The Fimbrial Protein is a Virulence Factor and Potential Vaccine Antigen of<i>Avibacterium paragallinarum</i>

Liu, C.-C.; Ou, Shan-Chia; Tan, Duen-Huey; Hsieh, Ming-Kun; Shien, Jui-Hung; Chang, Poa-Chun

doi:10.1637/11410-031316-reg.1

Cited by 7 publications

(4 citation statements)

References 27 publications

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“…Congruent with previous observations that cell surface proteins are main targets of positive selection in both eukaryotes and prokaryotes [15, 62–66], most genes showing evidence for positive selection in this study encode cell surface proteins, such as outer membrane proteins, transporters, permeases, porins, cell surface appendages. Notably, a number of the proteins found here to show evidence for positive selection have reported or plausible functions in virulence, including genes encoding fimbriae, pili, flagella-related proteins [67, 68]. In addition, an autotransporter outer membrane beta-barrel domain-containing protein and the outer membrane protein assembly factor BamA, which both participate in the beta-barrel assembly, showed evidence for positive selection and have been proposed to play direct and indirect roles in virulence in Gram-negative bacteria [69].…”

Section: Discussionmentioning

confidence: 99%

Serotype-specific evolutionary patterns of antimicrobial-resistant Salmonella enterica

et al. 2019

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Background The emergence of antimicrobial-resistant (AMR) strains of the important human and animal pathogen Salmonella enterica poses a growing threat to public health. Here, we studied the genome-wide evolution of 90 S. enterica AMR isolates, representing one host adapted serotype ( S. Dublin) and two broad host range serotypes ( S. Newport and S. Typhimurium). Results AMR S. Typhimurium had a large effective population size, a large and diverse genome, AMR profiles with high diversity, and frequent positive selection and homologous recombination. AMR S. Newport showed a relatively low level of diversity and a relatively clonal population structure. AMR S. Dublin showed evidence for a recent population bottleneck, and the genomes were characterized by a larger number of genes and gene ontology terms specifically absent from this serotype and a significantly higher number of pseudogenes as compared to other two serotypes. Approximately 50% of accessory genes, including specific AMR and putative prophage genes, were significantly over- or under-represented in a given serotype. Approximately 65% of the core genes showed phylogenetic clustering by serotype, including the AMR gene aac (6′)-Iaa . While cell surface proteins were shown to be the main target of positive selection, some proteins with possible functions in AMR and virulence also showed evidence for positive selection. Homologous recombination mainly acted on prophage-associated proteins. Conclusions Our data indicates a strong association between genome content of S. enterica and serotype. Evolutionary patterns observed in S . Typhimurium are consistent with multiple emergence events of AMR strains and/or ecological success of this serotype in different hosts or habitats. Evolutionary patterns of S . Newport suggested that antimicrobial resistance emerged in one single lineage, Lineage IIC. A recent population bottleneck and genome decay observed in AMR S. Dublin are congruent with its narrow host range. Finally, our results suggest the potentially important role of positive selection in the evolution of antimicrobial resistance, host adaptation and serotype diversification in S. enterica . Electronic supplementary material The online version of this article (10.1186/s12862-019-1457-5) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

Serotype-specific evolutionary patterns of antimicrobial-resistant Salmonella enterica

et al. 2019

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“…Vaccination targeting adhesion proteins and essential virulence factors such as FimA [58, 59] and type 1 fimbrial protein is a commonly used approach due to the external localisation of these proteins and their exposure to host immune systems. Anti-fimbrial antibodies have been shown to interfere with function and reduce disease [60, 61] and a FimA vaccine provided protection against Streptococcus parasanguis, Streptococcus mitis, Streptococcus mutans and Streptococcus salivarius in rats [62-64].…”

Section: Resultsmentioning

confidence: 99%

Prediction ofBurkholderia pseudomalleiDsbA substrates identifies potential virulence factors and vaccine targets

Vezina

Petit

Martin

et al. 2020

Preprint

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AbstractIdentification of bacterial virulence factors is critical for understanding disease pathogenesis, drug discovery and vaccine development. In this study we used two approaches to predict virulence factors of Burkholderia pseudomallei, the Gram-negative bacterium that causes melioidosis. B. pseudomallei is naturally antibiotic resistant and there are no melioidosis vaccines. To identify B. pseudomallei protein targets for drug discovery and vaccine development, we chose to search for substrates of the B. pseudomallei periplasmic disulfide bond forming protein A (DsbA). DsbA introduces disulfide bonds into extra-cytoplasmic proteins and is essential for virulence in many Gram-negative organism, including B. pseudomallei. The first approach to identify B. pseudomallei DsbA virulence factor substrates was a large-scale genomic analysis of 511 unique B. pseudomallei disease-associated strains. This yielded 4,496 core gene products, of which we hypothesise 263 are DsbA substrates. Manual curation of the 263 mature proteins yielded 73 associated with disease pathogenesis or virulence. These were screened for structural homologues to predict potential B-cell epitopes. In the second approach, we searched the B. pseudomallei genome for homologues of the more than 90 known DsbA substrates in other bacteria. Using this approach, we identified 15 potential B. pseudomallei DsbA virulence factor substrates. Two putative B. pseudomallei virulence factors were identified by both methods: homologues of PenI family β-lactamase and of succinate dehydrogenase flavoprotein subunit. These two proteins could serve as high priority targets for future B. pseudomallei virulence factor characterization.

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“…Vaccination targeting adhesion proteins and essential virulence factors such as FimA [73] and type 1 fimbrial protein [74] is a commonly used approach due to the external localisation of these proteins and their exposure to host immune systems. Anti-fimbrial antibodies have been shown to interfere with function and reduce disease [75,76] and a FimA vaccine provided protection against Streptococcus parasanguis, Streptococcus mitis, Streptococcus mutans and Streptococcus salivarius in rats [77][78][79].…”

Section: Plos Onementioning

confidence: 99%

Prediction of Burkholderia pseudomallei DsbA substrates identifies potential virulence factors and vaccine targets

et al. 2020

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Identification of bacterial virulence factors is critical for understanding disease pathogenesis, drug discovery and vaccine development. In this study we used two approaches to predict virulence factors of Burkholderia pseudomallei, the Gram-negative bacterium that causes melioidosis. B. pseudomallei is naturally antibiotic resistant and there are no clinically available melioidosis vaccines. To identify B. pseudomallei protein targets for drug discovery and vaccine development, we chose to search for substrates of the B. pseudomallei periplasmic disulfide bond forming protein A (DsbA). DsbA introduces disulfide bonds into extra-cytoplasmic proteins and is essential for virulence in many Gram-negative organism, including B. pseudomallei. The first approach to identify B. pseudomallei DsbA virulence factor substrates was a large-scale genomic analysis of 511 unique B. pseudomallei disease-associated strains. This yielded 4,496 core gene products, of which we hypothesise 263 are DsbA substrates. Manual curation and database screening of the 263 mature proteins yielded 81 associated with disease pathogenesis or virulence. These were screened for structural homologues to predict potential B-cell epitopes. In the second approach, we searched the B. pseudomallei genome for homologues of the more than 90 known DsbA substrates in other bacteria. Using this approach, we identified 15 putative B. pseudomallei DsbA virulence factor substrates, with two of these previously identified in the genomic approach, bringing the total number of putative DsbA virulence factor substrates to 94. The two putative B. pseudomallei virulence factors identified by both methods are homologues of PenI family β-lactamase and a molecular chaperone. These two proteins could serve as high priority targets for future B. pseudomallei virulence factor characterization.

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The Fimbrial Protein is a Virulence Factor and Potential Vaccine Antigen ofAvibacterium paragallinarum

Cited by 7 publications

References 27 publications

Serotype-specific evolutionary patterns of antimicrobial-resistant Salmonella enterica

Serotype-specific evolutionary patterns of antimicrobial-resistant Salmonella enterica

Prediction ofBurkholderia pseudomalleiDsbA substrates identifies potential virulence factors and vaccine targets

Prediction of Burkholderia pseudomallei DsbA substrates identifies potential virulence factors and vaccine targets

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