Abstract: The present invention relates to novel genes from S. aureus and the polypeptides they encode. Also provided as are vectors, host cells, antibodies and recombinant methods for producing the same. The invention further relates to screening methods for identifying agonists and antagonists of S. aureus polypeptide activity. The invention additionally relates to diagnostic methods for detecting Staphylococcus nucleic acids, polypeptides and antibodies in a biological sample. The present invention further relates to novel vaccines for the prevention or attenuation of infection by Staphylococcus.

Abstract: Pancreatic carboxypeptidase B or an isoform or a mutein of carboxypeptidase B may be prepared by (a) expressing a natural or unnatural enzymatically inactive precursor form of carboxypeptidase B in a microorganism by secretion, (b) purifying the precursor form expressed by secretion, and (c) converting the purified precursor form into the active form by an enzymatic treatment. A nucleic acid construct and a host cell containing the construct are useful for preparing pancreatic carboxypeptidase B or an isoform or a mutein thereof by this method.

Abstract: Disclosed are novel synthetically-modified B. thuringiensis chimeric crystal proteins having improved insecticidal activity against coleopteran, dipteran and lepidopteran insects. Also disclosed are the nucleic acid segments encoding these novel peptides. Methods of making and using these genes and proteins are disclosed as well as methods for the recombinant expression, and transformation of suitable host cells. Transformed host cells and transgenic plants expressing the modified endotoxin are also aspects of the invention.

Abstract: A process for production of an alkaline tolerant dextranase enzyme comprises culturing a dextran-producing microorganism Streptomyces anulatus having accession no. ATCC PTA-3866 to produce an alkaline tolerant dextranase, Dex 1 wherein the protein in said enzyme is characterized by a MW of 63.3 kDa and Dex 2 wherein its protein is characterized by a MW of 81.8 kDa.

Abstract: The present invention relates to mutations of the subtilisin gene, some of which result in changes in the chemical characteristics of subtilisin enzyme. Mutations are created at specific nucleic acids of the subtilisin gene and, in various specific embodiments, the mutant enzymes possess altered chemical properties including, but not limited to, increased stability to oxidation, augmented proteolytic activity, and improved washability. The present invention also relates, but is not limited to, the amino acid and DNA sequences for two proteases derived from Bacillus lentus variants, subtilisin 147 and subtilisin 309, as well as mutations of these genes and the corresponding mutant enzymes.

Abstract: Novel protease variants derived from the DNA sequences of naturally-occurring or recombinant non-human proteases are disclosed. The variant proteases, in general, are obtained by in vitro modification of a precursor DNA sequence encoding the naturally-occurring or recombinant protease to generate the substitution of a plurality of amino acid residues in the amino acid sequence of a precursor protease. Such variant proteases have properties which are different from those of the precursor protease, such as altered wash performance. The substituted amino acid residue correspond to positions 62, 212, 230, 232, 252 and 257 of Bacillus amyloliquefaciens subtilisin.

Abstract: A nucleic acid sequence required for regulating the autolytic activity of bacteria is provided. Also provided are polypeptides encoded by the gene or mutant gene as well as vector and host cells for expressing these polypeptides. Methods for identifying and using agents which interact with the gene or mutant gene or polypeptides encoded thereby to inhibit bacterial growth and infectivity are also provided.

Abstract: Methods for the production of purified, catalytically active, recombinant memapsin 2 have been developed. The substrate and subsite specificity of the catalytically active enzyme have been determined. The substrate and subsite specificity information was used to design substrate analogs of the natural memapsin 2 substrate that can inhibit the function of memapsin 2. The substrate analogs are based on peptide sequences, shown to be related to the natural peptide substrates for memapsin 2. The substrate analogs contain at least one analog of an amide bond which is not capable of being cleaved by memapsin 2. Processes for the synthesis of two substrate analogues including isosteres at the sites of the critical amino acid residues were developed and the substrate analogues, OMR99-1 and OM99-2, were synthesized. OM99-2 is based on an octapeptide Glu-Val-Asn-Leu-Ala-Ala-Glu-Phe (SEQ ID NO:28) with the Leu-Ala peptide bond substituted by a transition-state isostere hydroxyethylene group (FIG. 1).

Abstract: A polypeptide with the properties of collagenase class I from Clostridium histolyticum (CHC I) and the amino acid sequence SEQ ID NO:2 which is optionally N-terminally extended by one or several amino acids of the sequence SEQ ID NO:3 is advantageously suitable for the isolation of cells from mammalian tissue and human tissue.

Abstract: Antimicrobial compounds and compositions and uses thereof, including the treatment and prevention of bacterial infections are described. The compounds and compositions include lantibiotic polypeptides and the nucleic acid sequences encoding the polypeptides. The compounds and compositions are useful as antimicrobials in antibiotic pharmaceutical preparation and as an antimicrobial or antiseptic dentifrice.

Abstract: Disclosed is a pO157 plasmid-specified polypeptide found in E. coli EDL933 and other enterohemorrhagic E. coli that binds to and cleaves C1-esterase inhibitor. Also disclosed are methods employing the polypeptide for diagnosing and treating colitis or hemolytic uremic syndrome, and methods of detecting potential therapeutics.

Abstract: Bacillus sp. NTAP-1 having been deposited under accession number FERM BP-6926; and a collagen-decomposing enzyme produced by bacterium. The above enzyme (1) has a capability of hydrolyzing, at the highest efficiency, collagen and gelatin from among casein, gelatin, albumin and collagen; (2) shows the optimum pH of 3.5 to 4.5; (3) shows the optimum temperature of 65 to 70° C.; (4) after heating at 60° C. at pH 6.0 for 4 hours, sustains an activity amounting to 60% or more of the level before the heat treatment; (5) remains stable at pH 3 to 6; and a molecular weight of approximately 46,000 when measured by SDS-PAGE.

Abstract: Novel carbonyl hydrolase mutants derived from the amino acid sequence of naturally-occurring or recombinant non-human carbonyl hydrolases and DNA sequences encoding the same. The mutant carbonyl hydrolases, in general, are obtained by in vitro modification of a precursor DNA sequence encoding the naturally-occurring or recombinant carbonyl hydrolase to encode the substitution, insertion or deletion of one or more amino acids in the amino acid sequence of a precursor carbonyl hydrolase. Such mutants have one or more properties which are different than the same property of the precursor hydrolase.

Abstract: The present invention relates to polypeptides with reduced immune response including reduced allergenicity having one or more amino acid residues being substituted with other amino acid residues and/or having coupled one or more polymeric molecules in the vicinity of the polypeptides metal binding site, a method for preparing modified polypeptides of the invention, the use of the polypeptide for reducing the immunogenicity and allergenicity and compositions comprising the polypeptide.

Abstract: The invention provides a method of producing a polypeptide having a C-terminal &agr;-carboxamide group. It particularly concerns an enzymatic modification of selected substrate polypeptides which result in cleavage of the substrate polypeptide to form a product peptide with a C-terminal arginine residue having an &agr;-carboxamide group (C-terminal “Arg-NH2”). The method includes contacting an aqueous-based solution including (i) ammonia reagent and (ii) the substrate polypeptide with (iii) clostripain.

Abstract: An antigenic preparation is provided containing an outer membrane protein associated with pathogenic strains of Leptospira. The protein has been designated ALipL32″ for Alipoprotein from Leptospira≅ and because the isolated polypeptide migrates to a position corresponding to a molecular weight of 32 kD in a denaturing polyacrylamide gel. The invention provides polynucleotides encoding LipL32 and antibodies that bind the protein which are useful in the diagnosis of leptospirosis. In addition, LipL32 can be used immunologically as a vaccine for spirochete-associated pathologies.

Abstract: The present invention relates to a novel strain of alkalothermophilic Bacillus sp. isolated from a hot spring at Vajeshwari, District Thane, The State of Maharashtra, India and deposited at American Type Culture Centre (ATCC), bearing accession No. PTA 972, said strain of Bacillus sp. having the following characteristics (i) aerobic, (ii) gram positive, (iii) motile, (iv) spore forming, (v) capable of growing in a alkaline medium at pH 8-10, and (vi) exhibiting negative reaction towards production of indole, hydrogen, sulfide, ammonia and urease and positive reaction for hydrolysis of starch, production of catalase, hydrolysis of casein and reduction of nitrate.

Abstract: The invention provides clpL polypeptides and DNA (RNA) encoding clpL polypeptides and methods for producing such polypeptides by recombinant techniques. Also provided are methods for utilizing polypeptides to screen for antibacterial compounds.

Abstract: A hybrid botulinal neurotoxin is disclosed. In one embodiment, the neurotoxin comprises a combination of a botulinal neurotoxin heavy chain and light chain, wherein the light chain and heavy chain are not of the same serotype and wherein the heavy and light chains are linked by a homobifunctional sulfydryl linker. A method for creating hybrid neurotoxins comprised of different functional domains is also disclosed.

Abstract: The present invention relates to a novel ppGpp synthetase and expression systems for improved production of proteins of interest in Gram-positive bacteria, involving use of the novel ppGpp synthetase.

Abstract: Large amounts of hairs and feathers can be decomposed and refined by treatment in an oxygen-containing gas stream with a fungus that can decompose hairs and feathers. The resulting decomposed and refined hairs and feathers are useful as a fertilizer.

Abstract: The invention provides pth polypeptides and polynucleotides encoding pth polypeptides and methods for producing such polypeptides by recombinant techniques. Also provided are methods for utilizing pth polypeptides to screen for antibacterial compounds.

Abstract: An S. aureus peptide deformylase iron complex composition, a method of isolating the composition, and a method of using the composition to screen for compounds that interact with a peptide deformylase are provided. The composition of the invention retains greater than about 95% of its catalytic deformylase activity after being stored at a protein concentration of greater than about 10 mg/ml in 50% glycerol at −20° C. for six months.

Abstract: The invention provides 1icD1 polypeptides and polynucleotides encoding 1icD1 polypeptides and methods for producing such polypeptides by recombinant techniques. Also provided are methods for utilizing licD1 polypeptides to screen for antibacterial compounds.

Abstract: The invention provides metK polypeptides and polynucleotides encoding metK polypeptides and methods for producing such polypeptides by recombinant techniques. Also provided are methods for utilizing metK polypeptides to screen for antibacterial compounds.

Abstract: A method for treating various diseases and conditions that are dependent on activated &agr;2 macroglobulin in the blood and extravascular tissue is disclosed. The method comprises orally administering a therapeutically effective amount of protease to a mammal to increase the amount of activated &agr;2 macroglobulin, which in turn enhances the clearance of TNF-&agr;, leptin, and &bgr;-amyloid while enhancing delivery of TGF-&bgr;. The protease may be any pharmaceutically acceptable protease, and preferably is of microbial and/or plant origin, given singly or in combination with vitamins, minerals, antioxidants, bioflavonoids, proanthocyanidins, herbs, herbal extracts, plant and animal concentrates, and non-prescription analgesics. The microbial protease is preferably administered in a total daily dosage of at least 100,000 HUT (or equivalent biological activity). The plant protease component is preferably administered in a total daily dosage of at least 50,000 PU (or equivalent biological activity).

Abstract: The present invention relates to a method of producing novel improved protein mutant which produce low allergenic response in humans compared to the parent of that mutant. Specifically, the present invention comprises neutralizing or reducing the allergenicity of a protein by introducing therein as replacement or modification of an epitope on such protein a sequence from human subtilisin.

Abstract: An adherence factor comprises a cell wall associated adhesin derived from Lactobacillus or a derivative, fragment, precursor or mutant of the adhesin, the adherence factor mediating adherence to epithelial cells and modulating gene expression to improve gut barrier function and gastrointestinal tract homeostasis.

Abstract: Novel synthetic leader peptides have been identified. The leader peptides have use in a method of enhancing the secretion of a recombinant polypeptide produced in a host cell. Polynucleotides encoding the novel leader peptides and a method of designing the polynucleotides are described.

Abstract: Mutant Bacillus lentus DSM 5483 proteases are derived by the replacement of at least one amino acid residue of the mature form of the B. lentus DSM 5483 alkaline protease. The mutant proteases are expressed by genes which are mutated by site-specific mutagenesis. The amino acid sites selected for replacement are identified by means of a computer based method which compares the three dimensional structure of the wild-type protease and a reference protease.

Abstract: This invention provides methods for practical in vitro sialylation of glycoproteins, including recombinantly produced glycoproteins. The methods are useful for large-scale modification of sialylation patterns.

Abstract: DNA encoding a therapeutically suitable glutaminase has been molecularly cloned. This allows one to obtain a polypeptide which is a therapeutically suitable glutaminase free of contaminating endotoxin. It has been found that this polypeptide is a potent anti-viral agent and when coupled to an anti-tumor monoclonal antibody is a potent anticancer agent. The glutaminase of the present invention is particularly useful for treating lung, breast and colon cancer cells and in the treatment of HIV-infected cells.

Abstract: An alkaline protease having the following properties; a gene encoding the same; a microorganism producing the same; and washing compositions containing the same; (i) acting over a broad pH value range of 4 to 13 and achieving, at pH 6 to 12, 80% or more the activity at the optimum pH value; (ii) when treated at 40° C. for 30 minutes, being stable over a pH value range of 6 to 11; (iii) having an isoelectric point of about 8.9 to 9.1; and (iv) having casein digesting activity that is not inhibited by oleic acid. The alkaline protease of the present invention is highly stable to various surface active agents and fatty acids, and exhibits high stability to oxidizing agents, and is therefore useful as an enzyme to be used in detergents for automatic dishwashers and laundry detergents, both containing bleaching components.

Abstract: Methods for the identification, production and use of staphylokinase derivatives characterized by a reduced immunogenicity after administration in patients. The derivatives of the invention are obtained by preparing a DNA fragment comprising at least the part of the coding sequence of staphylokinase that provides for its biological activity; performing in vitro site-directed mutagenesis on the DNA fragment to replace one or more codons for wild-type amino acids by a codon for another amino acid; cloning the mutated DNA fragment in a suitable vector; transforming or transfecting a suitable host cell with the vector; culturing the host cell under conditions suitable for expressing the DNA fragment; and purifying the expressed staphylokinase derivative to homogeneity. Preferably the DNA fragment is a 453 bp EcoRI-HindIII fragment of the plasmid pMEX602sakB, (pMEX.

Abstract: The invention relates to detergents characterized in that they contain &agr;-amylase from Bacillus amyloliquefaciens and protease from Bacillus lentus, optionally modified by genetic engineering, in addition to our usual ingredients compatible with said enzymes.

Abstract: A hyperthermostable protease having the amino acid sequence represented by the SEQ ID NO:1 of the Sequence Listing or a sequence derived therefrom by deletion, substitution, insertion or addition of one to several amino acid residues, a gene encoding the hyperthermostable protease, and a process for preparing the protease, aiming at providing by genetic engineering techniques a hyperthermophile protease which is advantageous for industrial use.

Abstract: The invention provides isolated nucleic acid compounds encoding FtsZ of Streptococcus pneumoniae. Also provided are vectors and transformed host cells for expressing the encoded protein, and a method for identifying compounds that bind and/or inhibit said protein.

Abstract: A purified thermostable enzyme is derived from the archael bacterium AEPII1a. The enzyme has a molecular weight of about 60.9 kilodaltons and has cellulase activity. The enzyme can be produced from native or recombinant host cells and can be used to aid in the digestion of cellulose where desired.

Abstract: The present invention features the use of PorB polypeptide as a therapeutic agent. In specific embodiment the invention features a chlamydial vaccine based on a PorB polypeptide, as well as methods for induction of a protective immune response against infection by Chlamydia and Chlamydiophila. The invention further features methods for identifying agents that offset PorB function (e.g., in transport of &agr;-ketoglutarate and which are effective as anti-chlamydial chemotherapeutic agents.

Abstract: Novel protease variants derived from the DNA sequences of naturally-occurring or recombinant non-human proteases are disclosed. The variant proteases, in general, are obtained by in vitro modification of a precursor DNA sequence encoding the naturally-occurring or recombinant protease to generate the substitution of a plurality of amino acid residues in the amino acid sequence of a precursor protease. Such variant proteases have properties which are different from those of the precursor protease, such as altered wash performance.

Abstract: The DegP (HtrA) protease is a multifunctional protein essential for the removal of misfolded and aggregated proteins in the periplasm. The present invention provides an assay for inhibitors of DegP activity, comprising mixing a suspected inhibitor of DegP activity with DegP and a suitable substrate (preferably a native substrate of DegP such as PapA) and detecting changes in DegP activity. DegP has been shown to be essential for virulence in several Gram negative pathogens. Only three natural targets for DegP have been described: colicin A lysis protein (Cal), pilin subunits (K88, K99, Pap) and recently HMW1 and HMW2 from Hemophilus influenzae. In vitro, DegP has shown weak protease activity on casein and several other non-native substrates. The present inventors have identified the major pilin subunit of the Pap pilus, PapA, as a native DegP substrate and demonstrated binding and proteolysis of this substrate in vitro.

Abstract: The present invention relates to enzymes produced by mutating the genes for a number of subtilases and expressing the mutated genes in suitable hosts are presented. The enzymes exhibit improved autoproteolytic stability in comparison to their wild type parent enzymes.

Abstract: The invention provides tarF polypeptides and DNA (RNA) encoding tarF polypeptides and methods for producing such polypeptides by recombinant techniques. Also provided are methods for utilizing tarF polypeptides to screen for antibacterial compounds.

Abstract: The invention provides ampS polypeptides and DNA (RNA) encoding ampS polypeptides and methods for producing such polypeptides by recombinant techniques. Also provided are methods for utilizing ampS polypeptides to screen for antibacterial compounds.

Abstract: The present invention provides novel aerobic, Gram-positive alkaliphilic bacteria which have been isolated from in and around alkaline soda lakes. These alkaliphiles have been analyzed according to the principles of numerical taxonomy with respect to each other and also to a collection of known bacteria. In addition, these bacterial taxa are further circumscribed by an analysis of the lipid components which serve as chemotaxonomic markers. The alkaliphiles of the present invention produce alkalitolerant enzymes which are capable of performing their functions at high pH which makes them uniquely suited for applications requiring such extreme conditions.

Abstract: The present invention relates to a method for screening chemically modified mutant enzymes for amidase and/or esterase activity. This method includes providing a chemically modified mutant enzyme with one or more amino acid residues from an enzyme being replaced by cysteine residues, where at least some of the cysteine residues are modified by replacing thiol hydrogen in the cysteine residues with a thiol side chain, contacting the chemically modified mutant enzyme with a substrate for an amidase and/or a substrate for an esterase, and determining whether the chemically modified mutant enzyme exhibits amidase and/or esterase activity. The present invention also relates to chemically modified mutant enzymes and a method of producing them where one or more amino acid residues from an enzyme are replaced by cysteine residues, and the cysteine residues are modified by replacing at least some of the thiol hydrogen in the cysteine residue with a thiol side chain to form the chemically modified mutant enzyme.

Abstract: An isolated DNA encoding a class I collagenase, particularly, the isolated DNA encoding the class I collagenase from Clostridium histolyticum, a vector containing the gene, a transformant containing the vector, a class I collagenase, and a method of preparing the class I collagenase are disclosed.

Abstract: Provided herein is a nucleotide sequence encoding an Arg-specific gingipain, said Arg-gingipain characterized as having an apparent molecular mass of 50 kDa as estimated by sodium dodecyl sulfate polyacrylamide gel electrophoresis and an apparent molecular mass of 44 kDa as estimated by gel filtration chromatography, said gingipain-1 having amidolytic and proteolytic activity for cleavage after arginine residues and having no amidolytic and/or proteolytic activity for cleavage after lysine residues, wherein the amidolytic and/or proteolytic activity is inhibited by cysteine protease group-specific inhibitors including iodoacetamide, iodoacetic acid, N-ethylmaleimide, leupeptin, antipain, trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane, TLCK, TPCK, p-aminobenzamidine, N-chlorosuccinamide, and chelating agents including EDTA and EGTA, wherein the amidolytic and/or proteolytic activity of said gingipain-1 is not sensitive to inhibition by human cystatin C, &agr;2-macroglobulin, &agr;1-proteinase inhibitor,

Abstract: New proteolytic enzymes are provided exhibiting improved properties for application in detergents, especially laundry detergents. These enzymes are obtained by expression of a gene encoding a proteolytic enzyme having an amino acid sequence which differs at least in one amino acid from the wild type enzyme. Preferred enzymes are certain mutants derived from the serine protease of Bacillus nov. spec. PB92.

Abstract: There are provided hyperthermostable proteases having an amino acid sequences represented by SEQ ID Nos. 1, 3 and 5 of the Sequence Listing or functional equivalents thereof and hyperthermostable protease genes encoding those hyperthermostable protease. There is also disclosed a process for preparation of a hyperthermostable protease by culturing a transformant containing the gene.