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Identification of antibody glycosylation structures that predict monoclonal antibody Fc-effector function

To determine monoclonal antibody (mAb) features that predict fragment crystalizable (Fc)-mediated effector functions against HIV. Monoclonal antibodies, derived from Chinese hamster ovary cells or Epstein-Barr virus-immortalized mouse heteromyelomas, with specificity to key regions of the HIV envelo... Full description

Journal Title: AIDS (London) 2014, Vol.28 (17), p.2523-2530
Main Author: CHUNG, Amy W
Other Authors: CRISPIN, Max , ALTER, Galit , PRITCHARD, Laura , ROBINSON, Hannah , GORNY, Miroslaw K , XIAOJIE YU , BAILEY-KELLOGG, Chris , ACKERMAN, Margaret E , SCANLAN, Chris , ZOLLA-PAZNER, Susan
Format: Electronic Article Electronic Article
Language: English
Subjects:
Publisher: Hagerstown, MD: Lippincott Williams & Wilkins
ID: ISSN: 0269-9370
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recordid: cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4429604
title: Identification of antibody glycosylation structures that predict monoclonal antibody Fc-effector function
format: Article
creator:
  • CHUNG, Amy W
  • CRISPIN, Max
  • ALTER, Galit
  • PRITCHARD, Laura
  • ROBINSON, Hannah
  • GORNY, Miroslaw K
  • XIAOJIE YU
  • BAILEY-KELLOGG, Chris
  • ACKERMAN, Margaret E
  • SCANLAN, Chris
  • ZOLLA-PAZNER, Susan
subjects:
  • AIDS/HIV
  • Animals
  • Antibodies, Monoclonal - chemistry
  • Antibodies, Monoclonal - immunology
  • Antibodies, Monoclonal - isolation & purification
  • Antibody Affinity
  • Antibody-Dependent Cell Cytotoxicity
  • antibody-dependent cellular cytotoxicity
  • antibody-dependent cellular phagocytosis
  • Article
  • Biological and medical sciences
  • Chromatography, High Pressure Liquid
  • Cricetulus
  • env Gene Products, Human Immunodeficiency Virus - immunology
  • glycan structure
  • Glycosylation
  • HIV - immunology
  • HIV Antibodies - chemistry
  • HIV Antibodies - immunology
  • HIV Antibodies - isolation & purification
  • Human viral diseases
  • Immunoglobulin Fc Fragments - chemistry
  • Immunoglobulin Fc Fragments - metabolism
  • Infectious diseases
  • Lentivirus
  • Medical sciences
  • Mice
  • monoclonal antibody
  • Phagocytosis
  • Protein Binding
  • Receptors, IgG - metabolism
  • Retroviridae
  • Viral diseases
  • Viral diseases of the lymphoid tissue and the blood. Aids
ispartof: AIDS (London), 2014, Vol.28 (17), p.2523-2530
description: To determine monoclonal antibody (mAb) features that predict fragment crystalizable (Fc)-mediated effector functions against HIV. Monoclonal antibodies, derived from Chinese hamster ovary cells or Epstein-Barr virus-immortalized mouse heteromyelomas, with specificity to key regions of the HIV envelope including gp120-V2, gp120-V3 loop, gp120-CD4(+) binding site, and gp41-specific antibodies, were functionally profiled to determine the relative contribution of the variable and constant domain features of the antibodies in driving robust Fc-effector functions. Each mAb was assayed for antibody-binding affinity to gp140(SR162), antibody-dependent cellular cytotoxicity (ADCC), antibody-dependent cellular phagocytosis (ADCP) and for the ability to bind to FcγRIIa, FcγRIIb and FcγRIIIa receptors. Antibody glycan profiles were determined by HPLC. Neither the specificity nor the affinity of the mAbs determined the potency of Fc-effector function. FcγRIIIa binding strongly predicted ADCC and decreased galactose content inversely correlated with ADCP, whereas N-glycolylneuraminic acid-containing structures exhibited enhanced ADCP. Additionally, the bi-antenary glycan arm onto which galactose was added predicted enhanced binding to FcγRIIIa and ADCC activity, independent of the specificity of the mAb. Our studies point to the specific Fc-glycan structures that can selectively promote Fc-effector functions independently of the antibody specificity. Furthermore, we demonstrated antibody glycan structures associated with enhanced ADCP activity, an emerging Fc-effector function that may aid in the control and clearance of HIV infection.
language: eng
source:
identifier: ISSN: 0269-9370
fulltext: no_fulltext
issn:
  • 0269-9370
  • 1473-5571
url: Link


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titleIdentification of antibody glycosylation structures that predict monoclonal antibody Fc-effector function
creatorCHUNG, Amy W ; CRISPIN, Max ; ALTER, Galit ; PRITCHARD, Laura ; ROBINSON, Hannah ; GORNY, Miroslaw K ; XIAOJIE YU ; BAILEY-KELLOGG, Chris ; ACKERMAN, Margaret E ; SCANLAN, Chris ; ZOLLA-PAZNER, Susan
creatorcontribCHUNG, Amy W ; CRISPIN, Max ; ALTER, Galit ; PRITCHARD, Laura ; ROBINSON, Hannah ; GORNY, Miroslaw K ; XIAOJIE YU ; BAILEY-KELLOGG, Chris ; ACKERMAN, Margaret E ; SCANLAN, Chris ; ZOLLA-PAZNER, Susan
descriptionTo determine monoclonal antibody (mAb) features that predict fragment crystalizable (Fc)-mediated effector functions against HIV. Monoclonal antibodies, derived from Chinese hamster ovary cells or Epstein-Barr virus-immortalized mouse heteromyelomas, with specificity to key regions of the HIV envelope including gp120-V2, gp120-V3 loop, gp120-CD4(+) binding site, and gp41-specific antibodies, were functionally profiled to determine the relative contribution of the variable and constant domain features of the antibodies in driving robust Fc-effector functions. Each mAb was assayed for antibody-binding affinity to gp140(SR162), antibody-dependent cellular cytotoxicity (ADCC), antibody-dependent cellular phagocytosis (ADCP) and for the ability to bind to FcγRIIa, FcγRIIb and FcγRIIIa receptors. Antibody glycan profiles were determined by HPLC. Neither the specificity nor the affinity of the mAbs determined the potency of Fc-effector function. FcγRIIIa binding strongly predicted ADCC and decreased galactose content inversely correlated with ADCP, whereas N-glycolylneuraminic acid-containing structures exhibited enhanced ADCP. Additionally, the bi-antenary glycan arm onto which galactose was added predicted enhanced binding to FcγRIIIa and ADCC activity, independent of the specificity of the mAb. Our studies point to the specific Fc-glycan structures that can selectively promote Fc-effector functions independently of the antibody specificity. Furthermore, we demonstrated antibody glycan structures associated with enhanced ADCP activity, an emerging Fc-effector function that may aid in the control and clearance of HIV infection.
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languageeng
publisherHagerstown, MD: Lippincott Williams & Wilkins
subjectAIDS/HIV ; Animals ; Antibodies, Monoclonal - chemistry ; Antibodies, Monoclonal - immunology ; Antibodies, Monoclonal - isolation & purification ; Antibody Affinity ; Antibody-Dependent Cell Cytotoxicity ; antibody-dependent cellular cytotoxicity ; antibody-dependent cellular phagocytosis ; Article ; Biological and medical sciences ; Chromatography, High Pressure Liquid ; Cricetulus ; env Gene Products, Human Immunodeficiency Virus - immunology ; glycan structure ; Glycosylation ; HIV - immunology ; HIV Antibodies - chemistry ; HIV Antibodies - immunology ; HIV Antibodies - isolation & purification ; Human viral diseases ; Immunoglobulin Fc Fragments - chemistry ; Immunoglobulin Fc Fragments - metabolism ; Infectious diseases ; Lentivirus ; Medical sciences ; Mice ; monoclonal antibody ; Phagocytosis ; Protein Binding ; Receptors, IgG - metabolism ; Retroviridae ; Viral diseases ; Viral diseases of the lymphoid tissue and the blood. Aids
ispartofAIDS (London), 2014, Vol.28 (17), p.2523-2530
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0CHUNG, Amy W
1CRISPIN, Max
2ALTER, Galit
3PRITCHARD, Laura
4ROBINSON, Hannah
5GORNY, Miroslaw K
6XIAOJIE YU
7BAILEY-KELLOGG, Chris
8ACKERMAN, Margaret E
9SCANLAN, Chris
10ZOLLA-PAZNER, Susan
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0Identification of antibody glycosylation structures that predict monoclonal antibody Fc-effector function
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descriptionTo determine monoclonal antibody (mAb) features that predict fragment crystalizable (Fc)-mediated effector functions against HIV. Monoclonal antibodies, derived from Chinese hamster ovary cells or Epstein-Barr virus-immortalized mouse heteromyelomas, with specificity to key regions of the HIV envelope including gp120-V2, gp120-V3 loop, gp120-CD4(+) binding site, and gp41-specific antibodies, were functionally profiled to determine the relative contribution of the variable and constant domain features of the antibodies in driving robust Fc-effector functions. Each mAb was assayed for antibody-binding affinity to gp140(SR162), antibody-dependent cellular cytotoxicity (ADCC), antibody-dependent cellular phagocytosis (ADCP) and for the ability to bind to FcγRIIa, FcγRIIb and FcγRIIIa receptors. Antibody glycan profiles were determined by HPLC. Neither the specificity nor the affinity of the mAbs determined the potency of Fc-effector function. FcγRIIIa binding strongly predicted ADCC and decreased galactose content inversely correlated with ADCP, whereas N-glycolylneuraminic acid-containing structures exhibited enhanced ADCP. Additionally, the bi-antenary glycan arm onto which galactose was added predicted enhanced binding to FcγRIIIa and ADCC activity, independent of the specificity of the mAb. Our studies point to the specific Fc-glycan structures that can selectively promote Fc-effector functions independently of the antibody specificity. Furthermore, we demonstrated antibody glycan structures associated with enhanced ADCP activity, an emerging Fc-effector function that may aid in the control and clearance of HIV infection.
subject
0AIDS/HIV
1Animals
2Antibodies, Monoclonal - chemistry
3Antibodies, Monoclonal - immunology
4Antibodies, Monoclonal - isolation & purification
5Antibody Affinity
6Antibody-Dependent Cell Cytotoxicity
7antibody-dependent cellular cytotoxicity
8antibody-dependent cellular phagocytosis
9Article
10Biological and medical sciences
11Chromatography, High Pressure Liquid
12Cricetulus
13env Gene Products, Human Immunodeficiency Virus - immunology
14glycan structure
15Glycosylation
16HIV - immunology
17HIV Antibodies - chemistry
18HIV Antibodies - immunology
19HIV Antibodies - isolation & purification
20Human viral diseases
21Immunoglobulin Fc Fragments - chemistry
22Immunoglobulin Fc Fragments - metabolism
23Infectious diseases
24Lentivirus
25Medical sciences
26Mice
27monoclonal antibody
28Phagocytosis
29Protein Binding
30Receptors, IgG - metabolism
31Retroviridae
32Viral diseases
33Viral diseases of the lymphoid tissue and the blood. Aids
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titleIdentification of antibody glycosylation structures that predict monoclonal antibody Fc-effector function
authorCHUNG, Amy W ; CRISPIN, Max ; ALTER, Galit ; PRITCHARD, Laura ; ROBINSON, Hannah ; GORNY, Miroslaw K ; XIAOJIE YU ; BAILEY-KELLOGG, Chris ; ACKERMAN, Margaret E ; SCANLAN, Chris ; ZOLLA-PAZNER, Susan
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1Animals
2Antibodies, Monoclonal - chemistry
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4Antibodies, Monoclonal - isolation & purification
5Antibody Affinity
6Antibody-Dependent Cell Cytotoxicity
7antibody-dependent cellular cytotoxicity
8antibody-dependent cellular phagocytosis
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11Chromatography, High Pressure Liquid
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13env Gene Products, Human Immunodeficiency Virus - immunology
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17HIV Antibodies - chemistry
18HIV Antibodies - immunology
19HIV Antibodies - isolation & purification
20Human viral diseases
21Immunoglobulin Fc Fragments - chemistry
22Immunoglobulin Fc Fragments - metabolism
23Infectious diseases
24Lentivirus
25Medical sciences
26Mice
27monoclonal antibody
28Phagocytosis
29Protein Binding
30Receptors, IgG - metabolism
31Retroviridae
32Viral diseases
33Viral diseases of the lymphoid tissue and the blood. Aids
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8ACKERMAN, Margaret E
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pages2523-2530
issn0269-9370
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abstractTo determine monoclonal antibody (mAb) features that predict fragment crystalizable (Fc)-mediated effector functions against HIV. Monoclonal antibodies, derived from Chinese hamster ovary cells or Epstein-Barr virus-immortalized mouse heteromyelomas, with specificity to key regions of the HIV envelope including gp120-V2, gp120-V3 loop, gp120-CD4(+) binding site, and gp41-specific antibodies, were functionally profiled to determine the relative contribution of the variable and constant domain features of the antibodies in driving robust Fc-effector functions. Each mAb was assayed for antibody-binding affinity to gp140(SR162), antibody-dependent cellular cytotoxicity (ADCC), antibody-dependent cellular phagocytosis (ADCP) and for the ability to bind to FcγRIIa, FcγRIIb and FcγRIIIa receptors. Antibody glycan profiles were determined by HPLC. Neither the specificity nor the affinity of the mAbs determined the potency of Fc-effector function. FcγRIIIa binding strongly predicted ADCC and decreased galactose content inversely correlated with ADCP, whereas N-glycolylneuraminic acid-containing structures exhibited enhanced ADCP. Additionally, the bi-antenary glycan arm onto which galactose was added predicted enhanced binding to FcγRIIIa and ADCC activity, independent of the specificity of the mAb. Our studies point to the specific Fc-glycan structures that can selectively promote Fc-effector functions independently of the antibody specificity. Furthermore, we demonstrated antibody glycan structures associated with enhanced ADCP activity, an emerging Fc-effector function that may aid in the control and clearance of HIV infection.
copHagerstown, MD
pubLippincott Williams & Wilkins
pmid25160934
doi10.1097/QAD.0000000000000444
oafree_for_read