Search results for: Joseph T. Barbieri

Items from 1 to 20 out of 30 results

article

Enhancing toxin-based vaccines against botulism

Amanda Przedpelski, William H. Tepp, Madison Zuverink, Eric A. Johnson, more

Vaccine > 2018 > 36 > 6 > 827-832

Botulinum neurotoxins (BoNT) are the most toxic proteins for humans. BoNTs are single chain proteins with an N-terminal light chain (LC) and a C-terminal heavy chain (HC). HC comprises a translocation domain (HC_N) and a receptor binding domain (HC_C). Currently, there are no approved vaccines against botulism. This study tests a recombinant, full-length BoNT/A1 versus LCHC_N/A1 and HC_C/A1 as vaccine...

chapter

Toxins from bacteria

James S. Henkel, Michael R. Baldwin, Joseph T. Barbieri

Experientia Supplementum > Molecular, Clinical and Environmental Toxicology > 1-29

Bacterial toxins damage the host at the site of bacterial infection or distant from the site. Bacterial toxins can be single proteins or oligomeric protein complexes that are organized with distinct AB structure-function properties. The A domain encodes a catalytic activity. ADP ribosylation of host proteins is the earliest post-translational modification determined to be performed by bacterial toxins;...

article

Solubility of the catalytic domains of Botulinum neurotoxin serotype E subtypes

Sheng Chen, Joseph T. Barbieri

Protein Expression and Purification > 2016 > 118 > Complete > 18-24

The Clostridium botulinum neurotoxins (BoNTs) are the most potent protein toxins known to humans. There are seven serotypes of the BoNTs (A–G), among which serotypes A, B, E and F are known to cause natural human intoxication. To date, eleven subtypes of LC/E, termed E1∼E11, have been identified. The LCs of BoNT/E were insoluble, prohibiting studies towards understanding the mechanisms of toxin action...

article

Multiple Domains of Tetanus Toxin Direct Entry into Primary Neurons

Faith C. Blum, William H. Tepp, Eric A. Johnson, Joseph T. Barbieri

Traffic > 15 > 10 > 1057 - 1065

Tetanus toxin elicits spastic paralysis by cleaving VAMP‐2 to inhibit neurotransmitter release in inhibitory neurons of the central nervous system. As the retrograde transport of tetanus neurotoxin (TeNT) from endosomes has been described, the initial steps that define how TeNT initiates trafficking to the retrograde system are undefined. This study examines TeNT entry into primary cultured cortical...

article

Pseudomonas aeruginosa serology and risk for re-isolation in the EPIC trial

Michael Anstead, Sonya L. Heltshe, Umer Khan, Joseph T. Barbieri, more

Journal of Cystic Fibrosis > 2013 > 12 > 2 > 147-153

The prognostic value of Pseudomonas aeruginosa serology for antibiotic therapy in cystic fibrosis patients is not well understood.Using five antigens from two ELISAs, we assessed whether positive serology in CF patients participating in the multi-center Early Pseudomonas Infection in Children (EPIC) trial would predict treatment failure, time to pulmonary exacerbation and risk for recurrent P. aeruginosa...

article

Vaccines against botulism

Andrew P-A Karalewitz, Joseph T Barbieri

Current Opinion in Microbiology > 2012 > 15 > 3 > 317-324

The clostridial neurotoxins (CNTs) are the most toxic proteins for humans and include botulinum neurotoxins (BoNT) and tetanus neurotoxin (TeNT). CNT neurotropism is based upon the preferred binding and entry into neurons and specific cleavage of neuronal SNARE proteins. While chemically inactive TeNT toxoid remains an effect vaccine, the current pentavalent vaccine against botulism is in limited...

article

Unique ganglioside binding by botulinum neurotoxins C and D‐SA

Abby R. Kroken, Andrew P.‐A. Karalewitz, Zhuji Fu, Michael R. Baldwin, more

The FEBS Journal > 278 > 23 > 4486 - 4496

The botulinum neurotoxins (BoNTs) are the most potent protein toxins for humans. There are seven serotypes of BoNTs (A–G), based on a lack of cross‐antiserum neutralization. The BoNT/C and BoNT/D serotypes include mosaic toxins that are organized as D–C and C–D toxins. One BoNT D–C mosaic toxin, BoNT/D‐South Africa (BoNT/D‐SA), was not fully neutralized by immunization with a vaccine composed of either...

article

Adenylate cyclase activity of Pseudomonas aeruginosa ExoY can mediate bleb-niche formation in epithelial cells and contributes to virulence

Victoria Hritonenko, James J. Mun, Connie Tam, Nathan C. Simon, more

Microbial Pathogenesis > 2011 > 51 > 5 > 305-312

We previously showed that ADP-ribosylation (ADP-r) activity of ExoS, a type III secreted toxin of Pseudomonas aeruginosa, enables bacterial replication in corneal and respiratory epithelial cells and correlates with bacterial trafficking to plasma membrane blebs (bleb-niche formation). Here, we explored another type III secreted toxin, ExoY, for its impact on intracellular trafficking and survival,...

article

Subunit vaccine efficacy against Botulinum neurotoxin subtypes

James S. Henkel, William H. Tepp, Amanda Przedpelski, Robert B. Fritz, more

Vaccine > 2011 > 29 > 44 > 7688-7695

Botulinum neurotoxins (BoNT) are classified into 7 serotypes (A–G) based upon neutralization by serotype-specific anti-sera. Several recombinant serotype-specific subunit BoNT vaccines have been developed, including a subunit vaccine comprising the receptor binding domain (HCR) of the BoNTs. Sequencing of the genes encoding BoNTs has identified variants (subtypes) that possess up to 32% primary amino...

article

Botulinum neurotoxin subtype A2 enters neuronal cells faster than subtype A1

Christina L. Pier, Chen Chen, William H. Tepp, Guangyun Lin, more

FEBS Letters > 2011 > 585 > 1 > 199-206

Botulinum neurotoxins (BoNTs), the causative agent of human botulism, are the most potent naturally occurring toxins known. BoNT/A1, the most studied BoNT, is also used as an important biopharmaceutical. In this study, the biological activity of BoNT/A1 is compared to that of BoNT/A2 using neuronal cell models. The data obtained indicate faster and increased intoxication of neuronal cells by BoNT/A2...

article

Identification of a Unique Ganglioside Binding Loop within Botulinum Neurotoxins C and D-SA,

Andrew P.-A. Karalewitz, Abby R. Kroken, Zhuji Fu, Michael R. Baldwin, more

Biochemistry > 2010 > 49 > 37 > 8117 - 8126

article

Structural Analysis of Botulinum Neurotoxin Type G Receptor Binding,

John Schmitt, Andrew Karalewitz, Desirée A. Benefield, Darren J. Mushrush, more

Biochemistry > 2010 > 49 > 25 > 5200 - 5205

article

Botulinum Neurotoxin A Protease: Discovery of Natural Product Exosite Inhibitors

Peter Šilhár, Kateřina Čapková, Nicholas T. Salzameda, Joseph T. Barbieri, more

Journal of the American Chemical Society > 2010 > 132 > 9 > 2868 - 2869

article

Chirality Holds the Key for Potent Inhibition of the Botulinum Neurotoxin Serotype A Protease

G. Neil Stowe, Peter Šilhár, Mark S. Hixon, Nicholas R. Silvaggi, more

Organic Letters > 2010 > 12 > 4 > 756 - 759

article

Benzylidene cyclopentenediones: First irreversible inhibitors against botulinum neurotoxin A’s zinc endopeptidase

Kateřina Čapková, Mark S. Hixon, Sabine Pellett, Joseph T. Barbieri, more

Bioorganic & Medicinal Chemistry Letters > 2010 > 20 > 1 > 206-208

A series of benzylidene cyclopentenedione-based inhibitors, acting through covalent modification of the active site of botulinum neurotoxin A light chain metalloprotease, are reported.

article

Synthetic substrate for application in both high and low throughput assays for botulinum neurotoxin B protease inhibitors

Nicholas T. Salzameda, Joseph T. Barbieri, Kim D. Janda

Bioorganic & Medicinal Chemistry Letters > 2009 > 19 > 20 > 5848-5850

A FRET peptide substrate was synthesized and evaluated for enzymatic cleavage by the BoNT/B light chain protease. The FRET substrate was found to be useful in both a high throughput assay to uncover initial ‘hits’ and a low throughput HPLC assay to determine kinetic parameters and modes of inhibition.

article

Association of botulinum neurotoxins with synaptic vesicle protein complexes

Michael R. Baldwin, Joseph T. Barbieri

Toxicon > 2009 > 54 > 5 > 570-574

Botulinum neurotoxins (BoNTs) elicit flaccid paralysis by cleaving SNARE proteins within peripheral neurons. BoNTs are classified into seven serotypes, termed A–G, based on antibody cross-neutralization. Clostridia produce BoNTs as single-chain toxins that are cleaved into a di-chain protein that comprises an N-terminal zinc metalloprotease domain that is linked by a disulfide bond to the C-terminal...

article

Glycosylated SV2 and Gangliosides as Dual Receptors for Botulinum Neurotoxin Serotype F

Zhuji Fu, Chen Chen, Joseph T. Barbieri, Jung-Ja P. Kim, more

Biochemistry > 2009 > 48 > 24 > 5631 - 5641

article

Catalytic Properties of Botulinum Neurotoxin Subtypes A3 and A4 ^†

James S. Henkel, Mark Jacobson, William Tepp, Christina Pier, more

Biochemistry > 2009 > 48 > 11 > 2522 - 2528

article

Molecular Basis for Tetanus Toxin Coreceptor Interactions ^†

Chen Chen, Michael R. Baldwin, Joseph T. Barbieri

Biochemistry > 2008 > 47 > 27 > 7179 - 7186

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Search results for: Joseph T. Barbieri

Enhancing toxin-based vaccines against botulism

Toxins from bacteria

Solubility of the catalytic domains of Botulinum neurotoxin serotype E subtypes

Multiple Domains of Tetanus Toxin Direct Entry into Primary Neurons

Pseudomonas aeruginosa serology and risk for re-isolation in the EPIC trial

Vaccines against botulism

Unique ganglioside binding by botulinum neurotoxins C and D‐SA

Adenylate cyclase activity of Pseudomonas aeruginosa ExoY can mediate bleb-niche formation in epithelial cells and contributes to virulence

Subunit vaccine efficacy against Botulinum neurotoxin subtypes

Botulinum neurotoxin subtype A2 enters neuronal cells faster than subtype A1

Identification of a Unique Ganglioside Binding Loop within Botulinum Neurotoxins C and D-SA,

Structural Analysis of Botulinum Neurotoxin Type G Receptor Binding,

Botulinum Neurotoxin A Protease: Discovery of Natural Product Exosite Inhibitors

Chirality Holds the Key for Potent Inhibition of the Botulinum Neurotoxin Serotype A Protease

Benzylidene cyclopentenediones: First irreversible inhibitors against botulinum neurotoxin A’s zinc endopeptidase

Synthetic substrate for application in both high and low throughput assays for botulinum neurotoxin B protease inhibitors

Association of botulinum neurotoxins with synaptic vesicle protein complexes

Glycosylated SV2 and Gangliosides as Dual Receptors for Botulinum Neurotoxin Serotype F

Catalytic Properties of Botulinum Neurotoxin Subtypes A3 and A4 ^†

Molecular Basis for Tetanus Toxin Coreceptor Interactions ^†

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