ArticleJournal of bacteriology2005
Trimeric structure of major outer membrane proteins homologous to OmpA in Porphyromonas gingivalis.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 43 citations in OpenAlex.
- Characterization of a Treponema denticola ATCC 35405 mutant strain with mutation accumulation, including a lack of phage-derived genes.PloS one · 2022Article
- Structural and functional insights into oligopeptide acquisition by the RagAB transporter from Porphyromonas gingivalis.Nature microbiology · 2020Article
- OmpA-Like Proteins ofJournal of pathogens · 2018Article
- Article
- Role of OmpA2 surface regions of Porphyromonas gingivalis in host-pathogen interactions with oral epithelial cells.MicrobiologyOpen · 2017Article
- In Silico Structure and Sequence Analysis of Bacterial Porins and Specific Diffusion Channels for Hydrophilic Molecules: Conservation, Multimericity and Multifunctionality.International journal of molecular sciences · 2016Article
- Characterization of wheat germ agglutinin lectin-reactive glycosylated OmpA-like proteins derived from Porphyromonas gingivalis.Infection and immunity · 2014Article
- Article
- Characterization of Treponema denticola mutants defective in the major antigenic proteins, Msp and TmpC.PloS one · 2014Article
- Spanin function requires subunit homodimerization through intermolecular disulfide bonds.Molecular microbiology · 2013Article
- E-selectin mediates Porphyromonas gingivalis adherence to human endothelial cells.Infection and immunity · 2012Article
- Article
- Characterization of an OmpA-like outer membrane protein of the acidophilic iron-oxidizing bacterium, Acidithiobacillus ferrooxidans.Extremophiles : life under extreme conditions · 2011Article
- Selective sorting of cargo proteins into bacterial membrane vesicles.The Journal of biological chemistry · 2011Article
- Evidence for a role of vertebrate Disp1 in long-range Shh signaling.Development (Cambridge, England) · 2010Article
- Anchoring and length regulation of Porphyromonas gingivalis Mfa1 fimbriae by the downstream gene product Mfa2.Microbiology (Reading, England) · 2009Article
- Identification of a gingipain-sensitive surface ligand of Porphyromonas gingivalis that induces Toll-like receptor 2- and 4-independent NF-kappaB activation in CHO cells.Infection and immunity · 2009Article
- An OmpA family protein, a target of the GinI/GinR quorum-sensing system in Gluconacetobacter intermedius, controls acetic acid fermentation.Journal of bacteriology · 2008Article
- Effects of various growth conditions in a chemostat on expression of virulence factors in Porphyromonas gingivalis.Applied and environmental microbiology · 2006Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The major outer membrane proteins Pgm6 (41 kDa) and Pgm7 (40 kDa) of Porphyromonas gingivalis ATCC 33277 are encoded by open reading frames pg0695 and pg0694, respectively, which form a single operon. Pgm6 and Pgm7 (Pgm6/7) have a high degree of similarity to Escherichia coli OmpA in the C-terminal region and are predicted to form eight-stranded beta-barrels in the N-terminal region. By sodium dodecyl sulfate-polyacrylamide gel electrophoresis, Pgm6/7 appear as bands with apparent molecular masses of 40 and 120 kDa, with and without a reducing agent, suggesting a monomer and trimer, respectively. To verify the predicted trimeric structure and function of Pgm6/7, we constructed three mutants with pg0695, pg0694, or both deleted. The double mutant produced no Pgm6/7. The single-deletion mutants appeared to contain less Pgm7 and Pgm6 and to form homotrimers that migrated slightly faster (115 kDa) and slower (130 kDa), respectively, than wild-type Pgm6/7 under nonreducing conditions. N-terminal amino acid sequencing and mass spectrometry analysis of partially digested Pgm6/7 detected only fragments from Pgm6 and Pgm7. Two-dimensional, diagonal electrophoresis and chemical cross-linking experiments with or without a reducing agent clearly showed that Pgm6/7 mainly form stable heterotrimers via intermolecular disulfide bonds. Furthermore, growth retardation and arrest of the three mutants and increased permeability of their outer membranes indicated that Pgm6/7 play an important role in outer membrane integrity. Based on results of liposome swelling experiments, these proteins are likely to function as a stabilizer of the cell wall rather than as a major porin in this organism.
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