The OmpA-like protein Loa22 is essential for leptospiral virulence

Pathogenic mechanisms of Leptospira interrogans, the causal agent of leptospirosis, remain largely unknown. This is mainly due to the lack of tools for genetic manipulations of pathogenic species. In this study, we characterized a mutant obtained by insertion of the transposon Himar1 into a gene enc...

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Published in:PLoS pathogens 2007-07, Vol.3 (7), p.e97-e97
Main Authors: Ristow, Paula, Bourhy, Pascale, da Cruz McBride, Flávia Weykamp, Figueira, Claudio Pereira, Huerre, Michel, Ave, Patrick, Girons, Isabelle Saint, Ko, Albert I, Picardeau, Mathieu
Format: Article
Language:English
Subjects:
Animals
Bacteria
Bacterial Outer Membrane Proteins - physiology
Base Sequence
Blood lipoproteins
Cricetinae
Developing countries
Disease Models, Animal
DNA Transposable Elements
Eubacteria
Experiments
Gene expression
Gene mutations
Genes
Genetic engineering
Genomes
Guinea Pigs
Hogs
Immunization
Infections
Kidney - metabolism
Kidney - microbiology
Kidney - pathology
LDCs
Leptospira interrogans - metabolism
Leptospira interrogans - pathogenicity
Leptospirosis
Leptospirosis - microbiology
Lipoproteins
Liver - metabolism
Liver - microbiology
Liver - pathology
Lung - metabolism
Lung - microbiology
Lung - pathology
Medical research
Medicine, Experimental
Microbiology
Molecular Sequence Data
Mortality
Pathogenesis
Protein Structure, Tertiary
Proteins
Proteolipids
Pyrophosphates
Spleen - metabolism
Spleen - microbiology
Spleen - pathology
Virulence
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Picardeau, Mathieu
description Pathogenic mechanisms of Leptospira interrogans, the causal agent of leptospirosis, remain largely unknown. This is mainly due to the lack of tools for genetic manipulations of pathogenic species. In this study, we characterized a mutant obtained by insertion of the transposon Himar1 into a gene encoding a putative lipoprotein, Loa22, which has a predicted OmpA domain based on sequence identity. The resulting mutant did not express Loa22 and was attenuated in virulence in the guinea pig and hamster models of leptospirosis, whereas the genetically complemented strain was restored in Loa22 expression and virulence. Our results show that Loa22 was expressed during host infection and exposed on the cell surface. Loa22 is therefore necessary for virulence of L. interrogans in the animal model and represents, to our knowledge, the first genetically defined virulence factor in Leptospira species.
doi_str_mv 10.1371/journal.ppat.0030097
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subjects Animals
Bacteria
Bacterial Outer Membrane Proteins - physiology
Base Sequence
Blood lipoproteins
Cricetinae
Developing countries
Disease Models, Animal
DNA Transposable Elements
Eubacteria
Experiments
Gene expression
Gene mutations
Genes
Genetic engineering
Genomes
Guinea Pigs
Hogs
Immunization
Infections
Kidney - metabolism
Kidney - microbiology
Kidney - pathology
LDCs
Leptospira interrogans - metabolism
Leptospira interrogans - pathogenicity
Leptospirosis
Leptospirosis - microbiology
Lipoproteins
Liver - metabolism
Liver - microbiology
Liver - pathology
Lung - metabolism
Lung - microbiology
Lung - pathology
Medical research
Medicine, Experimental
Microbiology
Molecular Sequence Data
Mortality
Pathogenesis
Protein Structure, Tertiary
Proteins
Proteolipids
Pyrophosphates
Spleen - metabolism
Spleen - microbiology
Spleen - pathology
Virulence
title The OmpA-like protein Loa22 is essential for leptospiral virulence
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