Methylation and in vivo expression of the surface-exposed Leptospira interrogans outer-membrane protein OmpL32
Eshghi, Azad and Pinne, Marija and Haake, David A. and Zuerner, Richard L. and Frank, Ami and Cameron, Caroline E.,, 158, 622-635 (2012),
doi = https://doi.org/10.1099/mic.0.054767-0,
publicationName = Microbiology Society,
issn = 1350-0872,
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.,
language=,
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