ArticleVirulence2018
Haemophilus parasuis α-2,3-sialyltransferase-mediated lipooligosaccharide sialylation contributes to bacterial pathogenicity.
Article in Virulence, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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
16 citing papers in PubMed, 27 citations in OpenAlex.
- Article
- Outer membrane vesicles of Glaesserlla parasuis activate the endosomal cGAS-STING-IRF3 pathway through nucleic acid payload delivery: a biological perspective on host defense protocol optimization.Veterinary research · 2025Article
- Research progress onFrontiers in veterinary science · 2025Review
- Epidemiological and comparative genomic analysis of pathogenicFrontiers in microbiology · 2025Article
- Epidemiology and pathogenicity ofFrontiers in microbiology · 2025Article
- Article
- Genomic insight into the diversity ofmSphere · 2024Article
- A marker-free genetic manipulation method for Glaesserella parasuis strains developed by alternately culturing transformants at 37°C and 30°C.BMC biotechnology · 2024Article
- A comparative study of the substrate preference of the sialidases, CpNanI, HpNanH, and BbSia2 towards 2-Aminobenzamide-labeled 3'-Sialyllactose, 6'-Sialyllactose, and Sialyllacto-N-tetraose-b.Biochemistry and biophysics reports · 2024Article
- Glycosphingolipids: from metabolism to chemoenzymatic total synthesis.Organic & biomolecular chemistry · 2024Review
- Resistin secreted by porcine alveolar macrophages leads to endothelial cell dysfunction duringVirulence · 2023Article
- Molecular characterization of Glaesserella parasuis strains circulating in North American swine production systems.BMC veterinary research · 2023Article
- Application of mouse model for evaluation of recombinant LpxC and GmhA as novel antigenic vaccine candidates of Glaesserella parasuis serotype 13.The Journal of veterinary medical science · 2021Article
- The Tat system and its dependent cell division proteins are critical for virulence of extra-intestinal pathogenicVirulence · 2020Article
- Effect of cAMP Receptor Protein Gene on Growth Characteristics and Stress Resistance ofFrontiers in cellular and infection microbiology · 2020Article
- Haemophilus parasuis VtaA2 is involved in adhesion to extracellular proteins.Veterinary research · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial lipooligosaccharide (LOS) is an important virulence-associated factor, and its sialylation largely confers its ability to mediate cell adhesion, invasion, inflammation, and immune evasion. Here, we investigated the function of the Haemophilus parasuis α-2,3-sialyltransferase gene, lsgB, which determines the terminal sialylation of LOS, by generating a lsgB deletion mutant as well as a complementation strain. Our data indicate a direct effect of lsgB on LOS sialylation and reveal important roles of lsgB in promoting the pathogenicity of H. parasuis, including adhesion to and invasion of porcine cells in vitro, bacterial load and survival in vivo, as well as a contribution to serum resistance. These observations highlight the function of lsgB in mediating LOS sialylation and more importantly its role in H. parasuis infection. These findings provide a more profound understanding of the pathogenic mechanism of this disease-causing bacterium.
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.