Icon Genetics Gmbh

Kentucky Bioprocessing, Inc.

The University of Southampton

Mor, Tsafrir

Frank Thieme

Romy Kandzia

Victor Klimyuk

Stefan Werner

Franziska Jarczowski

Yuri Gleba

Steven D Hume

Greg Pogue

Tsafrir Mor

Ernie Hiatt

Sylvestre Marillonnet

Ernst Weber

Carola Engler

Vesna Blazevic

Natalia Savelyeva

Anja Nickstadt

Maria Malm

Andre Diessner

Duc Bui-Minh

Freda K Stevenson

Warayut Chotprakaikiat

André Diessner

An immunogenic composition comprising at least one Norovirus antigen and at least one adjuvant which is at least one B subunit of an ABtoxin such as cholera toxin subunit B (CTB) or the B subunit of heat-labileexotoxin LT (LTB).

Immunogenic composition and vaccine for generating an immune response to norovirus

A process of producing a recombinant glycoprotein in a plant, in cells of a plant, or in plant cells is provided. The process comprises expressing in said plant, in cells of said plant or in said plant cells a nucleic acid sequence encoding a polypeptide having an N-glycosylation site and co-expressing a nucleic acid sequence encoding a heterologous single-subunit oligosaccharyltransferase.

Method of co-expressing a glycoprotein and a single-subunit olicosaccharyltransferase in a plant

Protein conjugate comprising a protein antigen for generating an immune response against the HER2/neu protein and an immunogenic carrier covalently bonded to said protein antigen, wherein said protein antigen

HER2/Neu cancer vaccine

A new, reliable, easily scalable and reproducible method for the production of recombinant butyrylcholinesterase (rBuChE) is provided. Through the utilization of a plant transfection procedure, various plant strains have been shown to generate effective and scalable amounts of rBuChE under acceptable manufacturing processes to permit reliable levels of such enzymes for desired nerve agent protection requirements (including tetrameric products). As well, such methods in engineered plant lines have shown suitable production of these enzymes in tetramer form with glycan formation and sialylation (for terminal groups) to allow for optimal potency against organophosphorus agent exposure as well as proper immunogenic response within the plant sources. The overall production method, including the transfection and production within mammalian cells, as well as the process steps involved for such a reliable sourcing platform from plants is thus encompassed within the invention.

Plant-based recombinant butyrylcholinesterase production methods

A new, reliable, easily scalable and reproducible method for the production of recombinant butyrylcholinesterase (rBuChE) is provided. Through the utilization of a plant transfection procedure, various plant strains have been shown to generate effective and scalable amounts of rBuChE under acceptable manufacturing processes to permit reliable levels of such enzymes for desired nerve agent protection requirements (including tetrameric products). As well, such methods in engineered plant lines have shown suitable production of these enzymes in tetramer form with glycan formation and sialyalation (for terminal groups) to allow for optimal potency against organophosphorus agent exposure as well as proper immunogenic response within the plant sources. The overall production method, including the transfection and production within mammalian cells, as well as the process steps involved for such a reliable sourcing platform from plants is thus encompassed within the invention.

A process of inserting a nucleic acid sequence of interest into an acceptor nucleic acid is provided. The process comprises amplifying by PCR a DNA comprising in the following order a sequence segment U, a nucleic acid sequence segment of known nucleotide sequence K2, and a nucleic acid sequence segment of known sequence K3. The process further comprises treating the linear double-stranded DNA molecules from the PCR amplification with an exonuclease to obtain a single-stranded overhang at the first end of the DNA and a single-stranded overhang comprising nucleic acid segments K2 and K3 at the second end of the DNA. The process additionally comprises annealing the product of the exonuclease treatment to a linearized double-stranded acceptor nucleic acid which has been designed to complement the single-stranded overhangs of the product of the exonuclease treatment.

Process of clean cloning

Growing community of inventors

Halle, Germany

Frank Thieme