title: Methylation and in vivo expression of the surface-exposed Leptospira interrogans outer-membrane protein OmpL32.
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.
authors.affiliation: Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC, Canada.
authors.forename: Azad
authors.initials: A
authors.lastname: Eshghi
authors.affiliation: Department of Medicine, David Geffen School of Medicine at University of California Los Angeles, Los Angeles, CA, USA.|Research Service, 151, Veterans Affairs Greater Los Angeles Healthcare System, Los Angeles, CA, USA.
authors.forename: Marija
authors.initials: M
authors.lastname: Pinne
authors.affiliation: Division of Infectious Diseases, 111F, Veterans Affairs Greater Los Angeles Healthcare System, Los Angeles, CA, USA.|Department of Medicine, David Geffen School of Medicine at University of California Los Angeles, Los Angeles, CA, USA.
authors.forename: David A
authors.initials: DA
authors.lastname: Haake
authors.affiliation: Infectious Bacterial Diseases Research Unit, National Animal Disease Center (NADC), Agricultural Research Service (ARS), United States Department of Agriculture (USDA), Ames, IA, USA.
authors.forename: Richard L
authors.initials: RL
authors.lastname: Zuerner
authors.affiliation: Infectious Bacterial Diseases Research Unit, National Animal Disease Center (NADC), Agricultural Research Service (ARS), United States Department of Agriculture (USDA), Ames, IA, USA.
authors.forename: Ami
authors.initials: A
authors.lastname: Frank
authors.affiliation: Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC, Canada.
authors.forename: Caroline E
authors.initials: CE
authors.lastname: Cameron
mesh_terms: D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism*; D006224:Cricetinae; D004195:Disease Models, Animal; D015180:Electrophoresis, Gel, Two-Dimensional; D015964:Gene Expression Regulation, Bacterial; D007668:Kidney / Q000382:microbiology; D007921:Leptospira interrogans / Q000235:genetics* / Q000378:metabolism*; D007922:Leptospirosis / Q000382:microbiology; D008099:Liver / Q000382:microbiology; D008745:Methylation; D008856:Microscopy, Fluorescence; D018272:Porins / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D001426:Bacterial Proteins; C100900:OmpL protein, bacteria; D018272:Porins