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Preparation of full-length human antibody

A humanized antibody, antibody technology, applied in the field of preparation of fully humanized antibody

Inactive Publication Date: 2005-06-15
CCL HLDG
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0042] A further problem with generating therapeutically effective antibodies targeting gp120 is that the primary structure of gp120, i.e. the amino acid sequence, is highly variable among different HIV-1 strains (Kuhmann et al., 2000; Hahn et al. , 1985; Modrow et al., 1987; Thomson et al., 2002)

Method used

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  • Preparation of full-length human antibody
  • Preparation of full-length human antibody
  • Preparation of full-length human antibody

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preparation example Construction

[0083] The present invention provides a method for producing fully humanized antibodies capable of recognizing a predetermined antigen without relying on human donors who have been exposed to the antigen. To achieve this, lymphocytes from natural human donors are immunized with the antigen of interest in vitro, and then antibody-producing cells against the antigen are identified and screened. Since lymphocytes immunize in vitro rather than in vivo, it is possible to regulate the antigen or antigen fragment recognized by the antibody. A preferred antigen is the HIV gp120 protein, particularly the binding site of the gp120 co-receptor molecule.

[0084] Unless otherwise stated, before further elaborating the present invention, the terms used in this application are defined as follows.

[0085] A "fully humanized antibody" refers to an antibody that contains only human sequences. The antibody is preferably a monoclonal antibody. A "naive human donor" is a person who has never b...

Embodiment 1

[0177] Preparation of peptide antigens

[0178] Synthetic peptides corresponding to HIV-1 gp120 V3 loop are listed in Table 1.

[0179] Table 1

[0180] Synthetic Peptide Amino Acid Sequence of Synthetic Peptide in HIV-1 gp120 V3 Co-receptor Molecular Binding Region

[0181] HIV-1 strain / subtype amino acid sequence and sequence comparison SEQ ID NO.

[0182] V3 ALL con HIV-1 consensus sequence N’- R K S I H I . . G P G Q A F Y A T -C’ 2

[0183] V3 A con Subtype A consensus sequence N’- - - - V R - . . - - - - - - - - - - -C’ 3

[0184] V3 B con Subtype B consensus sequence N’- - - - - - - . . - - - R - - - T - -C’ 4

[0185] V3 B(MN) MN(B subtype) N'- - - R - - - . . - - - R - - - T - -C' 5

[0186] V3 B(IIIB) IIIB(B subtype) N'- - - - - R - Q R - - - R - - V - C' 6

[0187] V3 C con Subtype C consensus sequence N’- - - - - R - . . - - - - T - - - - -C’ 7

[0188] V3 D con Subtype D consensus seq...

Embodiment 2

[0203] CD8 + and CD56 + Depletion of cell populations results in increased antigen-responsive immune cells

[0204] Because the removal of cytotoxic or suppressive cell populations plays an integral role in the overall immune response to antigens in vitro (Ohlin et al., 1989; 1992), various methods for removing cells were compared in in vitro immunological studies. Effects of cytotoxic agents. These reagents include LeuLeuOMe, anti-CD8 antibody used in cell magnetization removal, anti-CD56 antibody used in cell magnetization removal, and combination of anti-CD8 antibody and anti-CD56 antibody used in cell magnetization removal. Thus, peripheral blood mononuclear cells (PBMC S ) were treated with each reagent, or no reagent was added as a blank control (nil). Four PBMCs from different donors were tested. In vitro immunizations were performed as described in the "Materials and Methods" section, including primary and secondary immunizations with the peptide antigen TT-V3B(MN...

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Abstract

The present invention provides a method for producing a fully humanized antibody that recognizes a predetermined antigen and does not rely on a human donor who has been exposed to the antigen. To achieve this, lymphocytes from natural human donors are immunized in vitro with an antigen of interest, and antibody-producing cells directed against said antigen are then identified. Because lymphocytes immunize in vitro rather than in vivo, it is possible to modulate the antigen or antigen fragment recognized by the antibody. A preferred antigen is an HIV gp120 peptide, especially the co-receptor binding region of gp120.

Description

field of invention [0001] The present invention relates to methods for preparing fully human antibodies against any antigen of interest and the resulting antibodies. [0002] references [0003] U.S. Patent No. 5,023,252 [0004] U.S. Patent No. 6,190,871 [0005] U.S. Patent No. 6,228,361 [0006] U.S. Patent No. 6,261,558 [0007] U.S. Patent No. 6,391,635 [0008] U.S. Patent No. 6,395,275 [0009] U.S. Patent No. 6,514,496 [0010] U.S. Patent No. 6,592,904 [0011] Breedveld FC. (2000) Therapeutic monoclonal antibodies, Lancet 355: 735-40. [0012] Chin LT, Hinkula J, Levi M, Ohlin M, Wahren B, Borrebaeck CAK. (1994) Site-directed primary in vitro immunization: production of neutralizing human monoclonal antibodies to HIV-1 from seronegative donors. Immunology 81:428-434. [0013] Chin LT, Malmborg AC, Kristensson K, Hinkula J, Borrebaeck, CAK. (1995) In vitro modeling of humoral immune responses leads to antigen-specific isotype switching of autologous T helper ...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): C12N15/02A61K39/395A61P31/18C07K16/00C07K16/10C12N5/10C12P21/08
CPCA61K2039/5158A61P31/18C07K16/00C07K16/1063C07K2317/21C07K2317/34
Inventor 金立德
Owner CCL HLDG
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