ArticlePloS one2013
Leptospira interrogans enolase is secreted extracellularly and interacts with plasminogen.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 45 citations in OpenAlex.
- Leptospira glyceraldehyde-3-phosphate dehydrogenase (LiGAPDH): a cell-surface plasminogen binding protein.FEMS microbiology letters · 2026Article
- The Regulatory Mechanisms of Treponema pallidum Enolase on Macrophages: From Enzymatic Activity to Signal Transduction.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
- Leucine-rich repeat proteins ofFrontiers in microbiology · 2024Article
- Improvement the expression and purification of Loa22: a lipoprotein with OmpA domain from pathogenicIranian journal of microbiology · 2023Article
- The structure ofFrontiers in immunology · 2023Article
- Structural Characterization ofPathogens (Basel, Switzerland) · 2021Article
- Extracellular Proteome Analysis Shows the Abundance of Histidine Kinase Sensor Protein, DNA Helicase, Putative Lipoprotein Containing Peptidase M75 Domain and Peptidase C39 Domain Protein inPathogens (Basel, Switzerland) · 2021Article
- A Review on Host-Frontiers in cellular and infection microbiology · 2021Review
- Detection of virulence factors of South African Lactococcus garvieae isolated from rainbow trout, Oncorhynchus mykiss (Walbaum).The Onderstepoort journal of veterinary research · 2018Article
- Article
- Complement Evasion by PathogenicFrontiers in immunology · 2016Review
- Pathogenic Leptospira interrogans exoproteins are primarily involved in heterotrophic processes.Infection and immunity · 2015Article
- Analysis of Paracoccidioides secreted proteins reveals fructose 1,6-bisphosphate aldolase as a plasminogen-binding protein.BMC microbiology · 2015Article
- Article
- Comparative proteomics and expression analysis of five genes in Epicauta chinensis larvae from the first to fifth instar.PloS one · 2014Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Leptospira interrogans is the agent for leptospirosis, an important zoonosis in humans and animals across the globe. Surface proteins of invading pathogens, such as L. interrogans, are thought to be responsible for successful microbial persistence in vivo via interaction with specific host components. In particular, a number of invasive infectious agents exploit host proteolytic pathways, such as one involving plasminogen (Pg), which aid in efficient pathogen dissemination within the host. Here we show that L. interrogans serovar Lai binds host Pg and that the leptospiral gene product LA1951, annotated as enolase, is involved in this interaction. Interestingly, unlike in related pathogenic Spirochetes, such as Borrelia burgdorferi, LA1951 is not readily detectable in the L. interrogans outer membrane. We show that the antigen is indeed secreted extracellularly; however, it can reassociate with the pathogen surface, where it displays Pg-binding and measurable enzymatic activity. Hamsters infected with L. interrogans also develop readily detectable antibody responses against enolase. Taken together, our results suggest that the L. interrogans enolase has evolved to play a role in pathogen interaction with host molecules, which may contribute to the pathogenesis of leptospirosis.
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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.