Exploring Functions for Glycosylation in Host Defence
337
Acknowledgements
The co-ordinates for the CCP domain of Factor H, on which the molecular model
of DAF (Fig. 23.7) was based, were kindly sent to us by Professor E. Medof and
Professor M. Shoham. DAF was a gift from Prof. Paul Morgan and Dr. Claire Harris. The full glycan analysis of DAF will be published elsewhere.
The authors would like to thank Professor Ghislain Opdenakker and Dr.
Anthony Merry for their very helpful criticisms of the manuscript.
The GBI acknowledges support from the BBSRC and from the European Commission Grant BI04-CT95-0138.
Abbreviations
C: constant; CCP: complement control protein; CRD: carbohydrate recognition
domain; ER: endoplasmic reticulum; GPI: glycosylphosphatidylinositol; MBL:
mannose binding lectin also known as mannose binding protein; RA: Rheumatoid arthritis; TCR: T-cell receptor; V: variable chain, H: heavy chain, L: light
chain.
Abbreviations used for describing oligosaccharide structures: A: indicates the
number of antennae (from 1-4); G(O- 2) indicates the number of terminal galactose residues in the structure; F: fucose; B: bisecting N-acetyl glucosamine;
GlcNAc: N -acetyl glucosamine; S: sialic acid; MAC: membrane attack complex;
RF: Rheumatoid factor; DAF: decay accelerating factor; GPI: glycosylphosphatidyl inositol.
References
Barber LD, Patel TP, Percival L, Gumperz JE, Lanier LL, Phillips JH, Bigge JC, Wormald, MR, Parekh
RB, Parham, P. (1996) Unusual uniformity of the N-linked oligosaccharides of HLA-A, -B, and -C
glycoproteins. J Immunol 156: 3275-84
Bodian DL, Davis SJ, Rushmere NK, Morgan BP (1997) Mutational analysis of the active site and antibody epitopes of the complement-inhibitory glycoprotein, CD59. J Exp Med 185: 507-516.
Bole DG, Hendershot LM, Kearney JF (1986) Post-translational association of immunoglobulin heavy
chain binding protein with nascent heavy chains in nonsecreting and secreting hybridomas. J Cell
BioI 102: 1558-1566
Burton DR, Woof JM (1992) Human antibody effector function. Adv Immunol 51: 1-84
Coyne KE, Hall SE, Scott Thompson E, Arce MA, Kinoshita T, Fujita T, Anstee DJ, Rosse W, Lublin DM
(1992) Mapping of epitopes, glycosylation sites, and complement regulatory domains in human
decay accelerating factor. J Immunol 149: 2906 - 2913
Davies A, Simmons DL, Hale G, Harrison RA, Tighe H, Lachmann pJ, Waldman H. (1989) CD59, an
LY -6-like protein expressed in human lymphoid cells, regulates the action of the complement
membrane attack complex on homologous cells. J Exp Med 170: 637-654
The analyses referred to in this article were carried out in the Glycobiology Institute using an HPLC
system consisting of a Douglas Scientific DG604 degasser, two Waters 510 pumps, a Waters 717 autoinjector, a Waters Temperature Control Module and a Jasco FP-920 fluorescence detector. The system
was controlled via a Waters LAC/E box using Waters Expertease 3.1 software running on a DEC VAX
4000-200 computer. The Normal phase, and Weak Anion Exchange HPLC columns CGlycoSep Nand
GlycoSepC respectively) were obtained from Oxford GlycoSciences COGS) UK Ltd). Fluorescent labelling with 2-aminobenzamide was carried out using a Signal Labelling Kit, glycans were released by
hydrazine using the GlycoPrep 1000 or by PNGase F. Glycosidases were also obtained from OGS.
Curve fitting software was Peak Time, developed by Dr. E. Hait, Glycobiology Institute, Oxford.
337
Acknowledgements
The co-ordinates for the CCP domain of Factor H, on which the molecular model
of DAF (Fig. 23.7) was based, were kindly sent to us by Professor E. Medof and
Professor M. Shoham. DAF was a gift from Prof. Paul Morgan and Dr. Claire Harris. The full glycan analysis of DAF will be published elsewhere.
The authors would like to thank Professor Ghislain Opdenakker and Dr.
Anthony Merry for their very helpful criticisms of the manuscript.
The GBI acknowledges support from the BBSRC and from the European Commission Grant BI04-CT95-0138.
Abbreviations
C: constant; CCP: complement control protein; CRD: carbohydrate recognition
domain; ER: endoplasmic reticulum; GPI: glycosylphosphatidylinositol; MBL:
mannose binding lectin also known as mannose binding protein; RA: Rheumatoid arthritis; TCR: T-cell receptor; V: variable chain, H: heavy chain, L: light
chain.
Abbreviations used for describing oligosaccharide structures: A: indicates the
number of antennae (from 1-4); G(O- 2) indicates the number of terminal galactose residues in the structure; F: fucose; B: bisecting N-acetyl glucosamine;
GlcNAc: N -acetyl glucosamine; S: sialic acid; MAC: membrane attack complex;
RF: Rheumatoid factor; DAF: decay accelerating factor; GPI: glycosylphosphatidyl inositol.
References
Barber LD, Patel TP, Percival L, Gumperz JE, Lanier LL, Phillips JH, Bigge JC, Wormald, MR, Parekh
RB, Parham, P. (1996) Unusual uniformity of the N-linked oligosaccharides of HLA-A, -B, and -C
glycoproteins. J Immunol 156: 3275-84
Bodian DL, Davis SJ, Rushmere NK, Morgan BP (1997) Mutational analysis of the active site and antibody epitopes of the complement-inhibitory glycoprotein, CD59. J Exp Med 185: 507-516.
Bole DG, Hendershot LM, Kearney JF (1986) Post-translational association of immunoglobulin heavy
chain binding protein with nascent heavy chains in nonsecreting and secreting hybridomas. J Cell
BioI 102: 1558-1566
Burton DR, Woof JM (1992) Human antibody effector function. Adv Immunol 51: 1-84
Coyne KE, Hall SE, Scott Thompson E, Arce MA, Kinoshita T, Fujita T, Anstee DJ, Rosse W, Lublin DM
(1992) Mapping of epitopes, glycosylation sites, and complement regulatory domains in human
decay accelerating factor. J Immunol 149: 2906 - 2913
Davies A, Simmons DL, Hale G, Harrison RA, Tighe H, Lachmann pJ, Waldman H. (1989) CD59, an
LY -6-like protein expressed in human lymphoid cells, regulates the action of the complement
membrane attack complex on homologous cells. J Exp Med 170: 637-654
The analyses referred to in this article were carried out in the Glycobiology Institute using an HPLC
system consisting of a Douglas Scientific DG604 degasser, two Waters 510 pumps, a Waters 717 autoinjector, a Waters Temperature Control Module and a Jasco FP-920 fluorescence detector. The system
was controlled via a Waters LAC/E box using Waters Expertease 3.1 software running on a DEC VAX
4000-200 computer. The Normal phase, and Weak Anion Exchange HPLC columns CGlycoSep Nand
GlycoSepC respectively) were obtained from Oxford GlycoSciences COGS) UK Ltd). Fluorescent labelling with 2-aminobenzamide was carried out using a Signal Labelling Kit, glycans were released by
hydrazine using the GlycoPrep 1000 or by PNGase F. Glycosidases were also obtained from OGS.
Curve fitting software was Peak Time, developed by Dr. E. Hait, Glycobiology Institute, Oxford.