ArticleInfection and immunity2002
Cytotoxic activities of Leptospira interrogans hemolysin SphH as a pore-forming protein on mammalian cells.
Article in Infection and immunity, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers, 1 of them a synthesis that pooled it.
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Who cites it
42 citing papers in PubMed, 1 synthesis or guideline pooled it, 105 citations in OpenAlex.
- Trends and advances inFrontiers in microbiology · 2024Pooled it
- Leptospiral hemolysins induce proinflammatory cytokines through Toll-like receptor 2-and 4-mediated JNK and NF-κB signaling pathways.PloS one · 2012Trial
- Development of leptospiral virulence-modifying protein detection assay: implications for pathogenesis and diagnostic test development.Microbiology spectrum · 2025Article
- Story of Pore-Forming Proteins from Deadly Disease-Causing Agents to Modern Applications with Evolutionary Significance.Molecular biotechnology · 2024Review
- Cellular Pathophysiology of Leptospirosis: Role of Na/K-ATPase.Microorganisms · 2023Review
- Sph2Vaccines · 2023Article
- Characterization of a virulence-modifying protein ofFrontiers in microbiology · 2022Article
- Article
- PathogenicFrontiers in microbiology · 2022Article
- The role of leptospiremia and specific immune response in severe leptospirosis.Scientific reports · 2021Article
- Revisiting the Development of Vaccines Against PathogenicFrontiers in immunology · 2021Review
- A Review on Host-Frontiers in cellular and infection microbiology · 2021Review
- Article
- Characterization of a Novel Peptide from PathogenicPathogens (Basel, Switzerland) · 2020Article
- Leptospirosis is an invasive infectious and systemic inflammatory disease.Biomedical journal · 2020Review
- Raised levels of Il-6, Il-17a, and Il-22 in fatal leptospirosis.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2019Article
- Historical Review of Leptospirosis in the Korea (1945 - 2015).Infection & chemotherapy · 2019Review
- Bacterial Sphingomyelinases and Phospholipases as Virulence Factors.Microbiology and molecular biology reviews : MMBR · 2016Review
- Comparative analyses of transport proteins encoded within the genomes of Leptospira species.Microbial pathogenesis · 2016Article
- Comparative genomic analyses of transport proteins encoded within the genomes of Leptospira species.Microbial pathogenesis · 2015Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Leptospirosis is a spirochetal zoonosis that causes an acute febrile systemic illness in humans. Leptospira sp. hemolysins have been shown to be virulence factors for the pathogenesis of leptospirosis. Previously, we cloned a hemolysin SphH of Leptospira interrogans serovar lai, a homologue of L. borgpetersenii sphingomyelinase (SphA), from a genomic library (S. H. Lee, K. A. Kim, Y. K. Kim, I. W. Seong, M. J. Kim, and Y. J. Lee, Gene 254:19-28, 2000). Escherichia coli lysate harboring the sphH showed high hemolytic activities on sheep erythrocytes. However, it neither showed sphingomyelinase nor phospholipase activities, in contrast to SphA which was known to have sphingomyelinase activity. Interestingly, the SphH-mediated hemolysis on erythrocytes was osmotically protected by PEG 5000, suggesting that the SphH might have caused pore formation on the erythrocyte membrane. In the present study, we have prepared the Leptospira hemolysin SphH and investigated its hemolytic and cytotoxic activities on mammalian cells. SphH was shown to be a pore-forming protein on several mammalian cells: When treated with the SphH, the sheep erythrocyte membranes formed pores, which were morphologically confirmed by transmission electron microscopy. Furthermore, the SphH-mediated cytotoxicities on mammalian cells were demonstrated by the release of LDH and by inverted microscopic examinations. Finally, the immune serum against the full-length hemolysin could effectively neutralize the SphH-mediated hemolytic and cytotoxic activities. In conclusion, these results suggest that the virulence of Leptospira SphH was due to the pore formation on mammalian cell membranes.
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