Perturbed N-glycosylation of Halobacterium salinarum archaellum filaments leads to filament bundling and compromised cell motility

Shahar Sofer, Zlata Vershinin, Leen Mashni, Ran Zalk, Anat Shahar, Jerry Eichler and Iris Grossman-Haham ()
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Shahar Sofer: Ben-Gurion University of the Negev
Zlata Vershinin: Ben-Gurion University of the Negev
Leen Mashni: Ben-Gurion University of the Negev
Ran Zalk: Ben-Gurion University of the Negev
Anat Shahar: Ben-Gurion University of the Negev
Jerry Eichler: Ben-Gurion University of the Negev
Iris Grossman-Haham: Ben-Gurion University of the Negev

Nature Communications, 2024, vol. 15, issue 1, 1-13

Abstract: 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.

Date: 2024
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DOI: 10.1038/s41467-024-50277-1

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