Expression and Distribution of Leptospiral Outer Membrane Components during Renal Infection of Hamsters

Barnett, Jeanne K.; Barnett, Dean; Bolin, Carole A.; Summers, Theresa A.; Wagar, Elizabeth A.; Cheville, N. F.; Hartskeerl, Rudy A.; Haake, David A.

doi:10.1128/iai.67.2.853-861.1999

Cited by 118 publications

(57 citation statements)

References 36 publications

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“…In contrast, LipL32 is detectable both by immunohistochemistry and by immunoblot (Haake et al, 2000). The immunohistochemistry data presented here show that LIC10365-encoded protein, such as OmpL1, LipL41 and LipL32, among others (Barnett et al, 1999), is expressed by L. interrogans within the renal tubules of experimentally infected guinea-pigs ( Fig. 3).…”

Section: Mmentioning

confidence: 52%

A novel leptospiral protein increases ICAM-1 and E-selectin expression in human umbilical vein endothelial cells

Vieira

D’Atri

Schattner

et al. 2007

FEMS Microbiology Letters

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It has been reported previously that activation of vascular endothelium by outer membrane proteins of the spirochetes Borrelia sp. and Treponema sp. resulted in enhanced expression of endothelial cell adhesion molecules. To investigate the role of leptospiral proteins in this process, a predicted lipoprotein encoded by the gene LIC10365 was selected, which belongs to a paralogous family that presents a domain of unknown function, DUF1565. The LIC10365 gene was cloned and the protein expressed in Escherichia coli C43 (DE3) strain using the vector pAE. The recombinant protein tagged with N-terminal hexahistidine was purified by metal-charged chromatography and was used to assess its ability to activate cultured human umbilical vein endothelial cells. The rLIC10365 activated endothelium in such a manner that E-selectin and intercellular adhesion molecule 1 (ICAM-1) became upregulated in a dose-dependent fashion. The LIC10365-encoded protein was identified in vivo in the renal tubules of animal during experimental infection with Leptospira interrogans. Collectively, these results implicate the LIC10365-coding protein of L. interrogans as a potential effector molecule in the promotion of a host inflammatory response. This is the first report of a leptospiral protein capable of up-regulating the expression of endothelial cell adhesion molecules ICAM-1 and E-selectin.

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Section: Mmentioning

confidence: 52%

A novel leptospiral protein increases ICAM-1 and E-selectin expression in human umbilical vein endothelial cells

Vieira

D’Atri

Schattner

et al. 2007

FEMS Microbiology Letters

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“…Occasionally, the whole organism rolls up inside such a bubble, giving the appearance of an encysted spirochete (Swain, 1955). During renal leptospirosis, leptospires can, at any rate, change superficial molecules situated on the outer membrane, depending on the stage of infection and intrarenal localization (Barnett et al., 1999).…”

Section: Discussionmentioning

confidence: 99%

Recurrent Uveitis in Horses: Vitreal Examinations with Ultrastructural Detection of Leptospires

Brandes

Wollanke

Niedermaier

et al. 2007

Journal of Veterinary Medicine Series A

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This study documents the examination of 17 horses (both sexes, 3-18 years old) suffering from spontaneous equine recurrent uveitis (ERU). Vitreal samples obtained by pars plana vitrectomy were examined macroscopically and ultrastructurally, and in most cases also by cultural examination, by microscopic agglutination test (MAT) and by polymerase chain reaction. In 24% (4/17) of the animals, ultrastructural examination by electron microscopy revealed intact leptospiral bacteria in the vitreous. The leptospires were detected freely in the vitreous and also incorporated by a phagocyte. They were surrounded by a rim of proteinaceous material which was reduced around a phagocytosed leptospira. Ninety-four per cent (16/17) of the vitreal samples presented significant antibody levels in the MAT, mostly against leptospiral serovar Grippotyphosa. Seventy-five per cent (9/12) of bacterial culture examinations were positive for leptospira. Polymerase chain reaction was positive in all (16/16) examinations performed. Our findings support previous reports suggesting that leptospires play an important role in the pathogenesis of ERU. Interestingly, this study found leptospires after secondary and later acute episodes. A persistent leptospiral infection is therefore suggested as the cause of ERU.

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“…Furthermore, pathogenic, but not saprophytic, Leptospira have been shown to interrupt cell-to-cell junctions in vitro (Sato & Coburn, 2017). Enhanced vascular permeability facilitated by LIC10831 may allow the bacterium to escape host blood vessels to take up residence in preferred host tissues (Barnett et al, 1999;Ozuru et al, 2017).…”

Section: Lic10831 Also Binds Human Ve-cadherinmentioning

confidence: 99%

An extracellular Leptospira interrogans leucine‐rich repeat protein binds human E‐ and VE‐cadherins

Eshghi

Gaultney

England

et al. 2018

Cellular Microbiology

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Pathogenic Leptospira bacteria are the causative agents of leptospirosis, a zoonotic disease affecting animals and humans worldwide. These pathogenic species have the ability to rapidly cross host tissue barriers by a yet unknown mechanism. A comparative analysis of pathogens and saprophytes revealed a higher abundance of genes encoding proteins with leucine-rich repeat (LRR) domains in the genomes of pathogens. In other bacterial pathogens, proteins with LRR domains have been shown to be involved in mediating host cell attachment and invasion. One protein from the pathogenic species Leptospira interrogans, LIC10831, has been previously analysed via X-ray crystallography, with findings suggesting it may be an important bacterial adhesin. Herein we show that LIC10831 elicits an antibody response in infected animals, is actively secreted by the bacterium, and binds human E- and VE-cadherins. These results provide biochemical and cellular evidences of LRR protein-mediated host-pathogen interactions and identify a new multireceptor binding protein from this infectious Leptospira species.

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Expression and Distribution of Leptospiral Outer Membrane Components during Renal Infection of Hamsters

Cited by 118 publications

References 36 publications

A novel leptospiral protein increases ICAM-1 and E-selectin expression in human umbilical vein endothelial cells

A novel leptospiral protein increases ICAM-1 and E-selectin expression in human umbilical vein endothelial cells

Recurrent Uveitis in Horses: Vitreal Examinations with Ultrastructural Detection of Leptospires

An extracellular Leptospira interrogans leucine‐rich repeat protein binds human E‐ and VE‐cadherins

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