ArticleGenetics and molecular biology
The chitinase C gene PsChiC from Pseudomonas sp. and its synergistic effects on larvicidal activity.
Article in Genetics and molecular biology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 29 citations in OpenAlex.
- Genomic and functional profiles of two Antarctic chitin-degrading Arthrobacter strains.Extremophiles : life under extreme conditions · 2026Article
- Gene Cloning, Heterologous Expression, and In Silico Analysis of Chitinase B fromMolecules (Basel, Switzerland) · 2024Article
- Microbial chitinases and their relevance in various industries.Folia microbiologica · 2023Review
- Bacterial chitinases: genetics, engineering and applications.World journal of microbiology & biotechnology · 2022Review
- Associated bacteria of a pine sawyer beetle confer resistance to entomopathogenic fungi via fungal growth inhibition.Environmental microbiome · 2022Article
- Insecticidal and growth inhibitory activity of gut microbes isolated from adults of Spodoptera litura (Fab.).BMC microbiology · 2022Article
- Chitinases ofFrontiers in microbiology · 2019Review
- Article
- Chitinase-producing bacteria and their role in biocontrol.AIMS microbiology · 2017Review
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pseudomonas sp. strain TXG6-1, a chitinolytic gram-negative bacterium, was isolated from a vegetable field in Taixing city, Jiangsu Province, China. In this study, a Pseudomonas chitinase C gene (PsChiC) was isolated from the chromosomal DNA of this bacterium using a pair of specific primers. The PsChiC gene consisted of an open reading frame of 1443 nucleotides and encoded 480 amino acid residues with a calculated molecular mass of 51.66 kDa. The deduced PsChiC amino acid sequence lacked a signal sequence and consisted of a glycoside hydrolase family 18 catalytic domain responsible for chitinase activity, a fibronectin type III-like domain (FLD) and a C-terminal chitin-binding domain (ChBD). The amino acid sequence of PsChiCshowed high sequence homology (> 95%) with chitinase C from Serratia marcescens. SDS-PAGE showed that the molecular mass of chitinase PsChiC was 52 kDa. Chitinase assays revealed that the chitobiosidase and endochitinase activities of PsChiCwere 51.6- and 84.1-fold higher than those of pET30a, respectively. Although PsChiC showed little insecticidal activity towards Spodoptera litura larvae, an insecticidal assay indicated that PsChiC increased the insecticidal toxicity of SpltNPV by 1.78-fold at 192 h and hastened death. These results suggest that PsChiC from Pseudomonas sp. could be useful in improving the pathogenicity of baculoviruses.
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