The bvg‐repressed gene brtA, encoding biofilm‐associated surface adhesin, is expressed during host infection by Bordetella bronchiseptica

Nishikawa, Sayaka; Shinzawa, Naoaki; Nakamura, Keiji; Ishigaki, Keisuke; Abé, Hiroyuki; Horiguchi, Yasuhiko

doi:10.1111/1348-0421.12356

Cited by 27 publications

(38 citation statements)

References 50 publications

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“…Here we confirm the role for the Bvg-regulated adhesin BrtA, a putative homolog of the well-characterized LapA adhesin of Pseudomonas fluorescens , in biofilm formation by B . bronchiseptica , as has recently been reported by Nishikawa and colleagues [ 16 ]. Furthermore, we show that the c-di-GMP receptor LapD and the LapD-regulated protease LapG also participate in biofilm formation by B .…”

Section: Introductionsupporting

confidence: 73%

Homologs of the LapD-LapG c-di-GMP Effector System Control Biofilm Formation by Bordetella bronchiseptica

et al. 2016

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Biofilm formation is important for infection by many pathogens. Bordetella bronchiseptica causes respiratory tract infections in mammals and forms biofilm structures in nasal epithelium of infected mice. We previously demonstrated that cyclic di-GMP is involved in biofilm formation in B. bronchiseptica. In the present work, based on their previously reported function in Pseudomonas fluorescens, we identified three genes in the B. bronchiseptica genome likely involved in c-di-GMP-dependent biofilm formation: brtA, lapD and lapG. Genetic analysis confirmed a role for BrtA, LapD and LapG in biofilm formation using microtiter plate assays, as well as scanning electron and fluorescent microscopy to analyze the phenotypes of mutants lacking these proteins. In vitro and in vivo studies showed that the protease LapG of B. bronchiseptica cleaves the N-terminal domain of BrtA, as well as the LapA protein of P. fluorescens, indicating functional conservation between these species. Furthermore, while BrtA and LapG appear to have little or no impact on colonization in a mouse model of infection, a B. bronchiseptica strain lacking the LapG protease has a significantly higher rate of inducing a severe disease outcome compared to the wild type. These findings support a role for c-di-GMP acting through BrtA/LapD/LapG to modulate biofilm formation, as well as impact pathogenesis, by B. bronchiseptica

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Section: Introductionsupporting

confidence: 73%

Homologs of the LapD-LapG c-di-GMP Effector System Control Biofilm Formation by Bordetella bronchiseptica

et al. 2016

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“…Strain CVO also increased expression of a type I secretion system and a gene for an RTX‐related protein, both gene products potentially involved in adhesion. RTX protein VCBS‐repeat and cadherin‐like domains have been shown to mediate binding to abiotic surfaces (Hinsa et al ., ; Nishikawa et al ., ). The domain structure of the RTX‐type protein in strain CVO and its elevated gene expression during S 0 oxidation suggest it could play a role in surface attachment.…”

Section: Discussionmentioning

confidence: 97%

Comparison of sulfide‐oxidizingSulfurimonasstrains reveals a new mode of thiosulfate formation in subsurface environments

Lahme

Callbeck

Eland

et al. 2020

Environmental Microbiology

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Sulfur-oxidizing Sulfurimonas spp. are widespread in sediments, hydrothermal vent fields, aquifers and subsurface environments such as oil reservoirs where they play an important role in the sulfur cycle. We determined the genome sequence of the oil field isolate Sulfurimonas sp. strain CVO and compared its gene expression during nitrate-dependent sulfide oxidation to the coastal sediment isolate Sulfurimonas denitrificans. Formation of elemental sulfur (S 0 ) and high expression of sulfide quinone oxidoreductase (SQR) genes indicates that sulfide oxidation in both strains is mediated by SQR. Subsequent oxidation of S 0 was achieved by the sulfur oxidation enzyme complex (SOX). In the coastal S. denitrificans, the genes are arranged and expressed as two clusters: soxXY 1 Z 1 AB and soxCDY 2 Z 2 H, and sulfate was the sole metabolic end product. By contrast, the oil field strain CVO has only the soxCDY 2 Z 2 H cluster and not soxXY 1 Z 1 AB. Despite the absence of the soxXY 1 Z 1 AB cluster, strain CVO oxidized S 0 to thiosulfate and sulfate, demonstrating that soxCDY 2 Z 2 H genes alone are sufficient for S 0 oxidation in Sulfurimonas spp. and that thiosulfate is an additional metabolic end product. Screening of publicly available metagenomes revealed that Sulfurimonas spp. with only the soxCDY 2 Z 2 H cluster are widespread suggesting this mechanism of thiosulfate formation is environmentally significant.

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“…However, recent studies indicate that Bordetella cells do experience Bvg2 conditions in vivo (Mason et al, 2013;Hoo et al, 2014, Dewan et al, 2017. In another study, investigators identified B. bronchiseptica brtA, a lapA ortholog, and demonstrated it was a Bvg2 phase gene involved in biofilm formation and expressed in infected rat trachea (Nishikawa et al, 2016). Although we could find no reports of the concentrations of Na in a mammalian respiratory tract, eukaryotic cells have cycling pathways that excrete pyridines and NAD breakdown products for later use in NAD synthesis (Nikiforov et al, 2015), so it is reasonable to hypothesize that Na may be present extracellularly in the host.…”

Section: Discussionmentioning

confidence: 99%

The Bordetella bronchiseptica nic locus encodes a nicotinic acid degradation pathway and the 6‐hydroxynicotinate‐responsive regulator BpsR

Brickman

Armstrong

2018

Molecular Microbiology

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The classical Bordetella species use amino acids as carbon sources and can catabolize organic acids and tricarboxylic acid cycle intermediates. They are also auxotrophic for nicotinamide adenine dinucleotide (NAD) pathway precursors such as nicotinic acid. Bordetellae have a putative nicotinate catabolism gene locus highly similar to that characterized in Pseudomonas putida KT2440. This study determined the distribution of the nic genes among Bordetella species and analyzed the regulation of this nicotinic acid degradation system. Transcription of the Bordetella bronchiseptica nicC gene was repressed by the NicR ortholog, BpsR, previously shown to regulate extracellular polysaccharide synthesis genes. nicC expression was derepressed by nicotinic acid or by the first product of the degradation pathway, 6-hydroxynicotinic acid, which was shown to be the inducer. Results using mutants with either a hyperactivated pathway or an inactivated pathway showed a marked effect on growth on nicotinic acid that indicated this degradation pathway influences NAD biosynthesis. Pathway dysregulation also affected Bordetella BvgAS-mediated virulence gene regulation, demonstrating that fluctuation of intracellular nicotinic acid pools impacts Bvg phase transition responses.

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The bvg‐repressed gene brtA, encoding biofilm‐associated surface adhesin, is expressed during host infection by Bordetella bronchiseptica

Cited by 27 publications

References 50 publications

Homologs of the LapD-LapG c-di-GMP Effector System Control Biofilm Formation by Bordetella bronchiseptica

Homologs of the LapD-LapG c-di-GMP Effector System Control Biofilm Formation by Bordetella bronchiseptica

Comparison of sulfide‐oxidizingSulfurimonasstrains reveals a new mode of thiosulfate formation in subsurface environments

The Bordetella bronchiseptica nic locus encodes a nicotinic acid degradation pathway and the 6‐hydroxynicotinate‐responsive regulator BpsR

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