ArticleProceedings of the National Academy of Sciences of the United States of America2013
Rickettsia Sca2 has evolved formin-like activity through a different molecular mechanism.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 50 citations in OpenAlex.
- Article
- Divergent Rickettsia species exhibit distinct mechanisms of actin-based motility.The Journal of cell biology · 2026Article
- The pro-metastatic role of microbiota in tumors: a comprehensive review.Cancer cell international · 2026Review
- Legionella effector protein SidG disrupts host cytoskeleton via targeting Arp2/3 complex.PLoS pathogens · 2026Article
- Host cyclophilin-mediated maturation of an obligate intracellular bacterial surface virulence factor.bioRxiv : the preprint server for biology · 2025Article
- ThemBio · 2025Article
- The actin filament pointed-end depolymerase Srv2/CAP depolymerizes barbed ends, displaces capping protein, and promotes formin processivity.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- PathogenicJournal of bacteriology · 2024Review
- Critical roles ofInfection and immunity · 2024Article
- Membrane-dependent actin polymerization mediated by the Legionella pneumophila effector protein MavH.PLoS pathogens · 2023Article
- Single particle cryo-EM analysis of Rickettsia conorii Sca2 reveals a formin-like core.Journal of structural biology · 2023Article
- Metagenome diversity illuminates origins of pathogen effectors.bioRxiv : the preprint server for biology · 2023Article
- Membrane-dependent actin polymerization mediated by thebioRxiv : the preprint server for biology · 2023Article
- Functional Mimicry of Eukaryotic Actin Assembly by Pathogen Effector Proteins.International journal of molecular sciences · 2022Review
- Review
- Moonlighting in Rickettsiales: Expanding Virulence Landscape.Tropical medicine and infectious disease · 2022Review
- Lysine methylation shields an intracellular pathogen from ubiquitylation and autophagy.Science advances · 2021Article
- Folding Control in the Path of Type 5 Secretion.Toxins · 2021Review
- The enigmatic biology of rickettsiae: recent advances, open questions and outlook.Pathogens and disease · 2021Review
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Sca2 (surface cell antigen 2) is the only bacterial protein known to promote both actin filament nucleation and profilin-dependent elongation, mimicking eukaryotic formins to assemble actin comet tails for Rickettsia motility. We show that Sca2's functional mimicry of formins is achieved through a unique mechanism. Unlike formins, Sca2 is monomeric, but has N- and C-terminal repeat domains (NRD and CRD) that interact with each other for processive barbed-end elongation. The crystal structure of NRD reveals a previously undescribed fold, consisting of helix-loop-helix repeats arranged into an overall crescent shape. CRD is predicted to share this fold and might form together with NRD, a doughnut-shaped formin-like structure. In between NRD and CRD, proline-rich sequences mediate the incorporation of profilin-actin for elongation, and WASP-homology 2 (WH2) domains recruit actin monomers for nucleation. Sca2's α-helical fold is unusual among Gram-negative autotransporters, which overwhelmingly fold as β-solenoids. Rickettsia has therefore "rediscovered" formin-like actin nucleation and elongation.
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