ArticleThe Journal of biological chemistry2016
Type IV Pilus Alignment Subcomplex Proteins PilN and PilO Form Homo- and Heterodimers in Vivo.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- A pangenome-based strategy for designing a multi-epitope vaccine against non-toxin antigens of necrotic enteritis-associated Clostridium perfringens.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2026Article
- Article
- Integrative Structure and Function of thebioRxiv : the preprint server for biology · 2025Article
- Twitching motility suppressors reveal a role for FimX in type IV pilus extension dynamics.PLoS genetics · 2025Article
- The structure of the Tad pilus alignment complex reveals a periplasmic conduit for pilus extension.Nature communications · 2025Article
- PilY1 regulates the dynamic architecture of the type IV pilus machine in Pseudomonas aeruginosa.Nature communications · 2024Article
- Article
- Bacterial flagella hijack type IV pili proteins to control motility.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Crystal structure of monomeric Amuc_1100 from Akkermansia muciniphila.Acta crystallographica. Section F, Structural biology communications · 2020Article
- In vivo structure of the Legionella type II secretion system by electron cryotomography.Nature microbiology · 2019Article
- Rapid genetic and phenotypic changes in Pseudomonas aeruginosa clinical strains during ventilator-associated pneumonia.Scientific reports · 2019Article
- The Dynamic Structures of the Type IV Pilus.Microbiology spectrum · 2019Review
- The traffic ATPase PilF interacts with the inner membrane platform of the DNA translocator and type IV pili fromFEBS open bio · 2019Article
- Direct interactions between the secreted effector and the T2SS components GspL and GspM reveal a new effector-sensing step during type 2 secretion.The Journal of biological chemistry · 2018Article
- Structure and oligomerization of the periplasmic domain of GspL from the type II secretion system of Pseudomonas aeruginosa.Scientific reports · 2018Article
- Mechanisms and Targeted Therapies for Pseudomonas aeruginosa Lung Infection.American journal of respiratory and critical care medicine · 2018Review
- Conserved, unstructured regions in Pseudomonas aeruginosa PilO are important for type IVa pilus function.Scientific reports · 2018Article
- Diversity and Evolution of Myxobacterial Type IV Pilus Systems.Frontiers in microbiology · 2018Article
- Article
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Authors and funding
4 authors.
Funding
Abstract
Pseudomonas aeruginosa is a leading cause of hospital-acquired infections and is resistant to many antibiotics. Type IV pili (T4P) are among the key virulence factors used by P. aeruginosa for host cell attachment, biofilm formation, and twitching motility, making this system a promising target for novel therapeutics. Point mutations in the conserved PilMNOP alignment subcomplex were previously shown to have distinct effects on assembly and disassembly of T4P, suggesting that it may function in a dynamic manner. We introduced mutations encoding Cys substitutions into pilN and/or pilO on the chromosome to maintain normal stoichiometry and expression levels and captured covalent PilNO heterodimers, as well as PilN and PilO homodimers, in vivo Most covalent PilN or PilO homodimers had minimal functional impact in P. aeruginosa, suggesting that homodimers are a physiologically relevant state. However, certain covalent homo- or heterodimers eliminated twitching motility, suggesting that specific PilNO configurations are essential for T4P function. These data were verified using soluble N-terminal truncated fragments of PilN and PilO Cys mutants, which purified as a mixture of homo- and heterodimers at volumes consistent with a tetramer. Deletion of genes encoding alignment subcomplex components, PilM or PilP, but not other T4P components, including the motor ATPases PilB or PilT, blocked in vivo formation of disulfide-bonded PilNO heterodimers, suggesting that both PilM and PilP influence the heterodimer interface. Combined, our data suggest that T4P function depends on rearrangements at PilN and PilO interfaces.
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