A recombinant, fully human monoclonal antibody with antitumor activity constructed from phage-displayed antibody fragments

GA Huls; IAFM Heijnen; ME Cuomo; JC Koningsberger; E Boel; ARV de Vries; SAJ Loyson; W Helfrich; GPV Henegouwen; M van Meijer; J de Kruif; T Logtenberg

A recombinant, fully human monoclonal antibody with antitumor activity constructed from phage-displayed antibody fragments

GA Huls, IAFM Heijnen, ME Cuomo, JC Koningsberger, E Boel, ARV de Vries, SAJ Loyson, W Helfrich, GPV Henegouwen, M van Meijer, J de Kruif, T Logtenberg^*

^*Corresponding author for this work

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

91 Citations (Scopus)

Abstract

A single-chain Fv antibody fragment specific for the tumor-associated Ep-CAM molecule was isolated from a semisynthetic phage display library and converted into an intact, fully human IgG1 monoclonal antibody (huMab), The purified huMab had an affinity of 5 nM and effectively mediated tumor cell killing in: in vitro and in vivo assays. These experiments show that nonimmunized phage antibody display libraries can be used to obtain high-affinity, functional, and clinically applicable huMabs directed against a tumor-associated antigen.

Original language	English
Pages (from-to)	276-281
Number of pages	6
Journal	Nature Biotechnology
Volume	17
Issue number	3
Publication status	Published - Mar-1999

Keywords

phage display
Ep-CAM
single-chain Fv
immunotherapy
recombinant antibodies
IMMUNE-RESPONSE
HUMAN IGG1
MOUSE
THERAPY
ANTIGEN
PHARMACOKINETICS
IMMUNOTHERAPY
GLYCOPROTEIN
RECOGNITION
SELECTION

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@article{43db691ca54647dcb384b0035f052fbf,

title = "A recombinant, fully human monoclonal antibody with antitumor activity constructed from phage-displayed antibody fragments",

abstract = "A single-chain Fv antibody fragment specific for the tumor-associated Ep-CAM molecule was isolated from a semisynthetic phage display library and converted into an intact, fully human IgG1 monoclonal antibody (huMab), The purified huMab had an affinity of 5 nM and effectively mediated tumor cell killing in: in vitro and in vivo assays. These experiments show that nonimmunized phage antibody display libraries can be used to obtain high-affinity, functional, and clinically applicable huMabs directed against a tumor-associated antigen.",

keywords = "phage display, Ep-CAM, single-chain Fv, immunotherapy, recombinant antibodies, IMMUNE-RESPONSE, HUMAN IGG1, MOUSE, THERAPY, ANTIGEN, PHARMACOKINETICS, IMMUNOTHERAPY, GLYCOPROTEIN, RECOGNITION, SELECTION",

author = "GA Huls and IAFM Heijnen and ME Cuomo and JC Koningsberger and E Boel and {de Vries}, ARV and SAJ Loyson and W Helfrich and GPV Henegouwen and {van Meijer}, M and {de Kruif}, J and T Logtenberg",

year = "1999",

month = mar,

language = "English",

volume = "17",

pages = "276--281",

journal = "Nature Biotechnology",

issn = "1087-0156",

publisher = "Nature Publishing Group",

number = "3",

}

TY - JOUR

T1 - A recombinant, fully human monoclonal antibody with antitumor activity constructed from phage-displayed antibody fragments

AU - Huls, GA

AU - Heijnen, IAFM

AU - Cuomo, ME

AU - Koningsberger, JC

AU - Boel, E

AU - de Vries, ARV

AU - Loyson, SAJ

AU - Helfrich, W

AU - Henegouwen, GPV

AU - van Meijer, M

AU - de Kruif, J

AU - Logtenberg, T

PY - 1999/3

Y1 - 1999/3

N2 - A single-chain Fv antibody fragment specific for the tumor-associated Ep-CAM molecule was isolated from a semisynthetic phage display library and converted into an intact, fully human IgG1 monoclonal antibody (huMab), The purified huMab had an affinity of 5 nM and effectively mediated tumor cell killing in: in vitro and in vivo assays. These experiments show that nonimmunized phage antibody display libraries can be used to obtain high-affinity, functional, and clinically applicable huMabs directed against a tumor-associated antigen.

AB - A single-chain Fv antibody fragment specific for the tumor-associated Ep-CAM molecule was isolated from a semisynthetic phage display library and converted into an intact, fully human IgG1 monoclonal antibody (huMab), The purified huMab had an affinity of 5 nM and effectively mediated tumor cell killing in: in vitro and in vivo assays. These experiments show that nonimmunized phage antibody display libraries can be used to obtain high-affinity, functional, and clinically applicable huMabs directed against a tumor-associated antigen.

KW - phage display

KW - Ep-CAM

KW - single-chain Fv

KW - immunotherapy

KW - recombinant antibodies

KW - IMMUNE-RESPONSE

KW - HUMAN IGG1

KW - MOUSE

KW - THERAPY

KW - ANTIGEN

KW - PHARMACOKINETICS

KW - IMMUNOTHERAPY

KW - GLYCOPROTEIN

KW - RECOGNITION

KW - SELECTION

M3 - Article

SN - 1087-0156

VL - 17

SP - 276

EP - 281

JO - Nature Biotechnology

JF - Nature Biotechnology

IS - 3

ER -

A recombinant, fully human monoclonal antibody with antitumor activity constructed from phage-displayed antibody fragments

Abstract

Keywords

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