Repligen Corporation

Algis Anilionis

John L Palmer

Donald A Colbert

Daniel P Witt

The gene coding for a protein A-like material has been successfully cloned and expressed for the first time. The cloning of this gene with its nucleotide sequence characterization, also disclosed, enables those skilled in the art to obtain quantities of a protein A-like material nucleotide sequence for cloning in various host-vector systems. Protein A is well known as a valuable component of a variety of diagnostic test systems. The protein A-like material of the subject invention, and subfragments thereof, have the protein A properties of binding to IgG at the Fc region and activation of polyclonal antibody synthesis. Thus, these entities are useful in the same manner as protein A.

Cloned genes encoding recombinant protein A

The subject invention is directed to a novel Bacillus thuringiensis kurstaki .delta.-endotoxin prepared by use of a novel hybrid gene. This gene is cloned into a novel plasmid which is transformed into a prokaryotic host. The .delta.-endotoxin of the subject invention is active against Lepidoptera larvae.

Activated Bacillus thuringienses delta-endotoxin produced by an

A novel highly effective prokaryotic expression system is exemplified specifically by being used to produce the useful enzyme .beta.-glucuronidase (BG). This system uses a hybrid plasmid comprising BG gene promoter DNA. The level of expression of BG by an E. coli K-12 derivative host is in the 50% of total cellular protein range. The invention expression system also can be used to express other useful proteins, as disclosed herein.

Efficient prokaryotic expression system

Hybrid useful proteins are prepared by a novel biological system comprising a prokaryotic host transformed with novel hybrid plasmids' .beta.-glucuronidase (BG) gene DNZ and the desired protein gene DNA. Specifically exemplified are plasmids which comprise BG gene DNA and protein A DNA. E. coli K-12 derivative hosts transformed with plasmid pBG3-2.DELTA.n express &gt;60% of the desired fusion protein having protein A-like biological activity. Other useful proteins can be expressed via the elegant highly efficient expression system of the subject invention.

Hybrid proteins produced by an ultrahigh prokaryotic expression

A novel highly effective prokaryotic expression system is exemplified specifically by being used to produce the useful enzyme .beta.-glucuronidase (BG). This system uses a hybrid plasmid comprising BG gene promotor DNA. The level of expression of BG by an E. coli K-12 derivative host is in the 50% of total cellular protein range. The invention expression system also can be used to express other useful proteins, as disclosed herein.

Efficient prokaryotic expression system using portions of the E. coli .beta

Hybrid useful proteins are prepared by a novel biological system comprising a prokaryotic host transformed with novel hybrid plasmids' .beta.-glucuronidase (BG) gene DNA and the desired protein gene DNA. Specifically exemplified are plasmids which comprise BG gene DNA and protein A DNA. E. coli K-12 derivative hosts transformed with plasmid pBG3-2.DELTA.N express &gt;60% of the desired fusion protein having protein A-like biological activity. Other useful proteins can be expressed via the elegant highly efficient expression system of the subject invention.

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Arlington, MA, United States of America

Algis Anilionis