Novel strain of Pseudoruminococcus massiliensis possesses traits important in gut adaptation and host-microbe interactions

Gut Microbes. 2022 Jan-Dec;14(1):2013761. doi: 10.1080/19490976.2021.2013761.

Abstract

Fecal microbiota transplantation (FMT) is an efficient treatment for recurrent Clostridioides difficile infection and currently investigated as a treatment for other intestinal and systemic diseases. Better understanding of the species potentially transferred in FMT is needed. We isolated from a healthy fecal donor a novel strain E10-96H of Pseudoruminococcus massiliensis, a recently described strictly anaerobic species currently represented only by the type strain. The whole genome sequence of E10-96H had over 98% similarity with the type strain. E10-96H carries 20 glycoside hydrolase encoding genes, degrades starch in vitro and thus may contribute to fiber degradation, cross-feeding of other species and butyrate production in the intestinal ecosystem. The strain carries pilus-like structures, harbors pilin genes in its genome and adheres to enterocytes in vitro but does not provoke a proinflammatory response. P. massiliensis seems to have commensal behavior with the host epithelium, and its role in intestinal ecology should be studied further.

Keywords: FMT; Pseudoruminococcus; adhesion; gut microbiota; next-generation probiotic; pili; starch degradation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptation, Physiological
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Butyrates / metabolism
  • Firmicutes / classification
  • Firmicutes / genetics
  • Firmicutes / isolation & purification*
  • Firmicutes / physiology*
  • Gastrointestinal Microbiome
  • Genome, Bacterial
  • Glycoside Hydrolases / genetics
  • Glycoside Hydrolases / metabolism
  • Host Microbial Interactions
  • Humans
  • Intestines / microbiology*

Substances

  • Bacterial Proteins
  • Butyrates
  • Glycoside Hydrolases

Grants and funding

This work was supported by the Academy of Finland (323156) and Sigrid Juselius Foundation, Finland. Open access funded by Helsinki University Library.