ArticlePloS one2017
Pyridoxal phosphate synthases PdxS/PdxT are required for Actinobacillus pleuropneumoniae viability, stress tolerance and virulence.
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 25 citations in OpenAlex.
- Two-step bioconversion of pyridoxal 5'-phosphate from pyridoxine through cofactor regeneration and pyridoxine 5'-phosphate oxidase evolution.Synthetic and systems biotechnology · 2026Article
- Whole-Genome Analysis of PGP EndophyticInternational journal of molecular sciences · 2025Article
- Lupus and inflammatory bowel disease share a common set of microbiome features distinct from other autoimmune disorders.Annals of the rheumatic diseases · 2025Observational
- Functional and structural properties of pyridoxal reductase (PdxI) from Escherichia coli: a pivotal enzyme in the vitamin B6 salvage pathway.The FEBS journal · 2023Article
- Cronobacter sakazakii Pyridoxal Kinase PdxY Mediated by TreR and pESA3 Is Essential for Vitamin BApplied and environmental microbiology · 2023Article
- Proteomic and Phenotypic Analyses of a Putative YggS Family Pyridoxal Phosphate-Dependent Enzyme in Acidovorax citrulli.The plant pathology journal · 2023Article
- Actinobacillus utilizes a binding protein-dependent ABC transporter to acquire the active form of vitamin BThe Journal of biological chemistry · 2021Article
- Article
- The multifaceted role of vitamin BOpen biology · 2020Review
- Arsenic Response of Three AltiplanicFrontiers in microbiology · 2019Article
- Outer Membrane Lipoprotein Lip40 Modulates Adherence, Colonization, and Virulence ofFrontiers in microbiology · 2018Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pyridoxal 5'-phosphate (PLP) is an essential cofactor for numerous enzymes involved in a diversity of cellular processes in living organisms. Previous analysis of the Actinobacillus pleuropneumoniae S-8 genome sequence revealed the presence of pdxS and pdxT genes, which are implicated in deoxyxylulose 5-phosphate (DXP)-independent pathway of PLP biosynthesis; however, little is known about their roles in A. pleuropneumoniae pathogenicity. Our data demonstrated that A. pleuropneumoniae could synthesize PLP by PdxS and PdxT enzymes. Disruption of the pdxS and pdxT genes rendered the pathogen auxotrophic for PLP, and the defective growth as a result of these mutants was chemically compensated by the addition of PLP, suggesting the importance of PLP production for A. pleuropneumoniae growth and viability. Additionally, the pdxS and pdxT deletion mutants displayed morphological defects as indicated by irregular and aberrant shapes in the absence of PLP. The reduced growth of the pdxS and pdxT deletion mutants under osmotic and oxidative stress conditions suggests that the PLP synthases PdxS/PdxT are associated with the stress tolerance of A. pleuropneumoniae. Furthermore, disruption of the PLP biosynthesis pathway led to reduced colonization and attenuated virulence of A. pleuropneumoniae in the BALB/c mouse model. The data presented in this study reveal the critical role of PLP synthases PdxS/PdxT in viability, stress tolerance, and virulence of A. pleuropneumoniae.
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