ArticlePLoS neglected tropical diseases2019
Disruption of the NlpD lipoprotein of the plague pathogen Yersinia pestis affects iron acquisition and the activity of the twin-arginine translocation system.
Article in PLoS neglected tropical diseases, 2019. 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, 12 citations in OpenAlex.
- Secreted LysM proteins are required for niche competition and full virulence in Pseudomonas savastanoi during host plant infection.PLoS pathogens · 2025Article
- NlpD as a crucial factor in desiccation resistance and biofilm formation in Cronobacter sakazakii.Scientific reports · 2025Article
- Cpx-signalling facilitates Hms-dependent biofilm formation by Yersinia pseudotuberculosis.NPJ biofilms and microbiomes · 2022Article
- One fold, many functions-M23 family of peptidoglycan hydrolases.Frontiers in microbiology · 2022Review
- Design of a multi-epitope vaccine againstFrontiers in veterinary science · 2022Article
- The lipoprotein NlpD inVirulence · 2021Article
- Novel RNA Extraction Method for Dual RNA-seq Analysis of Pathogen and Host in the Early Stages ofMicroorganisms · 2021Article
- Searching for putative virulence factors in the genomes of Shewanella indica and Shewanella algae.Archives of microbiology · 2021Article
- Screening of an FDA-Approved Library for Novel Drugs againstAntibiotics (Basel, Switzerland) · 2021Article
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Authors and funding
12 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have previously shown that the cell morphogenesis NlpD lipoprotein is essential for virulence of the plague bacteria, Yersinia pestis. To elucidate the role of NlpD in Y. pestis pathogenicity, we conducted a whole-genome comparative transcriptome analysis of the wild-type Y. pestis strain and an nlpD mutant under conditions mimicking early stages of infection. The analysis suggested that NlpD is involved in three phenomena: (i) Envelope stability/integrity evidenced by compensatory up-regulation of the Cpx and Psp membrane stress-response systems in the mutant; (ii) iron acquisition, supported by modulation of iron metabolism genes and by limited growth in iron-deprived medium; (iii) activity of the twin-arginine (Tat) system, which translocates folded proteins across the cytoplasmic membrane. Virulence studies of Y. pestis strains mutated in individual Tat components clearly indicated that the Tat system is central in Y. pestis pathogenicity and substantiated the assumption that NlpD essentiality in iron utilization involves the activity of the Tat system. This study reveals a new role for NlpD in Tat system activity and iron assimilation suggesting a modality by which this lipoprotein is involved in Y. pestis pathogenesis.
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