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Gene expression of wild-type Porphyromnas gingivalis 33277 vs the transposon-mutant, J5-c5.

ABSTRACT: The P. gingivalis 33277 transposon mutant J5-c5, isolated in this study, was demonstrated to exhibit a lipid A deacylase phenotype. The mutant is unable to deacylate lipid A, which confers to it, in stark contrast to wild-type, an inability to evade the powerful TLR4 innate immune response. The mutant was shown to contain five transposons. In order to determine the affected gene responsible for this phenotype, we took the approach of comparing gene expression between wild-type and J5-c5 transposon mutant. RNA was extracted from three separate biological samples of each strain and RNAseq performed using Illumina’s HiSeq sequencing facility at the University of Washington Center for Precision Diagnostics. RNAseq data was analyzed closely following guidance outlined in Law et al (doi:10.12688/f1000research.9005.2).

ORGANISM(S): Porphyromonas gingivalis ATCC 33277

PROVIDER: GSE122289 | GEO | 2019/04/09

REPOSITORIES: GEO

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Gene expression of wild-type Porphyromnas gingivalis 33277 vs the transposon-mutant, J5-c5.

Project description:Gene expression of wild-type Porphyromnas gingivalis 33277 vs the transposon-mutant, J5-c5.

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The distinct immune-stimulatory capacities of Porphyromonas gingivalis strains 381 and 33277 are determined by the fimB allele and gingipain activity

Project description:The genomes of P. gingivalis strains 33277 and 381 are highly related phylogenetically. However, 33277 displays a reduced capacity to stimulate HEK cell TLR2-dependent signaling and THP-1 cell-dependent IL-1β production compared to 381, suggesting strain-specific differences in the expression of one or more bacterial immune-modulatory cell surface molecules. Genomic sequencing identified a single nucleotide polymorphism in the 33277 fimB allele (A>T), encoding a truncated FimB protein, relative to the 381 fimB allele. Gene exchange experiments indicated that the 33277 fimB allele contributes to the reduced immune-stimulatory capacity of this strain. Transcriptomic analyses determined that multiple genes related to carboxy-terminal domain (CTD) family proteins, including the gingipains, were upregulated in strain 33277 relative to strain 381. A gingipain substrate degradation assay confirmed that cell surface gingipain activity is higher in 33277; and an isogenic mutant strain deficient for the gingipains exhibited an increased capacity to activate TLR2 signaling and induce IL-1β production. Furthermore, 33277 and 381 isogenic mutant strains devoid of CTD cell surface proteins displayed increased immune-stimulatory capacities compared to the wild-type parental strains, confirming an immune-suppressive role for the gingipains. Collectively, our data indicate that the combination of an intact fimB allele and limited cell surface gingipain expression in strain 381 contributes to its relatively potent immune-stimulatory activity. Conversely, a defective fimB allele and high levels of cell surface gingipains reduce the capacity of strain 33277 to elicit host cell innate immune responses.

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