Abstract:
:We discovered that Enterococcus faecium (E. faecium), a ubiquitous commensal bacterium, and its secreted peptidoglycan hydrolase (SagA) were sufficient to enhance intestinal barrier function and pathogen tolerance, but the precise biochemical mechanism was unknown. Here we show E. faecium has unique peptidoglycan composition and remodeling activity through SagA, which generates smaller muropeptides that more effectively activates nucleotide-binding oligomerization domain-containing protein 2 (NOD2) in mammalian cells. Our structural and biochemical studies show that SagA is a NlpC/p60-endopeptidase that preferentially hydrolyzes crosslinked Lys-type peptidoglycan fragments. SagA secretion and NlpC/p60-endopeptidase activity was required for enhancing probiotic bacteria activity against Clostridium difficile pathogenesis in vivo. Our results demonstrate that the peptidoglycan composition and hydrolase activity of specific microbiota species can activate host immune pathways and enhance tolerance to pathogens.
journal_name
Elifejournal_title
eLifeauthors
Kim B,Wang YC,Hespen CW,Espinosa J,Salje J,Rangan KJ,Oren DA,Kang JY,Pedicord VA,Hang HCdoi
10.7554/eLife.45343subject
Has Abstractpub_date
2019-04-10 00:00:00issn
2050-084Xpii
45343journal_volume
8pub_type
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