Integration of multiple domains in a two-component sensor protein: the Bordetella pertussis BvgAS phosphorelay.

Uhl, Michaël; Miller, Jeff F.

doi:10.1002/j.1460-2075.1996.tb00440.x

Cited by 218 publications

(199 citation statements)

References 56 publications

(59 reference statements)

Supporting

Mentioning

189

Contrasting

Unclassified

Order By: Relevance

“…Expression of most virulence factors in Bordetella is regulated by the well-described BvgAS system (Mattoo et al, 2001;Uhl & Miller, 1996). During the Bvg + phase, BvgAS is activated and virulence factors -including filamentous haemagglutinin (FHA), pertussis toxin (PTX) and adenylate cyclase toxin (CyaA) -are expressed; this phase is required to establish an infection in a host organism.…”

Section: Introductionmentioning

confidence: 99%

Role of (p)ppGpp in biofilm formation and expression of filamentous structures in Bordetella pertussis

et al. 2013

View full text Add to dashboard Cite

Bordetella pertussis, the causative agent of whooping cough, is highly adapted to cause human infection. The production of virulence factors, such as adhesins and toxins, is just part of an array of mechanisms by which B. pertussis causes infection. The stringent response is a global bacterial response to nutritional limitation that is mediated by the accumulation of cellular ppGpp and pppGpp [termed together as (p)ppGpp]. Here, we demonstrate that production of (p)ppGpp was controlled by RelA and SpoT proteins in B. pertussis, and that mutation-induced loss of both proteins together caused deficiencies in (p)ppGpp production. The (p)ppGpp-deficient mutants also exhibited defects in growth regulation, decreases in viability under nutritionally limited conditions, increases in susceptibility to oxidative stress and defects in biofilm formation. Analysis of the secreted proteins and the respective transcripts showed that lack of (p)ppGpp led to decreased expression of fim3 and bsp22, which encode a fimbrial subunit and the selfpolymerizing type III secretion system tip protein, respectively. Moreover, electron microscopic analysis also indicated that (p)ppGpp regulated the formation of filamentous structures. Most virulence genes -including fim3 and bsp22 -were expressed in the Bvg + phase during which the BvgAS two-component system was activated. Although fim3 and bsp22 were downregulated in a (p)ppGpp-deficient mutant, normal expression of fhaB, cyaA and ptxA persisted. Lack of coherence between virulence gene expression and (p)ppGpp production indicated that (p)ppGpp did not modulate the Bvg phase. Taken together, our data indicate that (p)ppGpp may govern an as-yet-unrecognized system that influences B. pertussis pathogenicity.

show abstract

Section: Introductionmentioning

confidence: 99%

Role of (p)ppGpp in biofilm formation and expression of filamentous structures in Bordetella pertussis

et al. 2013

View full text Add to dashboard Cite

show abstract

“…Prn is expressed only when induced by the BvgAS two-component virulence control system (1). In the absence of Prn expression, BPP-1 can switch its infectious specificity, or tropism, by altering the major tropism determinant (mtd) gene.…”

mentioning

confidence: 99%

“…This gene encodes the protein responsible for receptor binding (2). Mtd variants are generated at high frequency by a diversity-generating retroelement (DGR) (1)(2)(3)(4). This DGR creates a mutant copy of an invariant DNA template repeat (TR) by transcription and reverse transcription.…”

mentioning

confidence: 99%

Three-dimensional structure of tropism-switching Bordetella bacteriophage

Dai¹,

Hodes²,

Hui³

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Bacteriophage BPP-1, which infects Bordetella species, can switch its specificity by mutations to the ligand-binding surface of its major tropism-determinant protein, Mtd. This targeted mutagenesis results from the activity of a phage-encoded diversity-generating retroelement. Purified Mtd binds its receptor with low affinity, yet BPP-1 binding and infection of Bordettella cells are efficient because of high-avidity binding between phage-associated Mtd and its receptor. Here, using an integrative approach of three-dimensional (3D) structural analyses of the entire phage by cryo-electron tomography and single-prticle cryo-electron microscopy, we provide direct localization of Mtd in the phage and the structural basis of the high-avidity binding of the BPP-1 phage. Our structure shows that each BPP-1 particle has a T = 7 icosahedral head and an unusual tail apparatus consisting of a short central tail "hub," six short tail spikes, and six extended tail fibers. Subtomographic averaging of the tail fiber maps revealed a two-lobed globular structure at the distal end of each long tail fiber. Tomographic reconstructions of immuno-gold-labeled BPP-1 directly localized Mtd to these globular structures. Finally, our icosahedral reconstruction of the BPP-1 head at 7Å resolution reveals an HK97-like major capsid protein stabilized by a smaller cementing protein. Our structure represents a unique bacteriophage reconstruction with its tail fibers and ligand-binding domains shown in relation to its tail apparatus. The localization of Mtd at the distal ends of the six tail fibers explains the high avidity binding of Mtd molecules to cell surfaces for initiation of infection.avidity | Bordetella phage | cryo-electron microscopy | tropism-determinant protein

show abstract

“…While transmitter and receiver domains were identified in both gene products, only CblT is predicted to have an HPt domain, known to be required for the transfer of phosphoryl groups to the receiver domain of the cognate response regulators in other phosphorelay pathways ( Fig. 2) (3,11,20,42). The lack of an HPt domain in CblS suggests that the potential transfer of phosphoryl groups from CblS to CblR must occur through an intermediate protein, which has a functional HPt domain.…”

Section: Discussionmentioning

confidence: 99%

Genetic Characterization of a Multicomponent Signal Transduction System Controlling the Expression of Cable Pili in Burkholderia cenocepacia

Tomich

Mohr

2004

J Bacteriol

View full text Add to dashboard Cite

Cable pili are peritrichous organelles expressed by certain strains of Burkholderia cenocepacia, believed to facilitate colonization of the lower respiratory tract in cystic fibrosis patients. The B. cenocepacia cblBACDS operon encodes the structural and accessory proteins required for the assembly of cable pili, as well as a gene designated cblS, predicted to encode a hybrid sensor kinase protein of bacterial two-component signal transduction systems. In this study we report the identification of two additional genes, designated cblT and cblR, predicted to encode a second hybrid sensor kinase and a response regulator, respectively. Analyses of the deduced amino acid sequences of the cblS and cblT gene products revealed that both putative sensor kinases have transmitter and receiver domains and that the cblT gene product has an additional C-terminal HPt domain. Mutagenesis of the cblS, cblT, or cblR gene led to a block in expression of CblA, the major pilin subunit, and a severe decrease in cblA transcript abundance. Using transcriptional fusion analyses, the decrease in the abundance of the cblA transcript in the cblS, cblT, and cblR mutants was shown to be due to a block in transcription from the cblB-proximal promoter, located upstream of the cblBACDS operon. Furthermore, ectopic expression of either cblS or cblR in wild-type B. cenocepacia strain BC7 led to a significant increase, while ectopic expression of cblT resulted in a dramatic decrease, in abundance of the CblA major pilin and the cblA transcript. Our results demonstrate that the B. cenocepacia cblS, cblT, and cblR genes are essential for cable pilus expression and that their effect is exerted at the level of transcription of the cblBACDS operon. These findings are consistent with the proposed function of the cblSTR gene products as a multicomponent signal transduction pathway controlling the expression of cable pilus biosynthetic genes in B. cenocepacia.

show abstract

Integration of multiple domains in a two-component sensor protein: the Bordetella pertussis BvgAS phosphorelay.

Cited by 218 publications

References 56 publications

Role of (p)ppGpp in biofilm formation and expression of filamentous structures in Bordetella pertussis

Role of (p)ppGpp in biofilm formation and expression of filamentous structures in Bordetella pertussis

Three-dimensional structure of tropism-switching Bordetella bacteriophage

Genetic Characterization of a Multicomponent Signal Transduction System Controlling the Expression of Cable Pili in Burkholderia cenocepacia

Contact Info

Product

Resources

About