SecB homologs can be associated with stress-responsive type II toxin–antitoxin (TA) systems and form tripartite toxin-antitoxin-chaperone systems (TAC). Here the authors provide structural insights into TACs by presenting the crystal structure of the M. tuberculosis TA-associated SecB chaperone in complex with the C-terminal ChAD (chaperone addiction) extension of the antitoxin HigA1.

This review discusses the templated spread of α-synuclein (α-syn) pathology in neurodegenerative disease from the perspective of proteopathic α-syn seeds. Recent discoveries concerning the structure and cell biology of pathological α-syn aggregates are highlighted.

A computationally designed molecular chaperone inhibits the interaction of normal prions with abnormal isoforms associated with transmissible spongiform encephalopathy, prolongs survival in infected mice and limits symptoms in infected macaques.