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Title TccC3 Toxin Targets the Dynamic Population of F-Actin and Impairs Cell Cortex Integrity.
Journal, issue, pagesInt J Mol Sci, Vol. 23, Issue 13, Year 2022
Publish dateJun 24, 2022
AuthorsSongyu Dong / Weili Zheng / Nicholas Pinkerton / Jacob Hansen / Svetlana B Tikunova / Jonathan P Davis / Sarah M Heissler / Elena Kudryashova / Edward H Egelman / Dmitri S Kudryashov /
PubMed AbstractDue to its essential role in cellular processes, actin is a common target for bacterial toxins. One such toxin, TccC3, is an effector domain of the ABC-toxin produced by entomopathogenic bacteria of ...Due to its essential role in cellular processes, actin is a common target for bacterial toxins. One such toxin, TccC3, is an effector domain of the ABC-toxin produced by entomopathogenic bacteria of spp. Unlike other actin-targeting toxins, TccC3 uniquely ADP-ribosylates actin at Thr-148, resulting in the formation of actin aggregates and inhibition of phagocytosis. It has been shown that the fully modified F-actin is resistant to depolymerization by cofilin and gelsolin, but their effects on partially modified actin were not explored. We found that only F-actin unprotected by tropomyosin is the physiological TccC3 substrate. Yet, ADP-ribosylated G-actin can be produced upon cofilin-accelerated F-actin depolymerization, which was only mildly inhibited in partially modified actin. The affinity of TccC3-ADP-ribosylated G-actin for profilin and thymosin-β4 was weakened moderately but sufficiently to potentiate spontaneous polymerization in their presence. Interestingly, the Arp2/3-mediated nucleation was also potentiated by T148-ADP-ribosylation. Notably, even partially modified actin showed reduced bundling by plastins and α-actinin. In agreement with the role of these and other tandem calponin-homology domain actin organizers in the assembly of the cortical actin network, TccC3 induced intense membrane blebbing in cultured cells. Overall, our data suggest that TccC3 imposes a complex action on the cytoskeleton by affecting F-actin nucleation, recycling, and interaction with actin-binding proteins involved in the integration of actin filaments with each other and cellular elements.
External linksInt J Mol Sci / PubMed:35806028 / PubMed Central
MethodsEM (helical sym.)
Resolution3.9 Å
Structure data

EMDB-26987: T148-ADPR-F-actin
Method: EM (helical sym.) / Resolution: 3.9 Å

Source
  • Oryctolagus cuniculus (rabbit)

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