Toxin Instability and Its Role in Toxin Translocation from the Endoplasmic Reticulum to the Cytosol
Biomolecules, 2013 AB toxins enter a host cell by receptor-mediated endocytosis. The catalytic A chain then crosses the endosome or endoplasmic reticulum (ER) membrane to reach its cytosolic target. Dissociation of the A chain from the cell-binding B chain occurs before or
Ken Teter
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Characterization of botulinum neurotoxin type A neutralizing monoclonal antibodies and influence of their half-lives on therapeutic activity. [PDF]
PLoS ONE, 2010 Botulinum toxins, i.e. BoNT/A to/G, include the most toxic substances known. Since botulism is a potentially fatal neuroparalytic disease with possible use as a biowarfare weapon (Centers for Disease Control and Prevention category A bioterrorism agent),
Christelle Mazuet +4 more
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Domperidone Inhibits Clostridium botulinum C2 Toxin and Bordetella pertussis Toxin
Toxins, 2023 Bordetella pertussis toxin (PT) and Clostridium botulinum C2 toxin are ADP-ribosylating toxins causing severe diseases in humans and animals. They share a common translocation mechanism requiring the cellular chaperones Hsp90 and Hsp70, cyclophilins, and
Jinfang Jia +6 more
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Scientific Reports, 2021 Translocation is essential to the anthrax toxin mechanism. Protective antigen (PA), the binding component of this AB toxin, forms an oligomeric pore that translocates lethal factor (LF) or edema factor, the active components of the toxin, into the cell ...
Alexandra J. Machen +2 more
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The apoptogenic toxin AIP56 is a metalloprotease A-B toxin that cleaves NF-κb P65.
PLoS Pathogens, 2013 AIP56 (apoptosis-inducing protein of 56 kDa) is a major virulence factor of Photobacterium damselae piscicida (Phdp), a Gram-negative pathogen that causes septicemic infections, which are among the most threatening diseases in mariculture.
Daniela S Silva +14 more
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Diphtheria and the AB Toxin Group: a History and the Need for New Toxin Therapeutics
, 2023 AB toxins have historically been associated with significant morbidity, mortality through infections such as botulinum, anthrax, cholera, and diphtheria. These AB toxin-mediated diseases remain prevalent in low and middle income countries, with intermittent outbreaks of Shiga toxin-producing Escherichia coli (STEC) or whooping cough by Bordetella ...
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Proinflammatory Responses in the Murine Brain after Intranasal Delivery of Cholera Toxin: Implications for the Use of AB Toxins as Adjuvants in Intranasal Vaccines [PDF]
The Journal of Infectious Diseases, 2005 Intranasal delivery of vaccines provides an attractive alternative to parenteral delivery, but it requires appropriate mucosal adjuvants. Cholera toxin (CT) is a powerful mucosal adjuvant, but it can undergo retrograde transport to the brain via the olfactory system after intranasal delivery.
Michelle E, Armstrong +4 more
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Refinement and Neutralization Evaluation of the F(ab’)2 Type of Antivenom against the Deadly Jellyfish Nemopilema nomurai Toxins [PDF]
International Journal of Molecular Sciences, 2021 Jellyfish stings threaten people’s health and even life in coastal areas worldwide. Nemopilema nomurai is one of the most dangerous jellyfish in the East Asian Marginal Seas, which not only stings hundreds of thousands of people every year but also is assumed to be responsible for most deaths by jellyfish stings in China. However, there is no effective
Rongfeng Li +4 more
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Antibody-Mediated Inhibition of Ricin Toxin Retrograde Transport
mBio, 2014 Ricin is a member of the ubiquitous family of plant and bacterial AB toxins that gain entry into the cytosol of host cells through receptor-mediated endocytosis and retrograde traffic through the trans-Golgi network (TGN) and endoplasmic reticulum (ER ...
Anastasiya Yermakova +4 more
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Pet, a Non-AB Toxin, Is Transported and Translocated into Epithelial Cells by a Retrograde Trafficking Pathway [PDF]
Infection and Immunity, 2007 ABSTRACT The plasmid-encoded toxin (Pet) of enteroaggregative Escherichia coli is a 104-kDa autotransporter protein that exhibits proteolytic activity against the actin-binding protein α-fodrin. Intracellular cleavage of epithelial fodrin by Pet disrupts the actin cytoskeleton, causing both cytotoxic and ...
Navarro-GarcÃa, Fernando +4 more
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