ArticleMicrobiology (Reading, England)2012
Methylation and in vivo expression of the surface-exposed Leptospira interrogans outer-membrane protein OmpL32.
Article in Microbiology (Reading, England), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 28 citations in OpenAlex.
- Article
- Surface proteomics and label-free quantification of Leptospira interrogans serovar Pomona.PLoS neglected tropical diseases · 2021Article
- Needle lost in the haystack: multiple reaction monitoring fails to detectF1000Research · 2018Article
- Virulence of the zoonotic agent of leptospirosis: still terra incognita?Nature reviews. Microbiology · 2017Review
- Reverse Vaccinology: An Approach for Identifying Leptospiral Vaccine Candidates.International journal of molecular sciences · 2017Review
- Pathogenic Leptospires Modulate Protein Expression and Post-translational Modifications in Response to Mammalian Host Signals.Frontiers in cellular and infection microbiology · 2017Article
- Multiple Posttranslational Modifications of Leptospira biflexa Proteins as Revealed by Proteomic Analysis.Applied and environmental microbiology · 2016Article
- Pathogenic Leptospira interrogans exoproteins are primarily involved in heterotrophic processes.Infection and immunity · 2015Article
- An O-Methyltransferase Is Required for Infection of Tick Cells by Anaplasma phagocytophilum.PLoS pathogens · 2015Article
- The leptospiral outer membrane.Current topics in microbiology and immunology · 2015Review
- Post-translational modification of LipL32 during Leptospira interrogans infection.PLoS neglected tropical diseases · 2014Article
- LipL32 Is a Subsurface Lipoprotein of Leptospira interrogans: presentation of new data and reevaluation of previous studies.PloS one · 2013Article
- Leptospiral outer membrane protein microarray, a novel approach to identification of host ligand-binding proteins.Journal of bacteriology · 2012Article
- Arming the troops: Post-translational modification of extracellular bacterial proteins.Science progressReview
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Authors and funding
6 authors at 5 institutions in 2 countries.
Funding
Abstract
Recent studies have revealed that bacterial protein methylation is a widespread post-translational modification that is required for virulence in selected pathogenic bacteria. In particular, altered methylation of outer-membrane proteins has been shown to modulate the effectiveness of the host immune response. In this study, 2D gel electrophoresis combined with MALDI-TOF MS identified a Leptospira interrogans serovar Copenhageni strain Fiocruz L1-130 protein, corresponding to ORF LIC11848, which undergoes extensive and differential methylation of glutamic acid residues. Immunofluorescence microscopy implicated LIC11848 as a surface-exposed outer-membrane protein, prompting the designation OmpL32. Indirect immunofluorescence microscopy of golden Syrian hamster liver and kidney sections revealed expression of OmpL32 during colonization of these organs. Identification of methylated surface-exposed outer-membrane proteins, such as OmpL32, provides a foundation for delineating the role of this post-translational modification in leptospiral virulence.
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