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1. 发明申请

WO2016102436A1 CMP-DEPENDENT SIALIDASE ACTIVITY 审中-公开
标题翻译： CMP依赖性SIALIDASE活性
公开(公告)号：WO2016102436A1
公开(公告)日：2016-06-30
申请号：PCT/EP2015/080741
申请日：2015-12-21
申请人： F. HOFFMANN-LA ROCHE AG , ROCHE DIAGNOSTICS GMBH , ROCHE DIAGNOSTICS OPERATIONS, INC.
发明人： SOBEK, Harald , GREIF, Michael , THOMANN, Marco , MALIK, Sebastian
IPC分类号： C12N9/10 , C12P19/44
CPC分类号： C12P21/005 , C07K16/00 , C07K2317/41 , C12N9/1081 , C12P19/44 , C12Y204/99001 , C12Y301/03
摘要： The present disclosure is directed to the properties of certain glycosyltransferase variants having N-terminal truncation deletions or internal deletions. Any of the mutants disclosed in here exhibit α-2,6-sialyltransferase enzymatic activity in the presence of CMP-activated sialic acid as co-substrate, and in the presence of a suitable acceptor site. A fundamental finding documented in the present disclosure is that suchs enzyme are not only capable of catalyzing transfer of a sialidyl moiety but they are also capable of catalyzing hydrolytic cleavage of terminally bound sialic acid from a glycan. Particularly it was found that in the presence of cytidine 5'-monophosphate (CMP) glycosyltransferase activity is inhibited, and sialidase activity is stimulated. Sialidase activity was found to be dependent on the presence of a particular stretch of amino acids (position 90 to 108) in the polypeptide sequence of the reference (wildtype) hST6Gal-I polypeptide. Deletion of this sequence portion in an N-terminal truncation variant was found to abolish sialidase activity, notably both in the presence and in the absence of CMP. Thus, disclosed are compositions, uses and methods employing the CMP-mediated feed-back regulation documented herein.
摘要翻译：本公开涉及具有N-末端截短缺失或内部缺失的某些糖基转移酶变体的性质。本文公开的任何突变体在存在CMP活化唾液酸作为底物的情况下和在合适的受体位点存在下显示出α-2,6-唾液酸转移酶酶活性。本公开文献中记载的基本发现是这样的酶不仅能够催化唾液酸基部分的转移，而且还能够催化从聚糖中终止结合的唾液酸的水解裂解。特别是发现在胞苷5'-单磷酸（CMP）存在下，糖基转移酶活性受到抑制，刺激唾液酸酶活性。发现唾液酸酶活性取决于参考（野生型）hST6Gal-1多肽的多肽序列中特定氨基酸段（位置90至108）的存在。发现N末端截短变体中该序列部分的缺失可以消除唾液酸酶活性，特别是在存在和不存在CMP的情况下。因此，公开了使用本文记载的CMP介导的反馈调节物的组合物，用途和方法。

2. 发明申请

WO2015001033A1 PROCESS FOR THE MONO- AND BI-SIALYLATION OF GLYCOPROTEINS EMPLOYING N-TERMINALLY TRUNCATED BETA-GALACTOSIDE ALPHA-2,6-SIALYLTRANSFERASE MUTANTS 审中-公开
标题翻译：使用N-末端截短的β-葡糖苷二磷酸二异氰酸酯酶突变体的甘氨酸的单一和双取代的方法
公开(公告)号：WO2015001033A1
公开(公告)日：2015-01-08
申请号：PCT/EP2014/064213
申请日：2014-07-03
申请人： F. HOFFMANN-LA ROCHE AG , ROCHE DIAGNOSTICS GMBH , ROCHE DIAGNOSTICS OPERATIONS, INC.
发明人： CZABANY, Tibor , ENGEL, Alfred , GREIF, Michael , JUNG, Christine , LULEY, Christiane , MALIK, Sebastian , MUELLER, Rainer , NIDETZKY, Bernd , RIBITSCH, Doris , SCHMOELZER, Katharina , SCHWAB, Helmut , SOBEK, Harald , SUPPMANN, Bernhard , THOMANN, Marco , ZITZENBACHER, Sabine
IPC分类号： C12P19/18 , C12P21/00 , C12N9/10 , C07K16/00
CPC分类号： C12P21/005 , C07K16/00 , C07K2317/14 , C07K2317/24 , C07K2317/41 , C12N9/1081 , C12P19/18 , C12Y204/99001
摘要： The present disclosure is directed to the use of certain glycosyltransferase variants having N-terminal truncation deletions. It was found that the combination of two different truncation variants of human β-galactoside-α-2,6-sialyltransferase I (hST6Gal-I) exhibited different specific sialyltransferase enzymatic activities. In one example, under conditions wherein the first variant Δ89 hST6Gal-I catalyzed formation of bi-sialylated target molecules the second variant Δ108 hST6Gal-I catalyzed formation of mono-sialylated target molecules. Thus, disclosed are variants of mammalian glycosyltransferase, nucleic acids encoding the same, methods and means for recombinantly producing the variants of mammalian glycosyltransferase and use thereof, particularly for sialylating in a quantitatively controlled manner terminal acceptor groups of glycan moieties being part of glycoproteins such as immunoglobulins.
摘要翻译：本公开涉及使用具有N-末端截短缺失的某些糖基转移酶变体。发现人和半乳糖苷-α-2,6-唾液酸转移酶I（hST6Gal-1）的两种不同截短变体的组合表现出不同的特异性唾液酸转移酶酶活性。在一个实例中，在第一变体和Dgr; 89hST6Gal-1催化双唾液酸化靶向分子的形成的条件下，第二变体Dgr; 108hST6Gal-1催化单唾液酸化靶分子的形成。因此，公开了哺乳动物糖基转移酶的变体，编码它们的核酸，用于重组产生哺乳动物糖基转移酶变体的方法和手段及其用途，特别是以定量控制的方式唾液酸化作为糖蛋白部分的聚糖部分的末端受体基团，例如免疫球蛋白。

3. 发明申请

WO2015001034A1 N-TERMINALLY TRUNCATED GLYCOSYLTRANSFERASES 审中-公开
标题翻译： N-末端截短的谷氨酰胺转移酶
公开(公告)号：WO2015001034A1
公开(公告)日：2015-01-08
申请号：PCT/EP2014/064214
申请日：2014-07-03
申请人： F. HOFFMANN-LA ROCHE AG , ROCHE DIAGNOSTICS GMBH , ROCHE DIAGNOSTICS OPERATIONS, INC.
发明人： CZABANY, Tibor , ENGEL, Alfred , GREIF, Michael , JUNG, Christine , LULEY, Christiane , MALIK, Sebastian , MUELLER, Rainer , NIDETZKY, Bernd , RIBITSCH, Doris , SCHMOELZER, Katharina , SCHWAB, Helmut , SOBEK, Harald , SUPPMANN, Bernhard , THOMANN, Marco , ZITZENBACHER, Sabine
IPC分类号： C12N9/10
CPC分类号： C12N9/1081 , C12N9/1048 , C12Y204/99001
摘要： The present disclosure is directed to glycosyltransferase variants having N-terminal truncation deletions. Contrary to previous findings certain truncations comprising the conserved amino acid motif ("QVWxKDS") were found to be compatible with glycosyltransferase enzymatic activity, particularly in a human sialyltransferase (hST6Gal-I). Thus, disclosed are variants of mammalian glycosyltransferase, nucleic acids encoding the same, methods and means for recombinantly producing the variants of mammalian glycosyltransferase and use thereof, particularly for sialylating terminal acceptor groups of glycan moieties being part of glycoproteins such as immunoglobulins.
摘要翻译：本公开涉及具有N-末端截短缺失的糖基转移酶变体。与之前的发现相反，发现包含保守氨基酸基序（“QVWxKDS”）的某些截短与糖基转移酶酶活性相容，特别是在人唾液酸转移酶（hST6Gal-1）中。因此，公开了哺乳动物糖基转移酶的变体，编码它们的核酸，用于重组产生哺乳动物糖基转移酶变体的方法和手段及其用途，特别是用作糖蛋白的部分的聚糖末端受体基团，例如免疫球蛋白。

4. 发明申请

WO2014191240A1 QUANTITATIVE CONTROL OF SIALYLATION 审中-公开
标题翻译： SIALYLATION的量化控制
公开(公告)号：WO2014191240A1
公开(公告)日：2014-12-04
申请号：PCT/EP2014/060101
申请日：2014-05-16
申请人： F. HOFFMANN-LA ROCHE AG , ROCHE DIAGNOSTICS GMBH , ROCHE DIAGNOSTICS OPERATIONS, INC.
发明人： ENGEL, Alfred , GREIF, Michael , JUNG, Christine , MALIK, Sebastian , MUELLER, Rainer , SOBEK, Harald , SUPPMANN, Bernhard , THOMANN, Marco
IPC分类号： C12P21/00 , C12P19/18 , A61K39/395
CPC分类号： C12P19/18 , C12N9/1081 , C12P19/02 , C12P19/44 , C12P21/005
摘要： The present disclosure is directed to the use of certain glycosyltransferase variants having N-terminal truncation deletions. Contrary to previous findings certain truncations were found to exhibit sialidase enzymatic activity, particularly a variant of human sialyltransferase (hST6Gal-I) with a truncation deletion involving the first 89 N-terminal amino acids of the respective wild-type polypeptide. A fundamental finding documented in the present disclosure is that there exists a variant of this enzyme which is capable of catalyzing transfer of a glycosyl moiety as well as hydrolysis thereof. Thus, disclosed is a specific exemplary variant of mammalian glycosyltransferase, nucleic acids encoding the same, methods and means for recombinantly producing the variant of mammalian glycosyltransferase and use thereof, particularly for sialylating in a quantitatively controlled manner terminal acceptor groups of glycan moieties being part of glycoproteins such as immunoglobulins.
摘要翻译：本公开涉及使用具有N-末端截短缺失的某些糖基转移酶变体。与之前的发现相反，发现某些截短表现出唾液酸酶酶活性，特别是具有涉及相应野生型多肽的前89个N-末端氨基酸的截短缺失的人唾液酸转移酶（hST6Gal-1）的变体。在本公开文献中记载的基本发现是存在能够催化糖基部分的转移以及其水解的酶的变体。因此，所公开的是哺乳动物糖基转移酶的特定示例性变体，编码哺乳动物糖基转移酶的核酸，用于重组产生哺乳动物糖基转移酶变体的方法和手段及其用途，特别是以定量控制的方式唾液酸化，聚糖部分的末端受体基团是糖蛋白如免疫球蛋白。

5. 发明申请

WO2018114877A1 IN VITRO GLYCOENGINEERING OF ANTIBODIES 审中-公开
公开(公告)号：WO2018114877A1
公开(公告)日：2018-06-28
申请号：PCT/EP2017/083429
申请日：2017-12-19
申请人： F. HOFFMANN-LA ROCHE AG , HOFFMANN-LA ROCHE INC.
发明人： FALKENSTEIN, Roberto , WALCH, Heiko , MALIK, Sebastian , THOMANN, Marco , FREIHERR VON ROMAN, Matthias , SCHMID, Ingrid , DORN, Roland , HINGAR, Michael
IPC分类号： C12P21/00 , C12P21/08 , C07K16/00
摘要： Herein is reported a method for producing an antibody comprising the steps of forming an antibody-antibody light chain affinity ligand complex, wherein the antibody light chain affinity ligand is immobilized on a solid phase, by applying a solution comprising the antibody to the immobilized antibody light chain affinity ligand, and incubating the complex formed in the previous step with one or more enzymes to modify the glycosylation of the antibody, thereby producing the antibody.

6. 发明申请

WO2018114878A1 RE-USE OF ENZYMES IN IN VITRO GLYCOENGINEERING OF ANTIBODIES 审中-公开
公开(公告)号：WO2018114878A1
公开(公告)日：2018-06-28
申请号：PCT/EP2017/083430
申请日：2017-12-19
申请人： F. HOFFMANN-LA ROCHE AG , HOFFMANN-LA ROCHE INC.
发明人： FALKENSTEIN, Roberto , MALIK, Sebastian , SCHMID, Ingrid , THOMANN, Marco , VON ROMAN, Matthias Freiherr , WALCH, Heiko
IPC分类号： C12P21/08 , C07K17/00
摘要： Herein is reported a method for the enzymatic preparation/production of an antibody with a modified glycosylation in the Fc-region comprises the steps of incubating an antibody that has a glycosylation in the Fc-region with one or more enzymes for a time sufficient and under conditions suitable to modify the glycosylation of the Fc-region to a defined form, separating in one or more chromatography steps the antibody with a modified glycosylation in the Fc-region from the one or more enzymes and thereby producing the antibody with a modified glycosylation in the Fc-region and one or more recycled enzymes, and repeating the incubating step with the one or more recycled enzymes at least once.

7. 发明申请

WO2016037947A1 GALACTOENGINEERED IMMUNOGLOBULIN 1 ANTIBODIES 审中-公开
公开(公告)号：WO2016037947A1
公开(公告)日：2016-03-17
申请号：PCT/EP2015/070285
申请日：2015-09-04
申请人： F. HOFFMANN-LA ROCHE AG , HOFFMANN-LA ROCHE INC. , GENENTECH, INC.
发明人： MALIK, Sebastian , REUSCH, Dietmar , SCHNUERIGER, Alfred , TEJADA, Max L.
IPC分类号： C07K16/32 , A61P35/00
CPC分类号： C07K16/32 , C07K2317/24 , C07K2317/41 , C07K2317/52 , C07K2317/732 , C07K2317/92 , C12P21/005
摘要： The present invention relates to galactoengineered recombinant antibodies of IgG1 isotype, methods for the production of said antibodies and uses thereof.
摘要翻译：本发明涉及IgG1同种型的半乳糖工程重组抗体，生产所述抗体的方法及其用途。

8. 发明申请

WO2018114879A1 METHOD FOR IN VITRO GLYCOENGINEERING OF ANTIBODIES 审中-公开
公开(公告)号：WO2018114879A1
公开(公告)日：2018-06-28
申请号：PCT/EP2017/083431
申请日：2017-12-19
申请人： F. HOFFMANN-LA ROCHE AG , HOFFMANN-LA ROCHE INC.
发明人： DAMS, Thomas , FALKENSTEIN, Roberto , MALIK, Sebastian , SCHMID, Ingrid , THOMANN, Marco , VON ROMAN, Matthias Freiherr , WALCH, Heiko
IPC分类号： C12P21/08 , C07K16/00
摘要： Herein is reported a method for the enzymatic production of an antibody with a modified glycosylation in the Fc-region comprising the steps of incubating the antibody light chain affinity ligand-bound monoclonal antibody with a glycosylation in the Fc-region with a first enzyme for a time sufficient and under conditions suitable to modify the glycosylation of the Fc-region, recovering the antibody from the antibody light chain affinity ligand, incubating the recovered antibody in solution with a second enzyme for a time sufficient and under conditions suitable to modify the glycosylation of the Fc-region to a defined form, separating the antibody with the modified glycosylation in the Fc-region from the second enzyme in a cation exchange chromatography, and thereby producing the antibody with a modified glycosylation in the Fc-region.

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