Type VI Secretion Systems Present New Insights on Pathogenic Yersinia

Yang, Xiaobing; Pan, Junfeng; Wang, Yao; Shen, Xihui

doi:10.3389/fcimb.2018.00260

Cited by 37 publications

(29 citation statements)

References 88 publications

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“…77 These core-component proteins are categorized into different subunits: the membrane complex (TssJLM), the baseplate complex (TssAEFGK), needle sheath complex (TssBC), sheath recycling ATPase (TssH), and the injection apparatus (Hcp, VgrG). 78 In the present study we found 12 such core-component proteins (TssABC, Hcp1, TssFGH, VgrG, TssJKLM) and two additional auxiliary component proteins (TagH and TagF) ( Table 2). Interestingly, most of these proteins found to be in the cytoplasmic region which suggests that these cytoplasm proteins can be further investigated for enhanced understanding of secreted protein transport during the pathogenesis.…”

Section: Analysis Of Type VI Secretion System Proteinssupporting

confidence: 53%

Proteomic profiling of Serratia marcescens by high-resolution mass spectrometry

2020

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Introduction: Serratia marcescens, an opportunistic human pathogen, is reported as an important cause of nosocomial infection and outbreaks. Although the genome of S. marcescens (ATCC 13880) was completely sequenced by 2014, there are no studies on the proteomic profile of the organism. The objective of the present study is to analyze the protein profile of S. marcescens (ATCC 13880) using a high resolution mass spectrometry (MS). Methods: Serratia marcescens ATCC 13880 strain was grown in Luria-Bertani broth and the protein extracted was subjected to trypsin digestion, followed by basic reverse phase liquid chromatography fractionation. The peptide fractions were then analysed using Orbitrap Fusion Mass Spectrometry and the raw MS data were processed in Proteome Discoverer software. Results: The proteomic analysis identified 15 009 unique peptides mapping to 2541 unique protein groups, which corresponds to approximately 54% of the computationally predicted protein-coding genes. Bioinformatic analysis of these identified proteins showed their involvement in biological processes such as cell wall organization, chaperone-mediated protein folding and ATP binding. Pathway analysis revealed that some of these proteins are associated with bacterial chemotaxis and beta-lactam resistance pathway. Conclusion: To the best of our knowledge, this is the first high-throughput proteomics study of S. marcescens (ATCC 13880). These novel observations provide a crucial baseline molecular profile of the S. marcescens proteome which will prove to be helpful for the future research in understanding the host-pathogen interactions during infection, elucidating the mechanism of multidrug resistance, and developing novel diagnostic markers or vaccine for the disease.

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Section: Analysis Of Type VI Secretion System Proteinssupporting

confidence: 53%

Proteomic profiling of Serratia marcescens by high-resolution mass spectrometry

2020

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“…Thus, many T6SS-encoding bacteria tightly regulate their T6SS at transcriptional, posttranscriptional, and/or posttranslational levels (26,27). The complex regulatory networks governing T6SS activity enable bacteria to respond according to environmental signals, including: temperature, pH, cation/ nutrient availability, osmolarity, and membrane perturbation (26,(28)(29)(30)(31)(32)(33)(34)(35)(36). For instance, the antibacterial T6SS of Pseudomonas aeruginosa (HSI-I), regarded as a defensive T6SS, remains silenced unless P. aeruginosa perceives an attack from a competing bacterium (37).…”

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confidence: 99%

The Tip of the VgrG Spike Is Essential to Functional Type VI Secretion System Assembly in Acinetobacter baumannii

Lopez

Feldman

2020

mBio

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The type VI secretion system (T6SS) is a critical weapon in bacterial warfare between Gram-negative bacteria. Although invaluable for niche establishment, this machine represents an energetic burden to its host bacterium. Acinetobacter baumannii is an opportunistic pathogen that poses a serious threat to public health due to its high rates of multidrug resistance. In some A. baumannii strains, the T6SS is transcriptionally downregulated by large multidrug resistance plasmids. Other strains, such as the clinical isolate AbCAN2, express T6SS-related genes but lack T6SS activity under laboratory conditions, despite not harboring these plasmids. This suggests that alternative mechanisms exist to repress the T6SS. Here, we used a transposon mutagenesis approach in AbCAN2 to identify novel T6SS repressors. Our screen revealed that the T6SS of this strain is inhibited by a homolog of VgrG, an essential structural component of all T6SSs reported to date. We named this protein inhibitory VgrG (VgrGi). Biochemical and in silico analyses demonstrated that the unprecedented inhibitory capability of VgrGi is due to a single amino acid mutation in a widely conserved C-terminal domain of unknown function, DUF2345. We also show that unlike in other bacteria, the C terminus of VgrG is essential for functional T6SS assembly in A. baumannii. Our study provides insight into the architectural requirements underlying functional assembly of the T6SS of A. baumannii. We propose that T6SS-inactivating point mutations are beneficial to the host bacterium, since they eliminate the energy cost associated with maintaining a functional T6SS, which appears to be unnecessary for A. baumannii virulence. IMPORTANCE Despite the clinical relevance of A. baumannii, little is known about its fundamental biology. Here, we show that a single amino acid mutation in VgrG, a critical T6SS structural protein, abrogates T6SS function. Given that this mutation was found in a clinical isolate, we propose that the T6SS of A. baumannii is probably not involved in virulence; this idea is supported by multiple genomic analyses showing that the majority of clinical A. baumannii strains lack proteins essential to the T6SS. We also show that, unlike in other species, the C terminus of VgrG is a unique architectural requirement for functional T6SS assembly in A. baumannii, suggesting that over evolutionary time, bacteria have developed changes to their T6SS architecture, leading to specialized systems.

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“…intermedia and Y. rohdei [64]. Various ABC transporters and a type-I fimbrial operon (D5F51_RS15015–D5F51_RS15045) were not present in Y.…”

Section: Resultsmentioning

confidence: 99%

Comparative genomic insights into Yersinia hibernica – a commonly misidentified Yersinia enterocolitica-like organism

et al. 2020

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Food-associated outbreaks linked to enteropathogenic Yersinia enterocolitica are of concern to public health. Pigs and their meat are recognized risk factors for transmission of Y. enterocolitica . This study aimed to describe the comparative genomics of Y. enterocolitica along with a number of misclassified Yersinia isolates, now constituting the recently described Yersinia hibernica . The latter was originally cultured from an environmental sample taken at a pig slaughterhouse. Unique features were identified in the genome of Y. hibernica, including a novel integrative conjugative element (ICE), denoted as ICE Yh-1 contained within a 255 kbp region of plasticity. In addition, a zebrafish embryo infection model was adapted and applied to assess the virulence potential among Yersinia isolates including Y. hibernica .

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Type VI Secretion Systems Present New Insights on Pathogenic Yersinia

Cited by 37 publications

References 88 publications

Proteomic profiling of Serratia marcescens by high-resolution mass spectrometry

Proteomic profiling of Serratia marcescens by high-resolution mass spectrometry

The Tip of the VgrG Spike Is Essential to Functional Type VI Secretion System Assembly in Acinetobacter baumannii

Comparative genomic insights into Yersinia hibernica – a commonly misidentified Yersinia enterocolitica-like organism

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