ArticleMicrobiologyOpen2017
Role of OmpA2 surface regions of Porphyromonas gingivalis in host-pathogen interactions with oral epithelial cells.
Article in MicrobiologyOpen, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 17 citations in OpenAlex.
- An Oxygen-Releasing Mouthwash Reduces Porphyromonas gingivalis Biofilm and Suppresses fimA and hagA Expression.International dental journal · 2026Article
- Article
- Review
- Illuminating the oral microbiome: cellular microbiology.FEMS microbiology reviews · 2023Article
- A Germin-Like Protein GLP1 of Legumes Mediates Symbiotic Nodulation by Interacting with an Outer Membrane Protein of Rhizobia.Microbiology spectrum · 2023Article
- Characterization of the O-Glycoproteome of Porphyromonas gingivalis.Microbiology spectrum · 2022Article
- Mechanisms of vascular damage by systemic dissemination of the oral pathogen Porphyromonas gingivalis.The FEBS journal · 2021Article
- Article
- Gingimaps: Protein Localization in the Oral PathogenMicrobiology and molecular biology reviews : MMBR · 2020Review
- Characterization ofMicrobiology (Reading, England) · 2019Article
- Inhibition of sialidase activity and cellular invasion by the bacterial vaginosis pathogen Gardnerella vaginalis.Archives of microbiology · 2018Article
- Role of OmpA2 surface regions of Porphyromonas gingivalis in host-pathogen interactions with oral epithelial cells.MicrobiologyOpen · 2017Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 3 countries.
Funding
Abstract
Outer membrane protein A (OmpA) is a key outer membrane protein found in Gram-negative bacteria that contributes to several crucial processes in bacterial virulence. In Porphyromonas gingivalis, OmpA is predicted as a heterotrimer of OmpA1 and OmpA2 subunits encoded by adjacent genes. Here we describe the role of OmpA and its individual subunits in the interaction of P. gingivalis with oral cells. Using knockout mutagenesis, we show that OmpA2 plays a significant role in biofilm formation and interaction with human epithelial cells. We used protein structure prediction software to identify extracellular loops of OmpA2, and determined these are involved in interactions with epithelial cells as evidenced by inhibition of adherence and invasion of P. gingivalis by synthetic extracellular loop peptides and the ability of the peptides to mediate interaction of latex beads with human cells. In particular, we observe that OmpA2-loop 4 plays an important role in the interaction with host cells. These data demonstrate for the first time the important role of P. gingivalis OmpA2 extracellular loops in interaction with epithelial cells, which may help design novel peptide-based antimicrobial therapies for periodontal disease.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.