Exploring protein N -glycosylation in ammonia-oxidizing Nitrososphaerota archaea through glycoproteomic analysis

作者：Satoshi Nakagawa, Hirokazu Yagi, Tomoki Suyama, Shigeru Shimamura, Saeko Yanaka, Maho Yagi‐Utsumi, Shingo Kato, Moriya Ohkuma, Koichi Kato, Ken Takai · 发表于：mBio · 年份：2025 · DOI：10.1128/mbio.03859-24 · 被引用次数：6 · 研究领域：Microbial Community Ecology and Physiology、Protist diversity and phylogeny、Genomics and Phylogenetic Studies

ABSTRACT Ammonia-oxidizing archaea of the phylum Nitrososphaerota , formerly known as Thaumarchaeota , are globally distributed and play critical roles in the nitrogen and carbon cycles, particularly in environments with low ammonia concentrations. Like most archaea, Nitrososphaerota cells are enveloped by S-layer proteins, implicated in concentrating ammonium ions. These proteins are typically modified post-translationally by N -glycans, which often play significant roles in various biological processes, including protein function regulation, protection from phages, and environmental adaptation. Nevertheless, the glycobiological characteristics of Nitrososphaerota remain largely unexplored. Here, we investigated the glycoproteome of ammonia-oxidizing Nitrososphaerota , specifically focusing on the terrestrial Nitrososphaera viennensis and the marine Nitrosopumilus piranensis . Both species exhibited similar protein arrays throughout their growth phases, including those associated with N -glycosylation. Ns. viennensis consistently exhibited N -glycosylation predominantly on an S-layer protein and multicopper oxidase domain-containing proteins throughout all growth phases, with a marked increase during and after the late exponential phase. The glycan, characterized as a novel hexasaccharide with a chitobiose core, is hypothesized to play a role in nitrogen storage due to its probable nitrogen-rich composition, modifying asparagine residues within the conserved triplet sequence...