Search bioRxiv⌕ Search

bioRxiv · 10.1101/2025.06.24.661241

Integrative microbiome- and metatranscriptome-based analyses reveal diagnostic biomarkers for peri-implantitis

Abstract

Peri-implantitis is a severe biofilm-associated infection of the tissues around dental implants that increases the risk of implant failure. The prognosis of peri-implantitis treatment is compromised by the resistance of well-organized and mature bacterial biofilms. Thus, early diagnosis of a pathogenic biofilm would enable treatment at a prognostically favourable stage. However, relatively little is known about how the microbial constitution of the biofilm changes during disease development. The aim of this cross-sectional study was therefore to identify peri-implant taxonomic and functional biomarkers that reliably indicate peri-implantitis using paired data from full length 16S rRNA gene amplicon sequencing (full-16S) and metatranscriptomics (RNAseq). Disease signatures were identified using 24 healthy and 24 peri-implantitis-associated biofilm samples from 32 patients. The taxonomic measurements were validated with 68 additional full-16S samples from another 40 patients. Both full-16S and RNAseq revealed significant differences between healthy and peri-implantitis samples, with respect to both the microbiome and functional profiles. A shift from aerotolerant Gram-positive bacteria to anaerobic Gram-negative bacteria was observed in peri-implantitis. Distinct metabolic pathways were expressed in healthy and peri-implantitis samples. Our results, based on paired taxonomic and functional profiles, provide for the first time important insights into the complex peri-implant biofilm ecology related to amino acid metabolism. Integrating taxonomic and functional information improved the predictive ability (AUC = 0.85) of the machine learning models and revealed diagnostic biomarkers with large effect sizes (Cohens d > 0.8). Primary biomarkers included health-associated Streptococcus, Rothia species and enzymes associated with peri-implantitis (urocanate hydratase, tripeptide aminopeptidase, NADH:ubiquinone reductase, phosphoenolpyruvate carboxykinase and polyribonucleotide nucleotidyltransferase - mostly expressed by Fusobacteriia and Bacteroidia). Thus, biofilm profiling at these two molecular levels reveals highly predictive disease biomarkers and provide the basis for developing early diagnostics and individualized therapy approaches for peri-implant diseases.

Source connections

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Joshi, A. A., Szafranski, S. P., Steglich, M., Yang, I., Qu, T., Xiao, X., Behrens, W., Grischke, J., Haeussler, S., Stiesch, M.. 2025-06-24. Integrative microbiome- and metatranscriptome-based analyses reveal diagnostic biomarkers for peri-implantitis. https://doi.org/10.1101/2025.06.24.661241

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related preprints

pTRIP, a novel integration plasmid for Listeria monocytogenes

In the past decades, several tools to genetically modify the human pathogen Listeria monocytogenes were developed. Here, we constructed a new integrative plasmid system for L. monocytogenes named pTRIP, for treB insertion plasmid. pTRIP is a vector which stably integrates into the treB locus of the wild type EGD-e. This locus encodes the sole trehalose-specific EIIB and EIIC component of a phosphotransferase system. Successful integration leads to the disruption of treB and thus, to an inability of the resulting L. monocytogenes strains to grow on trehalose as sole carbon source. Due to integration through double homologous recombination, it is the first integrative system which does not require antibiotic selection pressure. To assess functionality of the pTRIP system, prfA and its native promoter region were integrated into the treB locus of a {Delta}prfA strain. Complementation was confirmed in 78% of the isolated clones, indicating successful integration of prfA into the treB locus. We further constructed derivatives of pTRIP harboring the constitutive Pp60 (pTRIP1) and the inducible Prha (pTRIP2) promoter to further expand application possibilities. Microscopic analyses confirmed the functionality of both promoter constructs and showed dose-dependent induction for Prha. pTRIP is an efficient tool for stable gene expression as well as functional studies and expands genetic modification possibilities for L. monocytogenes.

microbiology↗

A rational design strategy and validation for protease-resistant fusion-inhibitor antiviral peptides

Peptide-based fusion inhibitors are promising pharmaceuticals in the fight against enveloped viruses relying on membrane fusion for host infection. However, peptide therapeutic applications have long been hindered by their poor stability in vivo. Here, we discovered that peptide inhibitors with the wildtype sequence of the heptad repeat 2 (HR2) domain of the SARS-CoV-2 spike protein are efficiently cleaved by Transmembrane Protease, Serine 2 (TMPRSS2), a key protease involved in the SARS-CoV-2 virus-cell fusion pathway. We then identified the corresponding cleavage sites and designed three protease-resistant peptides using ranking based on deep mutational scanning and natural occurrence. The three candidates all exhibit inhibitory activity in a cell-cell fusion assay. A high-resolution cryo-EM structure of the top candidate, HR2-NHN, bound to its HR1 target reveals the molecular basis for its potent activity. The top candidate of the cell-based screening assay significantly improved efficacy relative to the wildtype peptide when administered 12 h before infection in both an authentic virus-cell infection assay and a mouse assay. More broadly, our results suggest that the design strategies for protease-resistant peptides could be applied to a broad spectrum of other enveloped viruses and pave the way for the development of safe, prophylactic antivirals that can be administered before exposure.

microbiology↗

Host soluble inositol phosphate signaling promotes coronavirus replication

Coronaviruses rely extensively on host pathways for replication, making host-directed therapies an attractive strategy for broad-spectrum antivirals with reduced risk of viral resistance. Here we identify the host soluble inositol phosphate pathway as a previously unrecognized dependency for coronavirus infection. Genetic or pharmacologic inhibition of several kinases in this pathway markedly suppresses replication of both alpha- and betacoronaviruses, while increasing pathway activity promotes viral replication. We developed UNC7844, a potent multi-target inhibitor of these kinases, which reduces coronavirus replication by more than four orders of magnitude in cultured cells and suppresses coronavirus infection in mice. Mechanistically, UNC7844 suppresses inositol (pyro)phosphates production, disrupts phosphoinositide homeostasis, and impairs late endosomal dynamics, blocking early post-entry steps required for viral genome release and replication. Together, our findings establish the soluble inositol (pyro)phosphate pathway as an important regulator of coronavirus infection and highlight its inhibition as a promising host-directed antiviral strategy.

microbiology↗