ArticleInfection and immunity2000
The leptospiral major outer membrane protein LipL32 is a lipoprotein expressed during mammalian infection.
Article in Infection and immunity, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 181 papers, 1 of them a synthesis that pooled it.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
181 citing papers in PubMed, 1 synthesis or guideline pooled it, 480 citations in OpenAlex.
- Trends and advances inFrontiers in microbiology · 2024Pooled it
- A systematic review ofOne health (Amsterdam, Netherlands) · 2026Article
- Artificial Irrigation Impacts the Seasonal Occurrence of Pathogenic Leptospira in Its Wild Reservoirs in a Mediterranean Environment.Zoonoses and public health · 2026Article
- Divergent Fates of Hardjo Leptospires: Early Transcriptomic Response ofTransboundary and emerging diseases · 2026Article
- A case report of an Amami rabbit (Pentalagus furnessi) infected with Leptospira interrogans.The Journal of veterinary medical science · 2025Article
- Design, Development and Immunogenic Evaluation of a Novel Lipl32 Recombinant Protein of Local Pathogenic Leptospira Serovars.Archives of Razi Institute · 2025Article
- Molecular and serological detection ofOpen veterinary journal · 2025Article
- Comparative Genome Analysis of 25 Sri LankanEvolutionary bioinformatics online · 2025Article
- UnveilingFrontiers in public health · 2025Article
- Production and characterization of immunoglobulin G anti-rLipL32 antibody as a biomarker for the diagnosis of leptospirosis.Veterinary world · 2024Article
- Improved Antibody Detection for Canine Leptospirosis: ELISAs Modified Using Local Leptospiral Serovar Isolates from Asymptomatic Dogs.Animals : an open access journal from MDPI · 2024Article
- Article
- Leptospiral adhesins: from identification to future perspectives.Frontiers in microbiology · 2024Review
- LipL41 and LigA/LigB Gene Silencing on a LipL32 KnockoutPathogens (Basel, Switzerland) · 2023Article
- Prevalence and Characteristics of Novel PathogenicMicroorganisms · 2023Article
- Application of a Multiplex PCR Assay for Molecular Identification of Pathogenic and Non-Pathogenic Leptospires based on lipL32 andArchives of Razi Institute · 2023Article
- Evaluation ofFrontiers in microbiology · 2023Article
- Weil's Disease-Immunopathogenesis, Multiple Organ Failure, and Potential Role of Gut Microbiota.Biomolecules · 2022Review
- Prevalence of PathogenicPathogens (Basel, Switzerland) · 2022Article
- Molecular detection of pathogenic Leptospira spp. in urban rodents from wet markets in northeast Malaysia.Journal of advanced veterinary and animal research · 2022Article
121 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 4 institutions in 1 country.
Funding
Abstract
We report the cloning of the gene encoding the 32-kDa lipoprotein, designated LipL32, the most prominent protein in the leptospiral protein profile. We obtained the N-terminal amino acid sequence of a staphylococcal V8 proteolytic-digest fragment to design an oligonucleotide probe. A Lambda-Zap II library containing EcoRI fragments of Leptospira kirschneri DNA was screened, and a 5.0-kb DNA fragment which contained the entire structural lipL32 gene was identified. Several lines of evidence indicate that LipL32 is lipid modified in a manner similar to that of other procaryotic lipoproteins. The deduced amino acid sequence of LipL32 would encode a 272-amino-acid polypeptide with a 19-amino-acid signal peptide, followed by a lipoprotein signal peptidase cleavage site. LipL32 is intrinsically labeled during incubation of L. kirschneri in media containing [(3)H]palmitate. The linkage of palmitate and the amino-terminal cysteine of LipL32 is acid labile. LipL32 is completely solubilized by Triton X-114 extraction of L. kirschneri; phase separation results in partitioning of LipL32 exclusively into the hydrophobic, detergent phase, indicating that it is a component of the leptospiral outer membrane. CaCl(2) (20 mM) must be present during phase separation for recovery of LipL32. LipL32 is expressed not only during cultivation but also during mammalian infection. Immunohistochemistry demonstrated intense LipL32 reactivity with L. kirschneri infecting proximal tubules of hamster kidneys. LipL32 is also a prominent immunogen during human leptospirosis. The sequence and expression of LipL32 is highly conserved among pathogenic Leptospira species. These findings indicate that LipL32 may be important in the pathogenesis, diagnosis, and prevention of leptospirosis.
Indexed as
Identifiers
What OpenQuestion holds
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.