ArticleJournal of bacteriology2012
Two protein lysine methyltransferases methylate outer membrane protein B from Rickettsia.
Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
18 citing papers in PubMed, 27 citations in OpenAlex.
- Innate immune responses to Rickettsia: emerging themes and contrasts between species.Current opinion in microbiology · 2026Review
- Obligate intracellular bacteria and host cell death pathways-the matter of life and death.Cell and tissue research · 2025Review
- A new target of multiple lysine methylation in bacteria.Journal of bacteriology · 2025Article
- Critical roles ofInfection and immunity · 2024Article
- The Mycobacterium tuberculosis methyltransferase Rv2067c manipulates host epigenetic programming to promote its own survival.Nature communications · 2023Article
- Methylation of PhoP by CheR RegulatesmBio · 2021Article
- Lysine methylation shields an intracellular pathogen from ubiquitylation and autophagy.Science advances · 2021Article
- The enigmatic biology of rickettsiae: recent advances, open questions and outlook.Pathogens and disease · 2021Review
- Characterization of Lysine Monomethylome and Methyltransferase in Model Cyanobacterium Synechocystis sp. PCC 6803.Genomics, proteomics & bioinformatics · 2020Article
- The purification of reduced β2-glycoprotein I showed its native activity in vitro.Lipids in health and disease · 2017Article
- Structural Insights into Substrate Recognition and Catalysis in Outer Membrane Protein B (OmpB) by Protein-lysine Methyltransferases from Rickettsia.The Journal of biological chemistry · 2016Article
- The METTL20 Homologue from Agrobacterium tumefaciens Is a Dual Specificity Protein-lysine Methyltransferase That Targets Ribosomal Protein L7/L12 and the β Subunit of Electron Transfer Flavoprotein (ETFβ).The Journal of biological chemistry · 2016Article
- Secretome of obligate intracellular Rickettsia.FEMS microbiology reviews · 2015Review
- An O-Methyltransferase Is Required for Infection of Tick Cells by Anaplasma phagocytophilum.PLoS pathogens · 2015Article
- The functional diversity of protein lysine methylation.Molecular systems biology · 2014Review
- Multimethylation of Rickettsia OmpB catalyzed by lysine methyltransferases.The Journal of biological chemistry · 2014Article
- Recent molecular insights into rickettsial pathogenesis and immunity.Future microbiology · 2013Review
- Arming the troops: Post-translational modification of extracellular bacterial proteins.Science progressReview
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Rickettsia prowazekii, the etiologic agent of epidemic typhus, is a potential biological threat agent. Its outer membrane protein B (OmpB) is an immunodominant antigen and plays roles as protective envelope and as adhesins. The observation of the correlation between methylation of lysine residues in rickettsial OmpB and bacterial virulence has suggested the importance of an enzymatic system for the methylation of OmpB. However, no rickettsial lysine methyltransferase has been characterized. Bioinformatic analysis of genomic DNA sequences of Rickettsia identified putative lysine methyltransferases. The genes of the potential methyltransferases were synthesized, cloned, and expressed in Escherichia coli, and expressed proteins were purified by nickel-nitrilotriacetic acid (Ni-NTA) affinity chromatography. The methyltransferase activities of the purified proteins were analyzed by methyl incorporation of radioactively labeled S-adenosylmethionine into recombinant fragments of OmpB. Two putative recombinant methyltransferases (rRP789 and rRP027-028) methylated recombinant OmpB fragments. The specific activity of rRP789 is 10- to 30-fold higher than that of rRP027-028. Western blot analysis using specific antibodies against trimethyl lysine showed that both rRP789 and rRP027-028 catalyzed trimethylation of recombinant OmpB fragments. Liquid chromatography-tandem mass spectrometry (LC/MS-MS) analysis showed that rRP789 catalyzed mono-, di-, and trimethylation of lysine, while rRP027-028 catalyzed exclusively trimethylation. To our knowledge, rRP789 and rRP027-028 are the first biochemically characterized lysine methyltransferases of outer membrane proteins from Gram-negative bacteria. The production and characterization of rickettsial lysine methyltransferases provide new tools to investigate the mechanism of methylation of OmpB, effects of methylation on the structure and function of OmpB, and development of methylated OmpB-based diagnostic assays and vaccine candidates.
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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.