Deubiquitinating enzyme VCIP135 dictates the duration of botulinum neurotoxin type A intoxication

Abstract

Botulinum neurotoxins (BoNTs) are the most potent biological toxins. These proteases function by cleaving SNARE proteins, leading to paralysis and death from respiratory failure. BoNT serotype A (BoNT/A) has the most prolonged symptoms due to an extraordinarily stable catalytic light chain (LCA). BoNT/A intoxication can occur through ingestion (either sporadically or from a common food source), as a consequence of a clinical mishap, or potentially through bioterrorism, which would require mass mechanical ventilation. We report that LCA persistence is due to a particular deubiquitinating enzyme that binds a specific region of LCA and prevents its ubiquitin-dependent proteasomal degradation. These findings represent an essential step toward developing targeted molecular approaches to reducing morbidity and mortality from this toxin.

Document Details

Document Type
Pub Defense Publication
Publication Date
Jun 05, 2017
Source ID
10.1073/pnas.1621076114

Entities

People

  • Allan M. Weissman
  • Archana Kotiya
  • Erkan Kiris
  • George A. Oyler
  • Lino Tessarollo
  • Mei Yang
  • Sina Bavari
  • Yien Che Tsai

Organizations

  • Defense Threat Reduction Agency
  • Johns Hopkins University
  • National Cancer Institute
  • National Institute of Allergy and Infectious Diseases
  • United States Army Medical Research Institute of Infectious Diseases

Tags

Fields of Study

  • Biology
  • Medicine

Readers

  • Microbial Pathology
  • Molecular Biology and Genetics
  • Systems Analysis and Design