Methods of modulating the properties of a cell culture expressing a protein of interest are provided. In various embodiments the methods relate to the overexpression of proteins involved in the N-glycosylation pathway.

The present invention provides cell lines deficient in mannosyl (alpha-1,3-)-glycoprotein beta-1,2-N-acetylglucosaminyltransferase I (Mgat1). Also provided are methods for producing the Mga1 deficient cell lines and methods for using the Mgat1 deficient cell lines for the production of recombinant proteins having simple glycoforms.

The present disclosure relates to a nucleic acid construct having a chimeric nucleic acid molecule encoding a tripartite glycosyltransferase fusion protein. The chimeric nucleic acid molecule includes a first nucleic acid moiety encoding an amphipathic shield domain protein; a second nucleic acid moiety encoding a glycosyltransferase; and a third nucleic acid moiety encoding a water soluble expression decoy protein. The first nucleic acid moiety is coupled to the second nucleic acid moiety's 3 end and the third nucleic acid moiety is coupled to the second nucleic acid moiety's 5 end. The coupling may be direct or indirect. The present disclosure further relates to an expression vector, a host cell, and a tripartite glycosyltransferase fusion protein encoded by the nucleic acid construct. Also disclosed are methods of recombinantly producing a tripartite glycosyltransferase fusion protein in soluble form and methods of cell-free glycan remodeling.

The present invention relates to processes for producing industrial products such as hydrocarbon products from non-polar lipids in a vegetative plant part. Preferred industrial products include alkyl esters which may be blended with petroleum based fuels.

The present disclosure relates to recombinant proteins having N-acetylglucosaminyltransferase activity. The present disclosure further relates to methods for producing complex N-glycans including the steps of providing host cells containing such recombinant proteins and culturing the host cells such that the recombinant proteins are expressed.

The present invention relates to a cell-free enzyme-catalyzed process for producing glycoproteins of general formula (I) from a lipid-linked oligosaccharide and a peptide. Further, said process includes the construction of the lipid-linked oligosaccharide from a mannose trisaccharide containing core structure. Particularly, the lipid-linked oligosaccharide is a high mannose-, complex-, or hybrid-type N-glycan.

The present disclosure reports that a calcium-dependent serine protease, complement component is (C1s) has been identified as a protease responsive for cleavage of exogenous polypeptides expressed in mammalian cell lines such as CHO cells. These CHO cell lines provide for increased yield of antigenically correct, uncleaved exogenous polypeptide as compared to unmodified CHO cells expressing the active C1s protease. C1s-deficient cell lines and methods for use of same for producing exogenous polypeptides, e.g., human immunodeficiency virus (HIV) envelope glycoprotein polypeptides, such as, gp120 or human Factor VIII are provided.

A method for producing a modified cell deficient in mannosyl (alpha-1,3-)-glycoprotein beta-1,2-N-acetylglucosaminyltransferase 1 (MGAT1) activity. Also provided is a CHO cell line deficient in MGAT1 activity produced by the method. Further disclosed are methods for producing a glycoprotein.