PMID- 24084098
OWN - NLM
STAT- MEDLINE
DCOM- 20140211
LR  - 20181202
IS  - 1872-9142 (Electronic)
IS  - 0161-5890 (Linking)
VI  - 57
IP  - 2
DP  - 2014 Feb
TI  - Identification of amino acid residues involved in the interaction of canine IgE 
      with canine and human FcepsilonRIalpha.
PG  - 111-8
LID - S0161-5890(13)00495-1 [pii]
LID - 10.1016/j.molimm.2013.08.013 [doi]
AB  - The interaction of immunoglobulin E (IgE) antibodies with the high-affinity 
      receptor (FcepsilonRI) is important in anti-parasitic immunity and plays a central role 
      in allergic responses. It has been shown that the human Cepsilon3 domains comprise the 
      binding sites for FcepsilonRIalpha and crystal structure determination has shown that amino 
      acids in four sites contribute to the high affinity of the interaction. The role 
      of homologous residues within canine IgE-Fc, i.e. amino acids located at Cepsilon2-Cepsilon3 
      interface (residues 332-337), loop BC (residues 362-365), loop DE (residues 
      393-396), and loop FG (residues 424-427) in canine Cepsilon3 domain were targeted by 
      site-specific mutagenesis. The functional consequences of the mutations to 
      support (i) IgE-mediated, antigen-induced release of beta-hexosaminidase from RBL 
      cells transfected with canine or human FcepsilonRIalpha and (ii) the affinity of the 
      mutants for the soluble extracellular domain of the alpha-chain expressed in Pichia 
      pastoris were determined by Surface Plasmon Resonance (SPR). Kinetic analysis 
      supports the observed effects of IgE mutations on stimulus secretion coupling. 
      Potential applications of this study, leading to the generation of an IgE variant 
      with a disabled FcepsilonRIalpha binding site, are discussed.
CI  - Copyright (c) 2013 Elsevier Ltd. All rights reserved.
FAU - Ye, Hongtu
AU  - Ye H
AD  - Krebs Institute for Biomolecular Research, Department of Molecular Biology and 
      Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield S10 
      2TN, United Kingdom. Electronic address: mbp06hy@yahoo.co.uk.
FAU - Housden, Jonathan E M
AU  - Housden JE
FAU - Hunter, Michael
AU  - Hunter M
FAU - Sabban, Sari
AU  - Sabban S
FAU - Helm, Birgit A
AU  - Helm BA
LA  - eng
PT  - Journal Article
DEP - 20130928
PL  - England
TA  - Mol Immunol
JT  - Molecular immunology
JID - 7905289
RN  - 0 (Amino Acids)
RN  - 0 (FcepsilonRI alpha-chain, human)
RN  - 0 (Receptors, IgE)
RN  - 37341-29-0 (Immunoglobulin E)
RN  - EC 3.2.1.52 (beta-N-Acetylhexosaminidases)
SB  - IM
MH  - Amino Acids/genetics
MH  - Animals
MH  - Binding Sites
MH  - Cell Line
MH  - Dogs
MH  - Genetic Variation/immunology
MH  - Humans
MH  - Immunoglobulin E/chemistry/*genetics/*immunology
MH  - Mutagenesis, Site-Directed
MH  - Pichia/genetics
MH  - Protein Structure, Tertiary
MH  - Rats
MH  - Receptors, IgE/chemistry/*genetics/*immunology
MH  - Sequence Analysis, Protein
MH  - *Sequence Homology, Amino Acid
MH  - Surface Plasmon Resonance
MH  - Transfection
MH  - beta-N-Acetylhexosaminidases/metabolism
OTO - NOTNLM
OT  - Canine (ca)
OT  - Canine IgE variants
OT  - FcvarepsilonRIalpha
OT  - Human (hu)
OT  - Human/canine high-affinity receptor alpha chain
OT  - IgE/FcvarepsilonRIalpha
OT  - Kinetic constants
OT  - Soluble (s)
EDAT- 2013/10/03 06:00
MHDA- 2014/02/12 06:00
CRDT- 2013/10/03 06:00
PHST- 2013/08/13 00:00 [received]
PHST- 2013/08/22 00:00 [accepted]
PHST- 2013/10/03 06:00 [entrez]
PHST- 2013/10/03 06:00 [pubmed]
PHST- 2014/02/12 06:00 [medline]
AID - S0161-5890(13)00495-1 [pii]
AID - 10.1016/j.molimm.2013.08.013 [doi]
PST - ppublish
SO  - Mol Immunol. 2014 Feb;57(2):111-8. doi: 10.1016/j.molimm.2013.08.013. Epub 2013 
      Sep 28.