Genome features of Leptospira interrogans serovar Copenhageni

Nascimento, Ana L. T. O.; Verjovski-Almeida, Sérgio; Sluys, Marie‐Anne Van; Monteiro-Vitorello, Cláudia Barros; Camargo, Luís Eduardo Aranha; Digiampietri, Luciano Antônio; Harstkeerl, Rudy A.; Ho, Paulo Lee; Marques, Marilis V.; Oliveira, Mariana Cabral de; Setúbal, João Carlos; Haake, David A.; Martins, Elizabeth A. L.

doi:10.1590/s0100-879x2004000400003

Cited by 203 publications

(232 citation statements)

References 63 publications

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“…Two transmembrane channels, H + -PPase and phosphate sodium symporter, both contained IPAV-specific SNV mutations, but the latter had a dramatic decrease in its protein abundance in IPAV. We also observed high levels of expression of virulence-related proteins belonging to the TolC family and some ABC transporters, which interact in combination to facilitate the efflux of cytoplasmic components [64]. In addition, a TonB-like protein and a TonB-dependent outer membrane receptor were upregulated in strain 56601, indicating the intensified ability to uptake certain iron sources [65] from the environment to help its growth.…”

Section: Discussionmentioning

confidence: 91%

Comparative proteogenomic analysis of the Leptospira interrogans virulence-attenuated strain IPAV against the pathogenic strain 56601

et al. 2011

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The virulence-attenuated Leptospira interrogans serovar Lai strain IPAV was derived by prolonged laboratory passage from a highly virulent ancestral strain isolated in China. We studied the genetic variations of IPAV that render it avirulent via comparative analysis against the pathogenic L. interrogans serovar Lai strain 56601. The complete genome sequence of the IPAV strain was determined and used to compare with, and then rectify and reannotate the genome sequence of strain 56601. Aside from their highly similar genomic structure and gene order, a total of 33 insertions, 53 deletions and 301 single-nucleotide variations (SNVs) were detected throughout the genome of IPAV directly affecting 101 genes, either in their 5′ upstream region or within their coding region. Among them, the majority of the 44 functional genes are involved in signal transduction, stress response, transmembrane transport and nitrogen metabolism. Comparative proteomic analysis based on quantitative liquid chromatography (LC)-MS/MS data revealed that among 1 627 selected pairs of orthologs, 174 genes in the IPAV strain were upregulated, with enrichment mainly in classes of energy production and lipid metabolism. In contrast, 228 genes in strain 56601 were upregulated, with the majority enriched in the categories of protein translation and DNA replication/repair. The combination of genomic and proteomic approaches illustrated that altered expression or mutations in critical genes, such as those encoding a Ser/Thr kinase, carbon-starvation protein CstA, glutamine synthetase, GTP-binding protein BipA, ribonucleotidediphosphate reductase and phosphate transporter, and alterations in the translational profile of lipoproteins or outer membrane proteins are likely to account for the virulence attenuation in strain IPAV.

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Section: Discussionmentioning

confidence: 91%

Comparative proteogenomic analysis of the Leptospira interrogans virulence-attenuated strain IPAV against the pathogenic strain 56601

et al. 2011

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“…The genes LIC11009, LIC11360, and LIC11975 were identified by analysis of the genome sequences of the chromosome I of L. interrogans serovar Copenhageni; each gene is present as a single copy. 7 The CDSs LIC11009, LIC11360, and LIC11975 are predicted to be outer membrane proteins based on PSORT 4 and for LIC11975 and LIC11009 also by CELLO 22 programs. No putative conserved domains have been detected by BLAST.…”

Section: Resultsmentioning

confidence: 99%

“…3 Our laboratory has been using bioinformatics software, such as PSORT 4 and LipoP, 5 to analyze genome sequences of L. interrogans serovar Copenhageni. 6,7 This approach, combined with gene cloning and protein expression and purification, has led to development of several leptospiral recombinant proteins that can be experimentally characterized. Some of these proteins were identified as novel leptospiral adhesins that might be involved in the first steps of host-Leptospira interaction.…”

Section: Introductionmentioning

confidence: 99%

“…17,18 In the present study, we report the characterization of three novel leptospiral proteins. The selected genes, LIC11009, LIC11360, and LIC11975, were identified in genome sequences of L. interrogans serovar Copenhageni 6,7 and predicted to encode for membrane proteins. We show that the recombinant proteins bind extracellular matrix (ECM) molecules and are referred to as leptospiral surface adhesions Lsa23 (rLIC11360), Lsa26 (rLIC11009), and Lsa36 (rLIC11975) (number indicates molecular mass of the protein).…”

Section: Introductionmentioning

confidence: 99%

“…Putative coding sequences (CDSs) LIC11009, LIC11360 and LIC11975 were identified in the L. interrogans serovar Copenhageni genome 6,7 and selected based on their cellular localization predicted by PSORT 4 (http://psort.nibb.ac.jp), and CELLO 22 (http://cello.life.nctu.edu.tw/) programs. Locations predicted by these programs are cytoplasmic, cytoplasmic membrane, periplasmic, outer membrane, and extracellular (by PSORT), and cytoplasmic, periplasmic, outer membrane, inner membrane, and extracellular (by CELLO).…”

Section: Introductionmentioning

confidence: 99%

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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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Evaluation of binding activities of a putative lipoprotein LIC_13355 of Leptospira spp.

Silva,

Takahashi,

Teixeira

et al. 2024

FEBS Open Bio

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Pathogenic Leptospira is the etiological cause of the zoonotic life‐threatening infection called leptospirosis. The disease is spread worldwide with higher risk in tropical regions. Although leptospirosis represents a burden to the health of humans and animals, the pathogenic mechanisms of Leptospira infection are yet to be clarified. Leptospirosis infection is multifactorial, involving functionally redundant proteins with the capability to invade, disseminate, and escape the host's immune response. In this work, we describe a putative lipoprotein encoded by the gene LIC_13355, genome annotated as hypothetical of unknown function. The coding sequence is conserved among pathogenic Leptospira spp. with high percentage of coverage and identity. The recombinant protein, rLIC_13355, was expressed in Escherichia coli host system in its insoluble form. The circular dichroism spectrum of the refolded protein showed it containing a mixture of secondary structures. rLIC_13355 interacts with extracellular matrix (ECM) component laminin and binds plasminogen (PLG), generating plasmin (PLA), thus possibly participating during the adhesion and dissemination processes. The rLIC_13355 has the ability to interact with Ea.hy926 and HMEC‐1 endothelial cells either in monolayer or suspension. The binding of rLIC_13355 with monolayer cells is dose‐dependent on protein concentration. Taken together, our data suggest that this is presumably an adhesion lipoprotein that may play diverse roles in host–Leptospira interactions by mediating the interaction with host components and with endothelial cell.

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Genome features of Leptospira interrogans serovar Copenhageni

Cited by 203 publications

References 63 publications

Comparative proteogenomic analysis of the Leptospira interrogans virulence-attenuated strain IPAV against the pathogenic strain 56601

Comparative proteogenomic analysis of the Leptospira interrogans virulence-attenuated strain IPAV against the pathogenic strain 56601

Characterization of Three Novel Adhesins of Leptospira interrogans

Evaluation of binding activities of a putative lipoprotein LIC_13355 of Leptospira spp.

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