Towards a molecular picture of the archaeal cell surface

Archaea produce various protein filaments with specialised functions. While some archaea produce only one type of filament, the archaeal model species Sulfolobus acidocaldarius generates four. These include rotary swimming propellers analogous to bacterial flagella (archaella), pili for twitching motility (Aap), adhesive fibres (threads), and filaments facilitating homologous recombination upon UV stress (UV pili). Here, we use cryo-electron microscopy to describe the structure of the S. acidocaldarius archaellum at 2.0 Å resolution, and update the structures of the thread and the Aap pilus at 2.7 Å and 2.6 Å resolution, respectively. We define features unique to archaella of the order Sulfolobales and compare their structure to those of Aap and threads in the context of the S-layer. We define distinct N-glycan patterns in the three filaments and identify a putative O-glycosylation site in the thread. Finally, we ascertain whether N-glycan truncation leads to structural changes in archaella and Aap.

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Publication Details

Journal
Nature Communications
Published
2024-11-29
DOI
https://doi.org/10.1038/s41467-024-53986-9
Citations
6
Primary Topic
Enzyme Structure and Function
Type
article
Field-Weighted Citation Impact
0.70

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article

Towards a molecular picture of the archaeal cell surface

Cyril Hanus, Michail N. Isupov, Daniel R. Kattnig, Matthew C. Gaines et al.
6 citations
Nature Communications
Enzyme Structure and Function
0.70
article

Towards a molecular picture of the archaeal cell surface

Cyril Hanus, Michail N. Isupov, Daniel R. Kattnig, Matthew C. Gaines, Shamphavi Sivabalasarma, Clara L. Mollat, Risat Ul Haque, Jake K. Stephenson, Mathew McLaren, Bertram Daum, Vicki A. M. Gold, Sonja‐Verena Albers
article en
6 citations

Abstract

Archaea produce various protein filaments with specialised functions. While some archaea produce only one type of filament, the archaeal model species Sulfolobus acidocaldarius generates four. These include rotary swimming propellers analogous to bacterial flagella (archaella), pili for twitching motility (Aap), adhesive fibres (threads), and filaments facilitating homologous recombination upon UV stress (UV pili). Here, we use cryo-electron microscopy to describe the structure of the S. acidocaldarius archaellum at 2.0 Å resolution, and update the structures of the thread and the Aap pilus at 2.7 Å and 2.6 Å resolution, respectively. We define features unique to archaella of the order Sulfolobales and compare their structure to those of Aap and threads in the context of the S-layer. We define distinct N-glycan patterns in the three filaments and identify a putative O-glycosylation site in the thread. Finally, we ascertain whether N-glycan truncation leads to structural changes in archaella and Aap.

Nature CommunicationsVol. 15(1)
Inserm (FR), University of Freiburg (DE), Université Paris Cité (FR), University of Exeter (GB), Institut de Psychiatrie et Neurosciences de Paris (FR)
Wellcome Trust, Diamond Light Source, Leverhulme Trust, European Commission, Deutsche Forschungsgemeinschaft, Agence Nationale de la Recherche, Horizon 2020 Framework Programme, Medical Research Council, Biotechnology and Biological Sciences Research Council
Life below water
Openalex Percentile: Top 29%
Enzyme Structure and Function
0.70
DOIOpen Access PDFOpenAlex
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