ArticleNature communications2024
Perturbed N-glycosylation of Halobacterium salinarum archaellum filaments leads to filament bundling and compromised cell motility.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed.
- Two types of sheathed archaellum structures from Haloarcula marismortui differ in their outer layer architectures.Nature communications · 2026Article
- The assembly rules guiding hetero-oligomeric bacterioferritin organization and their evolutionary signature.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Identification of the D-glucuronyl C5-epimerase that introduces iduronic acid into N-linked glycans decorating archaeal glycoproteins.Communications biology · 2025Article
- Structure of a functional archaellum in Bacteria of the Chloroflexota phylum.Nature microbiology · 2025Article
- Article
- How Does the Archaellum Work?Biomolecules · 2025Review
- Unusual cell surfaces, pili, and archaella of Thermoplasmatales archaea.The ISME journal · 2025Article
- Article
- Towards a molecular picture of the archaeal cell surface.Nature communications · 2024Article
- N-glycosylation in Archaea - Expanding the process, components and roles of a universal post-translational modification.BBA advances · 2024Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The swimming device of archaea-the archaellum-presents asparagine (N)-linked glycans. While N-glycosylation serves numerous roles in archaea, including enabling their survival in extreme environments, how this post-translational modification contributes to cell motility remains under-explored. Here, we report the cryo-EM structure of archaellum filaments from the haloarchaeon Halobacterium salinarum, where archaellins, the building blocks of the archaellum, are N-glycosylated, and the N-glycosylation pathway is well-resolved. We further determined structures of archaellum filaments from two N-glycosylation mutant strains that generate truncated glycans and analyzed their motility. While cells from the parent strain exhibited unidirectional motility, the N-glycosylation mutant strain cells swam in ever-changing directions within a limited area. Although these mutant strain cells presented archaellum filaments that were highly similar in architecture to those of the parent strain, N-linked glycan truncation greatly affected interactions between archaellum filaments, leading to dramatic clustering of both isolated and cell-attached filaments. We propose that the N-linked tetrasaccharides decorating archaellins act as physical spacers that minimize the archaellum filament aggregation that limits cell motility.
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