Arabidopsis thaliana
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA137787 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:Recognition of microbial patterns by host pattern recognition receptors is a key step in immune activation in multicellular eukaryotes. Peptidoglycans (PGN) are major components of bacterial cell walls and possess immunity-stimulating activities in metazoans and plants. Here, we show that PGN sensing in Arabidopsis thaliana requires three LysM domain proteins, LYM1, LYM3 and CERK1. A 24 DNA microarray study using toral RNA from three Arabidopsis mutants (lym1-1, lym3-1, cerk1-2) as well as wild type treated with water or peptidoglycan.
2011-11-10 | E-GEOD-28004 | biostudies-arrayexpress
Project description:Recognition of microbial patterns by host pattern recognition receptors is a key step in immune activation in multicellular eukaryotes. Peptidoglycans (PGN) are major components of bacterial cell walls and possess immunity-stimulating activities in metazoans and plants. Here, we show that PGN sensing in Arabidopsis thaliana requires three LysM domain proteins, LYM1, LYM3 and CERK1.
2011-11-10 | GSE28004 | GEO
Project description:Expression analysis of Arabidopsis ein2 and bak1 mutants treated with the elicitors elf18 and Pep2.
| PRJNA173680 | ENA
Project description:Bordetella pertussis, the etiologic agent of whooping cough, remains a serious public health concern despite widespread vaccination. Improved therapeutics and vaccines are urgently needed to treat and prevent pertussis disease. Host recognition of bacterial peptidoglycan (PGN), including B. pertussis extracellular PGN fragment tracheal cytotoxin (TCT), shapes the immune response to infection. Peptidoglycan recognition proteins (PGLYRPs) are a conserved family of innate immune molecules which bind bacterial PGN. While they function as immune signaling receptors in arthropods, PGLYRPs in mammals have thus far been primarily recognized for their bactericidal activity. Previously thought to function only as antimicrobial peptides in mammals, the immune modulatory roles of this family of peptidoglycan recognition proteins are beginning to gain greater appreciation. Peptidoglycan recognition protein 1 (PGLYRP1) is a secreted antimicrobial protein. However, its role in mammalian host defenses and immune signaling during infection with Gram-negative pathogens, such as B. pertussis, remain largely unknown. Here, we identify a dual role for PGLYRP1 in modulating host immune responses to B. pertussis. Using knockout mice, single-cell and bulk transcriptomics and functional assays, we show that PGLYRP1 has bactericidal activity against B. pertussis in vitro and promotes early bacterial control in vivo. PGLYRP1 also dampens inflammatory responses and impedes bacterial killing later in infection. Mechanistically, PGLYRP1 enhances nucleotide oligomerization domain (NOD)-1 signaling in response to TCT while suppressing NOD2- and triggering receptor expressed on myeloid cells-1 (TREM-1)-mediated inflammatory pathways. TCT-bound PGLYRP1 selectively impairs TREM-1 activation compared to PGNs from other bacteria, revealing a novel bacterial immune evasion strategy. These findings demonstrate that B. pertussis co-opts PGLYRP1 to temper inflammation and alter immune signaling, revealing a novel immune evasion mechanism of manipulating the availability and structure of their exogenous peptidoglycan, revealing implications for host-pathogen evolution, vaccine design and host-directed therapeutics.
2026-03-11 | GSE324217 | GEO
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