| abstract |
Methods for producing proteins and glycoproteins are described in Pichia pastoris that lack detectable entanglement activity with antibodies produced against host cell antigens; in particular, methods are described where recombinant Pichia pastoris strains that do not exhibit an ß-mannosyltransferase 2 activity with respect to an N-glucan or O-glucan, and that do not exhibit at least one activity selected from a ß activity -manosyltransferase 1, 3 and 4, produce recombinant proteins and glycoproteins; These recombinant Pichia pastoris strains can produce proteins and glycoproteins that lack detectable a-mannosidase-resistant β-mannose residues therein and, thus, lack interlacing activity with antibodies produced against host cell antigens; Methods for producing bi-sialylated human erythropoietin in Pichia pastoris that lack detectable entanglement activity with antibodies produced against host cell antigens are further described. |