Glycosylation and functional activity of anti-D secreted by two human lymphoblastoid cell lines

Diane Cant; John Barford; Colin Harbour; Anne Fletcher; Nicole Packer; Andrew Gooley

doi:10.1007/BF00762397

Glycosylation and functional activity of anti-D secreted by two human lymphoblastoid cell lines

Diane Cant^*, John Barford, Colin Harbour, Anne Fletcher, Nicole Packer, Andrew Gooley

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

Abstract

Cell lines BTSN4 and BTSN5 were produced by the Epstein-Barr Virus (EBV) transformation of B-lymphocytes from the same human donor. Both secrete an anti-D monoclonal of the IgG1 subclass but these antibodies display vastly different effector activities. Specifically, anti-D from BTSN4 has a far greater activity in both monocyte-and lymphocyte-mediated ADCC reactions and causes a higher percentage of rosettes to be formed with monocyte-like U937 cells. This variation in functional activity is shown to coincide with changes in the structure of the sugar chains attached to the asparagine-297 site on the immunoglobulin heavy chain.

Original language	English
Pages (from-to)	223-228
Number of pages	6
Journal	Cytotechnology
Volume	15
Issue number	1-3
DOIs	https://doi.org/10.1007/BF00762397
Publication status	Published - Feb 1994

Keywords

anti-D
effector function
glycosylation
immunoglobulin G
monoclonal antibody

Access to Document

10.1007/BF00762397

Cite this

@article{46ecc7103c6f4fce99af68ebeb89bfa0,

title = "Glycosylation and functional activity of anti-D secreted by two human lymphoblastoid cell lines",

abstract = "Cell lines BTSN4 and BTSN5 were produced by the Epstein-Barr Virus (EBV) transformation of B-lymphocytes from the same human donor. Both secrete an anti-D monoclonal of the IgG1 subclass but these antibodies display vastly different effector activities. Specifically, anti-D from BTSN4 has a far greater activity in both monocyte-and lymphocyte-mediated ADCC reactions and causes a higher percentage of rosettes to be formed with monocyte-like U937 cells. This variation in functional activity is shown to coincide with changes in the structure of the sugar chains attached to the asparagine-297 site on the immunoglobulin heavy chain.",

keywords = "anti-D, effector function, glycosylation, immunoglobulin G, monoclonal antibody",

author = "Diane Cant and John Barford and Colin Harbour and Anne Fletcher and Nicole Packer and Andrew Gooley",

year = "1994",

month = feb,

doi = "10.1007/BF00762397",

language = "English",

volume = "15",

pages = "223--228",

journal = "Cytotechnology",

issn = "0920-9069",

publisher = "Springer, Springer Nature",

number = "1-3",

}

TY - JOUR

T1 - Glycosylation and functional activity of anti-D secreted by two human lymphoblastoid cell lines

AU - Cant, Diane

AU - Barford, John

AU - Harbour, Colin

AU - Fletcher, Anne

AU - Packer, Nicole

AU - Gooley, Andrew

PY - 1994/2

Y1 - 1994/2

N2 - Cell lines BTSN4 and BTSN5 were produced by the Epstein-Barr Virus (EBV) transformation of B-lymphocytes from the same human donor. Both secrete an anti-D monoclonal of the IgG1 subclass but these antibodies display vastly different effector activities. Specifically, anti-D from BTSN4 has a far greater activity in both monocyte-and lymphocyte-mediated ADCC reactions and causes a higher percentage of rosettes to be formed with monocyte-like U937 cells. This variation in functional activity is shown to coincide with changes in the structure of the sugar chains attached to the asparagine-297 site on the immunoglobulin heavy chain.

AB - Cell lines BTSN4 and BTSN5 were produced by the Epstein-Barr Virus (EBV) transformation of B-lymphocytes from the same human donor. Both secrete an anti-D monoclonal of the IgG1 subclass but these antibodies display vastly different effector activities. Specifically, anti-D from BTSN4 has a far greater activity in both monocyte-and lymphocyte-mediated ADCC reactions and causes a higher percentage of rosettes to be formed with monocyte-like U937 cells. This variation in functional activity is shown to coincide with changes in the structure of the sugar chains attached to the asparagine-297 site on the immunoglobulin heavy chain.

KW - anti-D

KW - effector function

KW - glycosylation

KW - immunoglobulin G

KW - monoclonal antibody

UR - http://www.scopus.com/inward/record.url?scp=0028694341&partnerID=8YFLogxK

U2 - 10.1007/BF00762397

DO - 10.1007/BF00762397

M3 - Article

C2 - 7765935

AN - SCOPUS:0028694341

SN - 0920-9069

VL - 15

SP - 223

EP - 228

JO - Cytotechnology

JF - Cytotechnology

IS - 1-3

ER -

Glycosylation and functional activity of anti-D secreted by two human lymphoblastoid cell lines

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this