PMID- 20506277
OWN - NLM
STAT- MEDLINE
DCOM- 20101126
LR  - 20100723
IS  - 1097-0290 (Electronic)
IS  - 0006-3592 (Linking)
VI  - 107
IP  - 1
DP  - 2010 Sep 1
TI  - Efficient expression and purification of human aglycosylated Fcgamma receptors in 
      Escherichia coli.
PG  - 21-30
LID - 10.1002/bit.22785 [doi]
AB  - Effector Fc gamma receptors (FcgammaRs) are expressed on the surface of a variety 
      of cells of hematopoietic lineage and serve as a bridge between adaptive and 
      innate immune responses. The interaction between immune complexes, formed by IgG 
      class antibodies that are crosslinked with antigen, and FcgammaRs triggers 
      signaling cascades that result in numerous cellular responses including the 
      activation or donwregulation of cytotoxic responses, cytokine release, and 
      antibody synthesis. Here, the extracellular domains of the human type I 
      transmembrane FcgammaRs were expressed in Escherichia coli and their interactions 
      to subclass IgGs (IgG1, IgG2, IgG3, and IgG4) antibodies were analyzed. 
      Expression using fully synthetic E. coli codon optimized FcgammaR genes and 
      optimization of sequences for N-terminal translation initiation region through 
      mRNA secondary structure prediction enabled us to achieve high yield of purified, 
      bacterially expressed receptors, including FcgammaRI and FcgammaRIIIa which have 
      not been successfully expressed in bacteria until now. The aglycosylated 
      FcgammaRs showed similar IgG subclass binding selectivity compared to the 
      respective glycosylated FcgammaRs expressed in mammalian cells.
CI  - 2010 Wiley Periodicals, Inc.
FAU - Jung, Sang Taek
AU  - Jung ST
AD  - Department of Chemical Engineering, University of Texas, Austin, 78712, USA.
FAU - Kang, Tae Hyun
AU  - Kang TH
FAU - Georgiou, George
AU  - Georgiou G
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biotechnol Bioeng
JT  - Biotechnology and bioengineering
JID - 7502021
RN  - 0 (Receptors, IgG)
RN  - 0 (Recombinant Proteins)
SB  - IM
MH  - Escherichia coli/*physiology
MH  - Genetic Enhancement/*methods
MH  - Glycosylation
MH  - Humans
MH  - Protein Engineering/*methods
MH  - Receptors, IgG/chemistry/*isolation & purification/*physiology
MH  - Recombinant Proteins/isolation & purification/metabolism
EDAT- 2010/05/28 06:00
MHDA- 2010/12/14 06:00
CRDT- 2010/05/28 06:00
PHST- 2010/05/28 06:00 [entrez]
PHST- 2010/05/28 06:00 [pubmed]
PHST- 2010/12/14 06:00 [medline]
AID - 10.1002/bit.22785 [doi]
PST - ppublish
SO  - Biotechnol Bioeng. 2010 Sep 1;107(1):21-30. doi: 10.1002/bit.22785.