/14 06:00 [pubmed]
PHST- 2022/01/29 06:00 [medline]
PHST- 2021/01/13 12:13 [entrez]
AID - 10.1007/s10719-020-09969-1 [pii]
AID - 10.1007/s10719-020-09969-1 [doi]
PST - ppublish
SO  - Glycoconj J. 2021 Feb;38(1):67-76. doi: 10.1007/s10719-020-09969-1. Epub 2021 Jan 
      13.