PMID- 15995984
OWN - NLM
STAT- MEDLINE
DCOM- 20051007
LR  - 20081121
IS  - 1613-4125 (Print)
IS  - 1613-4125 (Linking)
VI  - 49
IP  - 8
DP  - 2005 Aug
TI  - Proteolytic processing of the peanut allergen Ara h 3.
PG  - 744-55
AB  - The allergen Ara h 3 has been purified recently from peanuts. In contrast to 
      recombinant Ara h 3, a 60 kDa single-chain polypeptide, the allergen isolated 
      from its native source is extensively proteolytically processed. The 
      characteristic proteolytic processing for 11S plant storage proteins of the 
      glycinin family is observed for Ara h 3 yielding an acidic and a basic subunit, 
      bound by a disulfide bridge. In addition to this, proteolytic truncation is 
      observed for the acidic subunit but not for the basic subunit of Ara h 3. A 
      series of Ara h 3 polypeptides ranging from 13-45 kDa was separated by sodium 
      dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and each band was 
      digested by trypsin. Peptides related to the bands were identified and a scheme 
      positioning the different polypeptides in the Ara h 3 sequence has been 
      constructed. Peptide analysis showed sequence heterogeneity at two positions 
      indicating the presence of multiple genes encoding variant, but highly homologous 
      Ara h 3 proteins. The pool of Ara h 3 polypeptides from its native source 
      illustrated that allergen from the peanut is much more complex than the 
      recombinant protein used for epitope mapping experiments. From several Ara h 3 
      truncation products one or more immunoglobulin E (IgE) binding sites had been 
      removed. Characterization of the allergenicity of Ara h 3 should therefore also 
      include IgE-binding studies with peanut-derived Ara h 3, providing the high 
      degree of variation in the Ara h 3 protein structure, as this is what 
      peanut-allergic individuals are confronted with.
FAU - Piersma, Sander R
AU  - Piersma SR
AD  - FOM Institute for Atomic and Molecular Physics, Amsterdam, The Netherlands. 
      Piersma@amolf.nl
FAU - Gaspari, Marco
AU  - Gaspari M
FAU - Hefle, Susan L
AU  - Hefle SL
FAU - Koppelman, Stef J
AU  - Koppelman SJ
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Germany
TA  - Mol Nutr Food Res
JT  - Molecular nutrition & food research
JID - 101231818
RN  - 0 (Allergens)
RN  - 0 (Antigens, Plant)
RN  - 0 (Peptide Fragments)
RN  - 0 (Plant Proteins)
RN  - 0 (Protein Subunits)
RN  - 0 (Seed Storage Proteins)
RN  - 0 (allergen Ara h3)
RN  - EC 3.4.21.4 (Trypsin)
SB  - IM
MH  - Allergens/chemistry/*metabolism
MH  - Amino Acid Sequence
MH  - Antigens, Plant
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Molecular Sequence Data
MH  - Molecular Weight
MH  - Peptide Fragments/chemistry/metabolism
MH  - Plant Proteins
MH  - Protein Subunits/chemistry
MH  - Seed Storage Proteins
MH  - Sequence Alignment
MH  - Sequence Analysis, Protein
MH  - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
MH  - Trypsin/*metabolism
EDAT- 2005/07/05 09:00
MHDA- 2005/10/08 09:00
CRDT- 2005/07/05 09:00
PHST- 2005/07/05 09:00 [pubmed]
PHST- 2005/10/08 09:00 [medline]
PHST- 2005/07/05 09:00 [entrez]
AID - 10.1002/mnfr.200500020 [doi]
PST - ppublish
SO  - Mol Nutr Food Res. 2005 Aug;49(8):744-55. doi: 10.1002/mnfr.200500020.