ArticleInfection and immunity2014
High-temperature protein G is an essential virulence factor of Leptospira interrogans.
Article in Infection and immunity, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
20 citing papers in PubMed, 54 citations in OpenAlex.
- The Role of Heat Shock Protein (Hsp) Chaperones in Environmental Stress Adaptation and Virulence of Plant Pathogenic Bacteria.International journal of molecular sciences · 2025Review
- Hsp90, a team player in protein quality control and the stress response in bacteria.Microbiology and molecular biology reviews : MMBR · 2024Review
- Fulminant Leptospirosis Presenting with Rapidly Developing Acute Renal Failure and Multiorgan Failure.Biomedicines · 2024Article
- Identifying Leptospira interrogans putative virulence factors with a yeast protein expression screen.Applied microbiology and biotechnology · 2022Article
- Comparative Proteomic Analysis for a Putative Pyridoxal Phosphate-Dependent Aminotransferase Required for Virulence in Acidovorax citrulli.The plant pathology journal · 2021Article
- Article
- AAA+ Molecular Chaperone ClpB inInternational journal of molecular sciences · 2020Review
- Leptospirosis in cats: Current literature review to guide diagnosis and management.Journal of feline medicine and surgery · 2020Review
- Gene silencing based on RNA-guided catalytically inactive Cas9 (dCas9): a new tool for genetic engineering in Leptospira.Scientific reports · 2019Article
- Sex Matters: Male Hamsters Are More Susceptible to Lethal Infection with Lower Doses of Pathogenic Leptospira than Female Hamsters.Infection and immunity · 2018Article
- Isolation and Identification of Putative Protein Substrates of the AAA+ Molecular Chaperone ClpB from the Pathogenic SpirochaeteInternational journal of molecular sciences · 2018Article
- PathogenicOpen veterinary journal · 2018Review
- Virulence of the zoonotic agent of leptospirosis: still terra incognita?Nature reviews. Microbiology · 2017Review
- Inhibitory Effects of Emodin, Thymol, and Astragalin on Leptospira interrogans-Induced Inflammatory Response in the Uterine and Endometrium Epithelial Cells of Mice.Inflammation · 2017Article
- Animal Models of Leptospirosis: Of Mice and Hamsters.Frontiers in immunology · 2017Review
- Analysis of LexA binding sites and transcriptomics in response to genotoxic stress in Leptospira interrogans.Nucleic acids research · 2016Article
- Leptospira interrogans lpxD Homologue Is Required for Thermal Acclimatization and Virulence.Infection and immunity · 2015Article
- Pathogenic Leptospira interrogans exoproteins are primarily involved in heterotrophic processes.Infection and immunity · 2015Article
- Screening of a Leptospira biflexa mutant library to identify genes involved in ethidium bromide tolerance.Applied and environmental microbiology · 2014Article
- A putative regulatory genetic locus modulates virulence in the pathogen Leptospira interrogans.Infection and immunity · 2014Article
Corrections and comments
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Authors and funding
10 authors at 5 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Leptospira interrogans is a global zoonotic pathogen and is the causative agent of leptospirosis, an endemic disease of humans and animals worldwide. There is limited understanding of leptospiral pathogenesis; therefore, further elucidation of the mechanisms involved would aid in vaccine development and the prevention of infection. HtpG (high-temperature protein G) is the bacterial homolog to the highly conserved molecular chaperone Hsp90 and is important in the stress responses of many bacteria. The specific role of HtpG, especially in bacterial pathogenesis, remains largely unknown. Through the use of an L. interrogans htpG transposon insertion mutant, this study demonstrates that L. interrogans HtpG is essential for virulence in the hamster model of acute leptospirosis. Complementation of the htpG mutant completely restored virulence. Surprisingly, the htpG mutant did not appear to show sensitivity to heat or oxidative stress, phenotypes common in htpG mutants in other bacterial species. Furthermore, the mutant did not show increased sensitivity to serum complement, reduced survival within macrophages, or altered protein or lipopolysaccharide expression. The underlying cause for attenuation thus remains unknown, but HtpG is a novel leptospiral virulence factor and one of only a very small number identified to date.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.