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Highly galactosylated anti-her2 antibodies and uses thereof

A technology of galactosylation and fucosylation, which is used in antitumor drugs, digestive systems, chemical instruments and methods, etc.

Inactive Publication Date: 2016-02-03
LABE FR DU FRACTIONNEMENT & DES BIOTECH SA
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, in a large number of patients with HER2+ cancers, trastuzumab is not therapeutically effective

Method used

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  • Highly galactosylated anti-her2 antibodies and uses thereof
  • Highly galactosylated anti-her2 antibodies and uses thereof
  • Highly galactosylated anti-her2 antibodies and uses thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0208] Example 1: Trastuzumab Transgenicly Produced

[0209] The glycosylation pattern of trastuzumab antibodies produced in the milk of transgenic goats was determined by releasing N-glycans from the antibodies and running the released oligosaccharides on a column ("oligosaccharide tag").

[0210] Figure 1-4 and 6 show that from goat #1 ( Figure 2-4 ) and goat #2 ( figure 1 and 6 ) N-glycan oligosaccharides released from trastuzumab antibodies produced transgenically. Monosaccharide groups are described as follows:

[0211] Black squares: N-acetylglucosamine (GlcNac)

[0212] Triangle: fucose

[0213] Gray circle: Mannose

[0214] White circle: Galactose

[0215] Gray diamonds: N-glycolylneuramic acid (NGNA): a type of sialic acid

[0216] White diamonds: N-acetylneuraminic acid (NANA): a type of sialic acid

[0217] figure 1 Representative chromatograms of N-glycan oligosaccharides released from transgenic trastuzumab antibodies produced in the milk of goat #2 a...

Embodiment 2

[0228] Example 2: Glycosylation Analysis of Trastuzumab Transgenically Produced in Other Animals

[0229] Figure 9 The relative percentages of the different N-glycan oligosaccharides present in transgenicly produced trastuzumab from the milk of goat #3 on lactation day 7 and goat #4 on day 3 / 4 of lactation are described and also summarized in In Table 3 below:

[0230] Table 3: Summary of Trastuzumab-generated data in goats #3 and #4

[0231]

[0232] *Calculated according to the formula in the manual

[0233] Figure 10 The relative percentages of different N-glycan oligosaccharides present in transgenicly produced trastuzumab antibodies from milk of goat #5 on day 3 of lactation and goat #6 on days 5, 6 and 7 of lactation are described in , and are also summarized in Table 4 below:

[0234] Table 4: Summary of data for Trastuzumab produced in goats #5 and #6

[0235]

[0236] *Calculated according to the formula in the manual

[0237] Figure 11 The relative p...

Embodiment 3

[0247] Characterization of the trastuzumab produced by the transgene of embodiment 3

[0248] Functional characterization of transgenically produced trastuzumab produced in goat milk with commercial / trastuzumab comparison. Binding affinities to HER2-expressing cell lines, CD16 on NK cells, and C1q were quantified. In addition, these antibodies were evaluated for their ability to induce lysis of HER2-expressing cell lines by antibody-dependent cell-mediated cytotoxicity (ADCC) and complement-dependent cytotoxicity (CDC), as well as their ability to inhibit cell proliferation.

[0249] For transgenic produced trastuzumab lot A, transgenic produced trastuzumab lot B and commercial / trastuzumab (Roche), antigen recognition on the HER2-expressing SK-BR-3 cell line was of the same order (arbitrary dissociation constant, Kd, ​​2-6 μg / ml). Transgenicly produced trastuzumab antibody with an IC of 30 μg / ml (for batch A) and 25 μg / ml (for batch B) 50 Values ​​bind to the CD16 rece...

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Abstract

In one aspect, the disclosure relates to highly galactosylated anti-HER2 antibodies and compositions thereof. In one aspect, the disclosure relates to populations of anti-HER2 antibodies with a high level of galactosylation, and compositions thereof. In one aspect, the disclosure relates to methods of production and use of highly galactosylated anti-HER2 antibodies and populations of anti-HER2 antibodies with a high level of galactosylation. In some embodiments the anti-HER-2 antibody is trastuzumab.

Description

[0001] related application [0002] This application claims the benefit under 35 U.S.C § 119(e) of U.S. Provisional Application Serial No. 61 / 764,488, filed February 13, 2013, entitled "Highly Galactosylated Anti-HER2 Antibodies and Uses Thereof," the entirety of which The disclosure is incorporated herein by reference. field of invention [0003] The present invention relates in part to the field of anti-HER2 antibodies. Background of the invention [0004] HER2 (human epidermal growth factor receptor 2), also known as HER2 / neu or ErbB2, is a member of the epidermal growth factor receptor family. HER2 is a plasma membrane-bound receptor tyrosine kinase that can dimerize with itself and with other members of the epidermal growth factor receptor family (HER1, HER2, HER3 and HER4). Dimerization in turn leads to the activation of various intracellular pathways. HER2 is an oncogene that is overexpressed in a variety of cancers, including breast, ovarian, gastric and uterine c...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): C07K16/32
CPCC07K2317/12C07K2317/41C07K2317/73C07K2317/732C07K2317/734C07K16/32A61P1/04A61P15/00A61P35/00C07K2317/14C07K2317/92
Inventor H.M.米德L-H.陈
Owner LABE FR DU FRACTIONNEMENT & DES BIOTECH SA
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