Proteomic and bioinformatic analysis of outer membrane proteins of the protobacterium Bartonella henselae (Bartonellaceae)

Dm, Li; Qy, Liu; Zhao, Fei; Hu, Yanyan; Xiao, Deng; Yx, Gu; Xp, Song; Jz, Zhang

doi:10.4238/vol10-3gmr1153

Cited by 12 publications

(7 citation statements)

References 37 publications

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“…We failed to detect HbpB in B. henselae using the western blot method. This result is in good agreement with those of proteomic analysis of outer membrane fractions of B. henselae and B. quintana [51], [52], [53], [54], [55], [56], which showed that HbpB was not detectable using this method. Since HbpA is the most abundant Hbp in B. henselae [52], [51], we checked its level in B. henselae pNS2Trc and B. henselae pNS2Trc ::hbpA AS using mouse antibody directed against HbpB.…”

Section: Resultssupporting

confidence: 90%

Heme Binding Proteins of Bartonella henselae Are Required when Undergoing Oxidative Stress During Cell and Flea Invasion

et al. 2012

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Bartonella are hemotropic bacteria responsible for emerging zoonoses. These heme auxotroph alphaproteobacteria must import heme for their growth, since they cannot synthesize it. To import exogenous heme, Bartonella genomes encode for a complete heme uptake system enabling transportation of this compound into the cytoplasm and degrading it to release iron. In addition, these bacteria encode for four or five outer membrane heme binding proteins (Hbps). The structural genes of these highly homologous proteins are expressed differently depending on oxygen, temperature and heme concentrations. These proteins were hypothesized as being involved in various cellular processes according to their ability to bind heme and their regulation profile. In this report, we investigated the roles of the four Hbps of Bartonella henselae, responsible for cat scratch disease. We show that Hbps can bind heme in vitro. They are able to enhance the efficiency of heme uptake when co-expressed with a heme transporter in Escherichia coli. Using B. henselae Hbp knockdown mutants, we show that these proteins are involved in defense against the oxidative stress, colonization of human endothelial cell and survival in the flea.

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Section: Resultssupporting

confidence: 90%

Heme Binding Proteins of Bartonella henselae Are Required when Undergoing Oxidative Stress During Cell and Flea Invasion

et al. 2012

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“…The proteomes of whole cells and subcellular fractions of B. quintana and B. henselae have been analyzed by two-dimensional gel electrophoresis and MALDI-TOF-MS of the protein spots. For example, two studies identified 44 [164] and 53 [165] proteins associated with the B. henselae outer membrane fractions. A third study analyzed the B. quintana membrane subproteome and found 60 proteins [166].…”

Section: Diagnostics and Identificationmentioning

confidence: 99%

Oroya Fever and Verruga Peruana: Bartonelloses Unique to South America

et al. 2014

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Bartonella bacilliformis is the bacterial agent of Carrión's disease and is presumed to be transmitted between humans by phlebotomine sand flies. Carrión's disease is endemic to high-altitude valleys of the South American Andes, and the first reported outbreak (1871) resulted in over 4,000 casualties. Since then, numerous outbreaks have been documented in endemic regions, and over the last two decades, outbreaks have occurred at atypical elevations, strongly suggesting that the area of endemicity is expanding. Approximately 1.7 million South Americans are estimated to be at risk in an area covering roughly 145,000 km2 of Ecuador, Colombia, and Peru. Although disease manifestations vary, two disparate syndromes can occur independently or sequentially. The first, Oroya fever, occurs approximately 60 days following the bite of an infected sand fly, in which infection of nearly all erythrocytes results in an acute hemolytic anemia with attendant symptoms of fever, jaundice, and myalgia. This phase of Carrión's disease often includes secondary infections and is fatal in up to 88% of patients without antimicrobial intervention. The second syndrome, referred to as verruga peruana, describes the endothelialcell-derived, blood-filled tumors that develop on the surface of the skin. Verrugae are rarely fatal, but can bleed and scar the patient. Moreover, these persistently infected humans provide a reservoir for infecting sand flies and thus maintaining B. bacilliformis in nature. Here, we discuss the current state of knowledge regarding this life-threatening, neglected bacterial pathogen and review its host-cell parasitism, molecular pathogenesis, phylogeny, sand fly vectors, diagnostics, and prospects for control.

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“…Second, our expressed proteome encompassed all proteins identified in three previous B. henselae proteomics studies (Rhomberg et al 2004;Eberhardt et al 2009;Li et al 2011), while adding many more low-abundance proteins (Supplemental Fig. S6A-C).…”

Section: Evidence For Having Reached An Expressed Proteome Endpointmentioning

confidence: 99%

Directed shotgun proteomics guided by saturated RNA-seq identifies a complete expressed prokaryotic proteome

et al. 2013

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Prokaryotes, due to their moderate complexity, are particularly amenable to the comprehensive identification of the protein repertoire expressed under different conditions. We applied a generic strategy to identify a complete expressed prokaryotic proteome, which is based on the analysis of RNA and proteins extracted from matched samples. Saturated transcriptome profiling by RNA-seq provided an endpoint estimate of the protein-coding genes expressed under two conditions which mimic the interaction of Bartonella henselae with its mammalian host. Directed shotgun proteomics experiments were carried out on four subcellular fractions. By specifically targeting proteins which are short, basic, low abundant, and membrane localized, we could eliminate their initial underrepresentation compared to the estimated endpoint. A total of 1250 proteins were identified with an estimated false discovery rate below 1%. This represents 85% of all distinct annotated proteins and 90% of the expressed protein-coding genes. Genes that were detected at the transcript but not protein level, were found to be highly enriched in several genomic islands. Furthermore, genes that lacked an ortholog and a functional annotation were not detected at the protein level; these may represent examples of overprediction in genome annotations. A dramatic membrane proteome reorganization was observed, including differential regulation of autotransporters, adhesins, and hemin binding proteins. Particularly noteworthy was the complete membrane proteome coverage, which included expression of all members of the VirB/D4 type IV secretion system, a key virulence factor.

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Proteomic and bioinformatic analysis of outer membrane proteins of the protobacterium Bartonella henselae (Bartonellaceae)

Cited by 12 publications

References 37 publications

Heme Binding Proteins of Bartonella henselae Are Required when Undergoing Oxidative Stress During Cell and Flea Invasion

Heme Binding Proteins of Bartonella henselae Are Required when Undergoing Oxidative Stress During Cell and Flea Invasion

Oroya Fever and Verruga Peruana: Bartonelloses Unique to South America

Directed shotgun proteomics guided by saturated RNA-seq identifies a complete expressed prokaryotic proteome

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