Boston Medical Center Corporation

Other

Clariant Finance (bvi) Limited

Dsm N.v.

Gist-brocades B.v.

University of Victoria Innovation and Development Corporation

The University Hospital

Micropure Technologies, Inc.

Dsm IP Assets B.v.

Diane P Williams

John R Murphy

Brian E Jones

Wilhelmus J Quax

Sara Iverson

Frits Goedegebuur

Roberta L Farrell

Pieter Van Solingen

Jimmie A Keeton

Margareta Adriana Herweijer

Graham K Farrington

Hugh W Morgan

William Hintz

Peter Leonard Bergquist

McIver Daniel

Simon Forster

Roberta Lee Farrell

Dean Moody

Vidar Gronberg

Rudolf Franciscus Van Beckhoven

Wilhelmina Theresia Herbes

Wilhelmus Antonius Van Der Kleij

Margaretha Adriana Herwijer

Moreland David Gibbs

Paige Anderson

Peter Bergquist

Hugh Morgan

Roy Daniels

Brian Edward Jones

Margaretha Adriana Herweijer

Rudolf FWC Van Beckhoven

A composition and method for reducing the levels of pathogenic bacteria in an aquatic environment. The composition includes isolatedwhich are able to reduce a number of well known pathogenic bacterium from aquatic environments. The preferredis strain RRRL B-30535.

Probiotic composition containing Bacillus cereus RRRL B-30535

The present invention concerns DNA sequences from the maltase/maltose permease genes having transcriptional activity, expression vectors comprising these sequences and their use for the production of proteins.

Kluyveromyces lactis maltase/maltose permease bi-directional promoter and use thereof

Alkalophilic and thermophilic cellulases having high stability to elevated temperatures and pH have been isolated from an organism of unknown species, which most closely resembles those in the Caldicellulosiruptor genus and which has been called by us, Tok7B.1, These cellulases have been cloned and expressed in a recombinant system, so that they can be produced in quantity. These are particularly useful in treating cellulosic materials including cotton-containing fabrics, as detergent additives, and in aqueous compositions. We also provide genomic DNA which can be used in recombinant expression vectors and expression systems to produce enhanced alkali and/or temperature stability properties in cellulases other than those specifically described.

Compositions and methods for treating cellulose containing fabrics using truncated cellulase enzyme compositions

Alkalitolerant xylanases

Thermostable xylanases

A chimeric toxin comprising protein fragments joined together by peptide bonds, the chimeric toxin comprising, in sequential order, beginning at the amino terminal end of the chimeric toxin,

DNA encoding chimeric toxin

A chimeric toxin comprising protein fragments joined together by peptide bonds, the chimeric toxin comprising, in sequential order, beginning at the amino terminal end of the chimeric toxin, (a) the enzymatically active Fragment A of diphtheria toxin, (b) a first fragment including the cleavage domain 1.sub.1 adjacent the Fragment A of diphtheria toxin, (c) a second fragment comprising at least a portion of the hydrophobic transmembrane region of Fragment B of diphtheria toxin, the second fragment having a deletion of at least 50 diphtheria toxin amino acid residues, the deletion being C-terminal to the portion of the transmembrane region, and the second fragment not including domain 1.sub.2, and (d) a third fragment comprising a portion of a cell-specific polypeptide ligand, the portion including at least a portion of the binding domain of the polypeptide ligand, the portion of the binding domain being effective to cause the chimeric toxin to bind selectively to a predetermined class of cells to be attacked by the enzymatically active Fragment A.

Chimeric toxins

A chimeric toxin comprising protein fragments joined together by peptide bonds, the chimeric toxin comprising, in sequential order, beginning at the amino terminal end of the chimeric toxin, (a) the enzymatically active Fragment A of diphtheria toxin, (b) a first fragment including the cleavage domain 1.sub.1 adjacent the Fragment A of diphtheria toxin, (c) a second fragment comprising at least a portion of the hydrophobic transmembrane region of Fragment B of diphtheria toxin, the second fragment having a deletion of at least 50 diphtheria toxin amino acid residues, the deletion being C-terminal to the portion of the transmembrane region, and the second fragment not including domain 1.sub.2, and (d) a third fragment comprising a portion of a cell-specific polypeptide ligand, the portion including at least a portion of the binding domain of the polypeptide ligand, the portion of the binding domain being effective to cause the chimeric toxin to bind selectively to a predetermined class of cells to be attacked by the enzymatically active Fragment A, the chimeric toxin possessing any of, greater toxicity than that of a toxin comprised of DAB.sub.486 fused to the third fragment, a lower K.sub.d for the sites on cells of the predetermined class to which the chimeric toxin binds than that of a toxin comprised of DAB.sub.486 fused to the third fragment, greater resistance to proteolytic degradation than that exhibited by a toxin comprised of DAB.sub.486 fused to the third fragment, greater resistance to the inhibition of its cytotoxicity by the cell-specific polypeptide ligand than that exhibited by DAB.sub.486 fused to the third fragment, the ability to inhibit protein synthesis to a given degree by a period of exposure that is shorter than the period of exposure required by DAB.sub.489 fused to the third fragment to inhibit protein synthesis to the same degree, or the ability to effect a more rapid onset of the inhibition of protein synthesis than that exhibited by DAB.sub.486 fused to the third fragment.

DNA encoding chimeric diphtheria toxins

A chimeric diptheria toxin comprising protein fragments joined together by peptide bonds.

Growing community of inventors

Hopkinton, MA, United States of America

Diane P Williams