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10.1073/pnas.1718172115 http://scihub22266oqcxt.onion/10.1073/pnas.1718172115 C5789950!5789950 !29311294     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=29311294 &cmd=llinks): Failed to open stream: HTTP request failed! 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Glycoengineering of antibody (Herceptin) through yeast expression and in vitro enzymatic glycosylation |pdf=|usr=}}{{29311294 }} gab.com Text Glycoengineering of antibody (Herceptin) through yeast expression and in vitro enzymatic glycosylation JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=29311294 #FOAvip Monoclonal antibodies (mAbs) have been developed as therapeutics, especially for the treatment of cancer, inflammation, and infectious diseases. Because the glycosylation of mAbs in the Fc region influences their interaction with effector cells that kill antibody-targeted cells, and the current method of antibody production is relatively expensive, efforts have been directed toward the development of alternative expressing systems capable of large-scale production of mAbs with desirable glycoforms. In this study, we demonstrate that the mAb trastuzumab expressed in glycoengineered P. pastoris can be remodeled through deglycosylation by endoglycosidases identified from the Carbohydrate Active Enzymes database and through transglycosylation using glycans with a stable leaving group to generate a homogeneous antibody designed to optimize the effector functions. The 10 newly identified recombinant bacterial endoglycosidases are complementary to existing endoglycosidases (EndoA, EndoH, EndoS), two of which can even accept sialylated tri- and tetraantennary glycans as substrates. Twit Text FOAVip Glycoengineering of antibody (Herceptin) through yeast expression and in vitro enzymatic glycosylation ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=29311294 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29311294 #FOAvip English Wikipedia <ref>{{Cite pmid|29311294 }}</ref> Glycoengineering of antibody (Herceptin) through yeast expression and in vitro enzymatic glycosylation #MMPMID29311294 Liu CP ; Tsai TI ; Cheng T ; Shivatare VS ; Wu CY ; Wu CY ; Wong CH Proc Natl Acad Sci U S A 2018[Jan]; 115 (4 ): 720-725 PMID29311294 show ga Monoclonal antibodies (mAbs) have been developed as therapeutics, especially for the treatment of cancer, inflammation, and infectious diseases. Because the glycosylation of mAbs in the Fc region influences their interaction with effector cells that kill antibody-targeted cells, and the current method of antibody production is relatively expensive, efforts have been directed toward the development of alternative expressing systems capable of large-scale production of mAbs with desirable glycoforms. In this study, we demonstrate that the mAb trastuzumab expressed in glycoengineered P. pastoris can be remodeled through deglycosylation by endoglycosidases identified from the Carbohydrate Active Enzymes database and through transglycosylation using glycans with a stable leaving group to generate a homogeneous antibody designed to optimize the effector functions. The 10 newly identified recombinant bacterial endoglycosidases are complementary to existing endoglycosidases (EndoA, EndoH, EndoS), two of which can even accept sialylated tri- and tetraantennary glycans as substrates. |Antibodies, Monoclonal/metabolism [MESH] |Antibody-Dependent Cell Cytotoxicity/physiology [MESH] |Glycoproteins/metabolism/*pharmacology [MESH] |Glycoside Hydrolases/*metabolism/pharmacology [MESH] |Glycosylation [MESH] |Humans [MESH] |Pichia/metabolism [MESH] |Polysaccharides/metabolism [MESH] |Saccharomyces cerevisiae/metabolism [MESH]Glycoengineering of antibody (Herceptin) through yeast expression and (epmc).pdf DeepDyve Pubget Overpricing