Assembly and architecture of the type III secretion sorting platform
Open accessPublished version of a preprint
Abstract
Type III secretion systems are bacterial nanomachines specialized in protein delivery into target eukaryotic cells. The structural and functional complexity of these machines demands highly coordinated mechanisms for their assembly and operation. The sorting platform is a critical component of type III secretion machines that ensures the timely engagement and secretion of proteins destined to travel this export pathway. However, the mechanisms that lead to the assembly of this multicomponent structure have not been elucidated. Herein, employing an extensive in vivo cross-linking strategy aided by structure modeling, we provide a detailed intersubunit contact survey of the entire sorting platform complex. Using the identified cross-links as signatures for pairwise intersubunit interactions in combination with systematic genetic deletions, we mapped the assembly process of this unique bacterial structure. Insights generated by this study could serve as the bases for the rational development of antivirulence strategies to combat several medically important bacterial pathogens.
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Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works
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- Authors
- Soto, J. E., Galán, J. E., & Lara-Tejero, M.
- Affiliations
- Department of Microbial Pathogenesis, Yale University School of Medicine, New Haven, CT 06536
- Yale University (US)
- Corresponding author
- Galán, Jorge E.
- ORCID
- Galán, Jorge E.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2022-12-13
- Volume
- 119
- Issue
- 51
- Pages
- e2218010119-e2218010119
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC9907115
- OpenAlex
- W4311587853
- Cited by
- 22
- References
- 3
- Citations by year
- 2026: 8 · 2025: 7 · 2024: 2 · 2023: 5
- FWCI
- 2.20
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion, cc-by-nc-nd)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- HHS | NIH | NIAID | Division of Microbiology and Infectious Diseases, National Institute of Allergy and Infectious Diseases (AI126158, AI030492)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Escherichia coli research studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Keywords
- type III secretion system, protein secretion, protein complex formation, intersubunit interactions, in vivo cross-linking, gene deletion, anti-virulence strategies, pathogenic bacteria
- MeSH terms
- Type III Secretion Systems, Bacterial Proteins, Salmonella typhimurium, Protein Transport
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