The Leptospiral Major Outer Membrane Protein LipL32 Is a Lipoprotein Expressed during Mammalian Infection

Haake, David A.; Chao, Garlo; Zuerner, Richard L.; Barnett, Jeanne K.; Barnett, Dean; Mazel, Mary; Matsunaga, James; Levett, Paul N.; Bolin, Carole A.

doi:10.1128/iai.68.4.2276-2285.2000

Cited by 396 publications

(466 citation statements)

References 35 publications

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“…Integral OMPs usually assume a ␤-barrel conformation (22), and 50 and 49 proteins were found in strains L550 and JB197, respectively, with potential to assume this conformation, including OmpLI, a proven transmembrane porin (23), and TonB-and TolC-related proteins (Table 5, which is published as supporting information on the PNAS web site). Lipoproteins activate host cells to induce a proinflammatory response (24) and may elicit protective immunity (25). We identified 128 and 121 putative lipoproteins (not including pseudogenes) in strains L550 and JB197, respectively, including all known Leptospira lipoproteins and an OmpA homolog (Table 6, which is published as supporting information on the PNAS web site).…”

Section: Resultsmentioning

confidence: 99%

Genome reduction inLeptospira borgpeterseniireflects limited transmission potential

Bulach

Zuerner

Wilson

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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344

334

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Leptospirosis is one of the most common zoonotic diseases in the world, resulting in high morbidity and mortality in humans and affecting global livestock production. Most infections are caused by either Leptospira borgpetersenii or Leptospira interrogans, bacteria that vary in their distribution in nature and rely on different modes of transmission. We report the complete genomic sequences of two strains of L. borgpetersenii serovar Hardjo that have distinct phenotypes and virulence. These two strains have nearly identical genetic content, with subtle frameshift and point mutations being a common form of genetic variation. Starkly limited regions of synteny are shared between the large chromosomes of L. borgpetersenii and L. interrogans, probably the result of frequent recombination events between insertion sequences. The L. borgpetersenii genome is Ϸ700 kb smaller and has a lower coding density than L. interrogans, indicating it is decaying through a process of insertion sequence-mediated genome reduction. Loss of gene function is not random but is centered on impairment of environmental sensing and metabolite transport and utilization. These features distinguish L. borgpetersenii from L. interrogans, a species with minimal genetic decay and that survives extended passage in aquatic environments encountering a mammalian host. We conclude that L. borgpetersenii is evolving toward dependence on a strict host-to-host transmission cycle.genome sequence ͉ leptospirosis ͉ spirochete

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Section: Resultsmentioning

confidence: 99%

Genome reduction inLeptospira borgpeterseniireflects limited transmission potential

Bulach

Zuerner

Wilson

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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344

334

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“…Live L. interrogans serovar Copenhageni strain M-20 was treated with 25 μg/mL of proteinase K, and aliquots of the bacterial suspensions were obtained at 0, 30, 60, 120, and 240 minutes. The suspensions were centrifuged and resuspended bacteria were used to coat microplates, followed by incubation with polyclonal antibodies against each protein, including the controls, LipL32 and DnaK, for outer 34 and cytoplasmic 35 protein, respectively. Proteins Lsa26, Lsa23, and Lsa36 were susceptible to protease treatment and showed statistically significant values after 60 minutes of incubation, when compared with 0 min control samples ( Figure 5).…”

Section: Resultsmentioning

confidence: 99%

“…Suspensions were subsequently centrifuged at 11,500 + g for 5 minutes, washed twice with PBS ls, and resuspended in PBS ls for an ELISA with antibodies against Lsa26, Lsa23, Lsa36, LipL32, and DnaK, as described below. LipL32 and DnaK are membrane 34 and cytoplasmic 35 leptospiral proteins and were used in our experiment as positive and negative controls, respectively.…”

Section: Introductionmentioning

confidence: 99%

Characterization of Three Novel Adhesins of Leptospira interrogans

Siqueira¹,

Atzingen²,

Alves³

et al. 2013

The American Society of Tropical Medicine and Hygiene

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Abstract. We report cloning, expression, purification, and characterization of three predicted leptospiral membrane proteins (LIC11360, LIC11009, and LIC11975). In silico analysis and proteinase K accessibility data suggest that these proteins might be surface exposed. We show that proteins encoded by LIC11360, LIC11009 and LIC11975 genes interact with laminin in a dose-dependent and saturable manner. The proteins are referred to as leptospiral surface adhesions 23, 26, and 36 (Lsa23, Lsa26, and Lsa36), respectively. These proteins also bind plasminogen and generate active plasmin. Attachment of Lsa23 and Lsa36 to fibronectin occurs through the involvement of the 30-kDa and 70-kDa heparin-binding domains of the ligand. Dose-dependent, specific-binding of Lsa23 to the complement regulator C4BP and to a lesser extent, to factor H, suggests that this protein may interfere with the complement cascade pathways. Leptospira spp. may use these interactions as possible mechanisms during the establishment of infection.

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“…LipL32 is also the major immunoreactive OMP shared by diverse serogroups (5). These characteristics suggest that LipL32 is useful for development of new leptospirosis serological diagnosis approaches (18).…”

Section: Discussionmentioning

confidence: 99%

Leptospirosis serosurvey in bovines from Brazilian Pantanal using IGG ELISA with recombinant protein LipL32 and microscopic agglutination test

Tomich¹,

Bomfim²,

Koury³

et al. 2007

Braz. J. Microbiol.

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This investigation was carried out in Brazilian Pantanal: region with important biodiversity. This region's climatic conditions, hydrology and geomorphology as well as the existence of great variety of wild species favor the maintenance of the Leptospira in the environment. The aim of this study was to evaluate IgG ELISA with recombinant protein LipL32 in comparison with microscopic agglutination test (MAT) and additionally contribute to the knowledge of the distribution of the one of most important worldwide zoonotic infection, assessing the seropositivity of bovine leptospirosis in beef cattle herds of Brazilian Pantanal, an important ecological preserved area, where cattle constitute not only the most important economic resource but also the major activity compatible of the conservation of natural resource of the region. Out of 282 samples of cattle serum analyzed, 143 (50.71%) were positive in MAT. The serovar Hardjo (genotypic Hardjoprajitno and Hardjobovis), Wolffi and Ballum showed the largest frequency of reactive samples. In the IgG ELISA rLipL32, 161 samples (57.09%) were positive. This result was higher than obtained by MAT (p<0.001). The sensitivity of the ELISA test was 99.30% and the specificity was 86.33%, based on the MAT. This test was shown to be a more sensitive, specific and accurate test for the diagnosis of bovine leptospirosis compared to the MAT.

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The Leptospiral Major Outer Membrane Protein LipL32 Is a Lipoprotein Expressed during Mammalian Infection

Cited by 396 publications

References 35 publications

Genome reduction inLeptospira borgpeterseniireflects limited transmission potential

Genome reduction inLeptospira borgpeterseniireflects limited transmission potential

Characterization of Three Novel Adhesins of Leptospira interrogans

Leptospirosis serosurvey in bovines from Brazilian Pantanal using IGG ELISA with recombinant protein LipL32 and microscopic agglutination test

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