Patents by Inventor Joseph T. Barbieri
Joseph T. Barbieri has filed for patents to protect the following inventions. This listing includes patent applications that are pending as well as patents that have already been granted by the United States Patent and Trademark Office (USPTO).
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Publication number: 20240139332Abstract: Provided herein are engineered non-catalytic, non-toxic tetanus toxin variants and methods of using such engineered tetanus toxin variants as low dose, protective vaccines that are non-toxic and more potent than their respective chemically inactivated toxoids. In addition, provided herein are conjugate vaccine carriers comprising engineered tetanus toxin variants and methods of using such conjugate vaccines to elicit T-cell dependent immune memory responses which can target a broad spectrum of microbial pathogens as a single vaccine.Type: ApplicationFiled: October 3, 2022Publication date: May 2, 2024Inventors: Joseph T. Barbieri, Eric A. Johnson, Sabine Pellett, William H. Tepp, Amanda Przedpelski
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Patent number: 11491239Abstract: Provided herein are engineered non-catalytic, non-toxic tetanus toxin variants and methods of using such engineered tetanus toxin variants as low dose, protective vaccines that are non-toxic and more potent than their respective chemically inactivated toxoids. In addition, provided herein are conjugate vaccine carriers comprising engineered tetanus toxin variants and methods of using such conjugate vaccines to elicit T-cell dependent immune memory responses which can target a broad spectrum of microbial pathogens as a single vaccine.Type: GrantFiled: December 17, 2018Date of Patent: November 8, 2022Assignees: The Medical College of Wisconsin, Inc., Wisconsin Alumni Research FoundationInventors: Joseph T. Barbieri, Eric A. Johnson, Sabine Pellett, William H. Tepp, Amanda Przedpelski
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Publication number: 20210300970Abstract: Provided herein are antigenic peptides comprising the SARS-CoV-2 spike protein receptor binding domain (CRBD) polypeptide or portions thereof, linked to a non-catalytic, non-toxic tetanus toxin variant (i.e., a modified tetanus toxin or “MTT”) and vaccine compositions comprising the same. In addition, provided herein are methods for making and using CRBD-MTT fusion proteins as immunogenic agents.Type: ApplicationFiled: March 24, 2021Publication date: September 30, 2021Inventors: Joseph T. Barbieri, Amanda Przedpelski, Eric A. Johnson, Sabine Pellett, William H. Tepp
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Publication number: 20200384120Abstract: Provided herein are engineered non-catalytic, non-toxic tetanus toxin variants and methods of using such engineered tetanus toxin variants as low dose, protective vaccines that are non-toxic and more potent than their respective chemically inactivated toxoids. In addition, provided herein are conjugate vaccine carriers comprising engineered tetanus toxin variants and methods of using such conjugate vaccines to elicit T-cell dependent immune memory responses which can target a broad spectrum of microbial pathogens as a single vaccine.Type: ApplicationFiled: December 17, 2018Publication date: December 10, 2020Applicants: THE MEDICAL COLLEGE OF WISCONSIN, INC., WISCONSIN ALUMNI RESEARCH FOUNDATIONInventors: Joseph T. Barbieri, Eric A. Johnson, Sabine Pellett, William H. Tepp, Amanda Przedpelski
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Patent number: 10688162Abstract: The present disclosure relates to chimeric neurotoxins and uses thereof. In particular, provided herein are chimeric botulinum neurotoxins with altered properties and uses thereof (e.g., research, screening, and therapeutic uses).Type: GrantFiled: January 10, 2018Date of Patent: June 23, 2020Assignee: CELLSNAP LLCInventors: Eric A. Johnson, Sabine Pellett, William H. Tepp, Marite Bradshaw, Christina L. Pier, Joseph T. Barbieri
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Publication number: 20190321453Abstract: The present invention provides a universal delivery platform of functional, heterologous compounds to specific cells using toxins modified to include a heterologous compound. In one embodiment, the toxin is an AB5 toxin. In one embodiment, the AB5 toxin is a heat-labile enterotoxin from E. coli (LT), including LTI, LTII, LTIIa, LTIIb, LTIIc and other recombinant forms of LT. Methods of use are also provided.Type: ApplicationFiled: April 25, 2019Publication date: October 24, 2019Inventors: Joseph T. Barbieri, Chen Chen, Amanda Przedpelski, Eric A. Johnson, Sabine Pellett
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Publication number: 20180193435Abstract: The present disclosure relates to chimeric neurotoxins and uses thereof. In particular, provided herein are chimeric botulinum neurotoxins with altered properties and uses thereof (e.g., research, screening, and therapeutic uses).Type: ApplicationFiled: January 10, 2018Publication date: July 12, 2018Inventors: Eric A. Johnson, Sabine Pellett, William H. Tepp, Marite Bradshaw, Christina L. Pier, Joseph T. Barbieri
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Patent number: 10011823Abstract: The present invention provides a novel modified BoNT/E catalytic domain and methods of use thereof. In one embodiment, the light chain residue 224, or a residue corresponding to residue 224, of the modified BoNT/E catalytic domain has been altered to be aspartic acid or glutamic acid. The modified catalytic domain cleaves SNAP23 but does not cleave SNAP29 or SNAP47, providing novel methods of treating diseases including without limitation, asthma, CF, chronic obstructive pulmonary, gastric acid efflux and inflammation, immune disorders with a cytokine component or cancers with a cytokine component.Type: GrantFiled: April 13, 2010Date of Patent: July 3, 2018Assignee: MEDICAL COLLEGE OF WISCONSIN, INC.Inventors: Joseph T. Barbieri, Sheng Chen
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Publication number: 20170281737Abstract: The present invention provides a universal delivery platform of functional, heterologous compounds to specific cells using toxins modified to include a heterologous compound. In one embodiment, the toxin is an AB5 toxin. In one embodiment, the AB5 toxin is a heat-labile enterotoxin from E. coli (LT), including LTI, LTII, LTIIa, LTIIb, LTIIc and other recombinant forms of LT. Methods of use are also provided.Type: ApplicationFiled: September 29, 2015Publication date: October 5, 2017Inventors: Joseph T. Barbieri, Chen Chen, Amanda Przedpelski, Eric A. Johnson, Sabine Pellett
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Publication number: 20120039941Abstract: The present invention provides a novel modified BoNT/E catalytic domain and methods of use thereof. In one embodiment, the light chain residue 224, or a residue corresponding to residue 224, of the modified BoNT/E catalytic domain has been altered to be aspartic acid or glutamic acid. The modified catalytic domain cleaves SNAP23 but does not cleave SNAP29 or SNAP47, providing novel methods of treating diseases including without limitation, asthma, CF, chronic obstructive pulmonary, gastric acid efflux and inflammation, immune disorders with a cytokine component or cancers with a cytokine component.Type: ApplicationFiled: April 13, 2010Publication date: February 16, 2012Inventors: Joseph T. Barbieri, Sheng Chen
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Patent number: 7833524Abstract: The present invention provides a preparation of botulinum toxin light chain type A or E, wherein the preparation is both catalytically active and soluble. Preferably, the preparation consists essentially of amino acid residues 1 through 425 of the botulinum toxin light chain type A. A method of screening inhibitors is also provided, wherein the method comprises exposing a test inhibitor to the preparation of botulinum toxin light chain type A and evaluating the biological activity of the preparation. In another embodiment, a method of providing a catalytically active, soluble preparation of botulinum toxin light chain, type A is provided, wherein the method comprises obtaining an expression vector comprising a DNA sequence encoding amino acid residues 1-425 and expressing a polypeptide.Type: GrantFiled: November 18, 2008Date of Patent: November 16, 2010Assignee: Wisconsin Alumni Research FoundationInventors: Eric A. Johnson, Marite Bradshaw, Michael Baldwin, Joseph T. Barbieri
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Patent number: 7820411Abstract: A method of producing botulinum toxin C-terminal receptor binding domain (HCR) is disclosed. The one embodiment, the method comprises the steps of (a) preparing E. coli transformed with an expression vector comprising DNA encoding HCR protein, (b) inducing expression of the HCR protein at a reduced temperature in a culture media, and (c) purifying the HCR protein via extraction, wherein the extraction comprises a clarification by centrifugation and a filtration, wherein the purified HCR protein is at least 10 mg/L of culture medium.Type: GrantFiled: February 29, 2008Date of Patent: October 26, 2010Assignee: Wisconsin Alumni Research FoundationInventors: Michael Baldwin, Marite Bradshaw, William H. Tepp, Eric A. Johnson, Joseph T. Barbieri, Christina L. Pier
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Publication number: 20090182123Abstract: The present invention provides a preparation of botulinum toxin light chain type A or E, wherein the preparation is both catalytically active and soluble. Preferably, the preparation consists essentially of amino acid residues 1 through 425 of the botulinum toxin light chain type A. A method of screening inhibitors is also provided, wherein the method comprises exposing a test inhibitor to the preparation of botulinum toxin light chain type A and evaluating the biological activity of the preparation. In another embodiment, a method of providing a catalytically active, soluble preparation of botulinum toxin light chain, type A is provided, wherein the method comprises obtaining an expression vector comprising a DNA sequence encoding amino acid residues 1-425 and expressing a polypeptide.Type: ApplicationFiled: November 18, 2008Publication date: July 16, 2009Inventors: Eric A. Johnson, Marite Bradshaw, Michael Baldwin, Joseph T. Barbieri
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Publication number: 20090017495Abstract: A method of producing botulinum toxin C-terminal receptor binding domain (HCR) is disclosed. The one embodiment, the method comprises the steps of (a) preparing E. coli transformed with an expression vector comprising DNA encoding HCR protein, (b) inducing expression of the HCR protein at a reduced temperature in a culture media, and (c) purifying the HCR protein via extraction, wherein the extraction comprises a clarification by centrifugation and a filtration, wherein the purified HCR protein is at least 10 mg/L of culture medium.Type: ApplicationFiled: February 29, 2008Publication date: January 15, 2009Inventors: Michael Baldwin, Eric A. Johnson, Joseph T. Barbieri, Marite Bradshaw, William H. Tepp, Christina L. Pier
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Patent number: 7465457Abstract: The present invention provides a preparation of botulinum toxin light chain type A or E, wherein the preparation is both catalytically active and soluble. Preferably, the preparation consists essentially of amino acid residues 1 through 425 of the botulinum toxin light chain type A. A method of screening inhibitors is also provided, wherein the method comprises exposing a test inhibitor to the preparation of botulinum toxin light chain type A and evaluating the biological activity of the preparation. In another embodiment, a method of providing a catalytically active, soluble preparation of botulinum toxin light chain, type A is provided, wherein the method comprises obtaining an expression vector comprising a DNA sequence encoding amino acid residues 1-425 and expressing a polypeptide.Type: GrantFiled: April 14, 2006Date of Patent: December 16, 2008Assignees: Wisconsin Alumni Research Foundation, The MCW Research Foundation, IncorporatedInventors: Eric A. Johnson, Marite Bradshaw, Michael Baldwin, Joseph T. Barbieri
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Patent number: 5986080Abstract: We have cloned and sequenced the cDNA encoding the 61 kD active fragment of a unique porcine chondrocyte nucleotide pyrophosphohydrolase (NTPPHase) from a porcine chondrocyte library. Degenerate oligonucleotides, corresponding to the N-terminal amino acid sequence of this peptide were hybridized to porcine chondrocyte cDNA and used to amplify DNA encoding the N-terminal sequence of 61 kD with the polymerase chain reaction (PCR). The PCR products were then used as probes to clone the entire open reading-frame for the 61 kD fragment from a porcine chondrocyte cDNA library. The length of the cloned cDNA was 2509 bp. Translation of the open-reading-frame predicts the 61 kD fragment to be a 459 amino acid protein. BLAST and FASTA analysis confirmed that this amino acid sequence was unique and did not possess high homology to any known proteins in the non-redundant protein data base.Type: GrantFiled: October 17, 1997Date of Patent: November 16, 1999Assignee: MCW Research FoundationInventors: Ikuko Masuda, Joseph T. Barbieri, Arthur L. Haas, Brian D. Halligan, Daniel J. McCarty, Lawrence M. Ryan
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Patent number: 5599665Abstract: A genetic construct containing a coding region for exoenzyme S activity from Pseudomonas aeruginosa is disclosed. A essentially pure protein preparation of the 49 kDa form of exoenzyme S is also disclosed. The protein product of the genetic construct may be used to modify the RAS protein function in mammalian carcinomas, used as a vaccine, or used to diagnose Pseudomonas aeruginosa infection.Type: GrantFiled: December 21, 1993Date of Patent: February 4, 1997Assignee: MCW Research FoundationInventors: Joseph T. Barbieri, Dara W. Frank, Scott M. Kulich