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ORIGINAL RESEARCH article

Front. Microbiol.
Sec. Biology of Archaea
Volume 15 - 2024 | doi: 10.3389/fmicb.2024.1463715
This article is part of the Research Topic Molecular Biology of Archaea - 2024 View all articles

Structural and functional insights from the sequences and complex domain architecture of adhesin-like proteins from Methanobrevibacter smithii and Methanosphaera stadtmanae

Provisionally accepted
  • Temasek Life Sciences Laboratory, Singapore, Singapore

The final, formatted version of the article will be published soon.

    Methanogenic archaea, or methanogens, are crucial in guts and rumens, consuming hydrogen, carbon dioxide, and other fermentation products. While the molecular interactions with other microorganisms are not fully understood, genomic sequences provide clues. The first genome sequences of human gut methanogens, Methanosphaera stadtmanae and Methanobrevibacter smithii, revealed genes encoding adhesin-like proteins (ALPs). These proteins were also found in other gut and rumen methanogens, but their characteristics and functions remain largely unknown. This study analyses the ALP repertoire of M. stadtmanae and M. smithii, using AI-guided protein structure predictions of unique ALP domains. Both genomes encode more than 40 ALPs each, comprising over 10% of their genomes. ALPs contain repetitive sequences, many unmatched in protein domain databases. We present unique sequence signatures of conserved ABD repeats in ALPs and propose a classification based on domain architecture. Our study offers insights into ALP features and how methanogens may interact with other microorganisms.

    Keywords: adhesins, Methanogens, Adhesin-like proteins (ALPs), Archaeal Big, Gut micobiome

    Received: 12 Jul 2024; Accepted: 03 Sep 2024.

    Copyright: © 2024 Gupta and Seedorf. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

    * Correspondence: Henning Seedorf, Temasek Life Sciences Laboratory, Singapore, Singapore

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