ArticlePloS one2015
The Immunoreactive Exo-1,3-β-Glucanase from the Pathogenic Oomycete Pythium insidiosum Is Temperature Regulated and Exhibits Glycoside Hydrolase Activity.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Development of lateral flow immunochromatographic assay with Anti-Pythium insidiosum antibodies for point-of-care testing of vascular pythiosis.Scientific reports · 2025Article
- Plant immunity suppression by an exo-β-1,3-glucanase and an elongation factor 1α of the rice blast fungus.Nature communications · 2023Article
- Three Diverse Granule Preparation Methods for Proteomic Analysis of Mature Rice (Molecules (Basel, Switzerland) · 2022Article
- A Review: Antimicrobial Therapy for Human Pythiosis.Antibiotics (Basel, Switzerland) · 2022Review
- History and Perspective of Immunotherapy for Pythiosis.Vaccines · 2021Review
- Prospecting Biomarkers for Diagnostic and Therapeutic Approaches in Pythiosis.Journal of fungi (Basel, Switzerland) · 2021Article
- Expression, purification, and characterization of the recombinant exo-1,3-β-glucanase (Exo1) of the pathogenic oomyceteHeliyon · 2020Article
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The oomycete organism, Pythium insidiosum, is the etiologic agent of the life-threatening infectious disease called "pythiosis". Diagnosis and treatment of pythiosis is difficult and challenging. Novel methods for early diagnosis and effective treatment are urgently needed. Recently, we reported a 74-kDa immunodominant protein of P. insidiosum, which could be a diagnostic target, vaccine candidate, and virulence factor. The protein was identified as a putative exo-1,3-ß-glucanase (Exo1). This study reports on genetic, immunological, and biochemical characteristics of Exo1. The full-length exo1 coding sequence (2,229 bases) was cloned. Phylogenetic analysis showed that exo1 is grouped with glucanase-encoding genes of other oomycetes, and is far different from glucanase-encoding genes of fungi. exo1 was up-regulated upon exposure to body temperature, and its gene product is predicted to contain BglC and X8 domains, which are involved in carbohydrate transport, binding, and metabolism. Based on its sequence, Exo1 belongs to the Glycoside Hydrolase family 5 (GH5). Exo1, expressed in E. coli, exhibited ß-glucanase and cellulase activities. Exo1 is a major intracellular immunoreactive protein that can trigger host immune responses during infection. Since GH5 enzyme-encoding genes are not present in human genomes, Exo1 could be a useful target for drug and vaccine development against this pathogen.
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