Glykos Finland Oy

Sk Innovation Co., Ltd.

Novartis International Pharmaceutical, Ltd.

Vtt Technical Research Centre of Finland Ltd

Anne Huuskonen

Markku Saloheimo

Anne Kanerva

Ann Westerholm-Parvinen

Christopher Landowski

Jari Natunen

Juhani Saarinen

Jukka Hiltunen

Noora Salovuori

Merja Elisa Penttila

Merja Penttilä

Anna-Liisa Hänninen

Sang Min Lee

Laura Ruohonen

Outi Koivistoinen

Merja Oja

Benjamin Patrick Sommer

Ramon Wahl

Christian Ostermeier

Heli Viskari

Jae Hoon Jo

Bernhard Helk

Annamari Heiskanen

Marja Ilmén

Hanna Salo

Simon MoonGeun Jung

Anne Leppänen

Heidi Salminen

Georg Schmidt

Eero Mustalahti

Marja Iimen

Simon Moon Geun Jung

Jussi Joensuu

The present disclosure relates to compositions and methods useful for the production of heterologous proteins in filamentous fungal cells.

Protease deficient filamentous fungal cells and methods of use thereof

Provided are a novel isoprene synthase derived from sweet potato and a method of preparing isoprene using the same, and more specifically, a novel isoprene synthase derived from sweet potato, a gene encoding the isoprene synthase, a host cell transformed with the gene, and a method of preparing isoprene using the same. The isoprene synthase of the present invention may have higher isoprene productivity as compared to isoprene synthases known in the related art to thereby be effectively used in isoprene biosynthesis and preparation of an isoprene polymer using the same.

Isoprene synthase and method of preparing isoprene using thereof

Multiple proteases deficient filamentous fungal cells and methods of use thereof

The present disclosure relates to compositions and methods useful for the production of heterologous proteins with reduced O-mannosylation in filamentous fungal cells, such ascells. More specifically, the invention provides a PMT-deficient filamentous fungal cell comprising a) at least a first mutation that reduces an endogenous protease activity compared to a parental filamentous fungal cell which does not have said first mutation, and, b) at least a second mutation in a PMT gene that reduces endogenous O-mannosyltransferase activity compared to a parental filamentous fungal cell which does not have said second mutation, wherein said filamentous fungal cell is selected from the group consisting oforcell.

O-mannosyltransferase deficient filamentous fungal cells and methods of use thereof

Multiple protease deficient filamentous fungal cells and methods of use thereof

The present disclosure relates to compositions and methods useful for the production of recombinant glycoproteins in filamentous fungal cells, such ascells, wherein at least 90% (mol %), preferably at least 95% of the total neutral N-glycans of said produced recombinant glycoprotein are mammalian-like N-glycans. More specifically, the invention provides a filamentous fungal cell comprising i. one or more mutations that reduces or eliminates one or more endogenous protease activity compared to a parental filamentous fungal cell which does not have said mutation(s); ii. a polynucleotide encoding a heterologous catalytic subunit of oligosaccharyl transferase; iii. a recombinant polynucleotide for increasing &#x3b1;1, 2 mannosidase activity;and, iv. a recombinant polynucleotide encoding said heterologous glycoprotein.

Production of glycoproteins with mammalian-like N-glycans in filamentous fungi

Described herein are compositions including filamentous fungal cells, such asfungal cells, having reduced protease activity and expressing fucosylation pathway. Further described herein are methods for producing a glycoprotein having fucosylated N-glycan, using genetically modified filamentous fungal cells, for example,fungal cells, as the expression system.

Production of fucosylated glycoproteins

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.

Fusion enzymes

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Helsinki, Finland

Anne Huuskonen