Characterization and Virulence of Hemolysin III from Vibrio vulnificus

Chen, Yu-Chung; Chang, Mau Song; Chuang, Yin-Ching; Jeang, Chii-Ling

doi:10.1007/s00284-004-4288-5

Cited by 49 publications

(44 citation statements)

References 27 publications

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“…TMX is a conserved, single-domain protein of unknown function that is homologous to a hemolysin III-related (HlyIII) protein in Bacillus cereus (26,27). Some evidence, obtained using recombinantly expressed HlyIII proteins in the heterologous E. coli background, suggested that HlyIII-related proteins function as hemolysins (28), but their presence in all bacteria makes this hypothesis unlikely. The function of HlyIII proteins has not been conclusively determined (29), but they were shown to be distant homologs of adipoR receptors found in yeasts and humans (29), the function of which also remains to be established.…”

Section: Discussionmentioning

confidence: 99%

Distinct Domains of CheA Confer Unique Functions in Chemotaxis and Cell Length in Azospirillum brasilense Sp7

2017

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Chemotaxis is the movement of cells in response to gradients of diverse chemical cues. Motile bacteria utilize a conserved chemotaxis signal transduction system to bias their motility and navigate through a gradient. A central regulator of chemotaxis is the histidine kinase CheA. This cytoplasmic protein interacts with membrane-bound receptors, which assemble into large polar arrays, to propagate the signal. In the alphaproteobacterium Azospirillum brasilense, Che1 controls transient increases in swimming speed during chemotaxis, but it also biases the cell length at division. However, the exact underlying molecular mechanisms for Che1-dependent control of multiple cellular behaviors are not known. Here, we identify specific domains of the CheA1 histidine kinase implicated in modulating each of these functions. We show that CheA1 is produced in two isoforms: a membraneanchored isoform produced as a fusion with a conserved seven-transmembrane domain of unknown function (TMX) at the N terminus and a soluble isoform similar to prototypical CheA. Site-directed and deletion mutagenesis combined with behavioral assays confirm the role of CheA1 in chemotaxis and implicate the TMX domain in mediating changes in cell length. Fluorescence microscopy further reveals that the membrane-anchored isoform is distributed around the cell surface while the soluble isoform localizes at the cell poles. Together, the data provide a mechanism for the role of Che1 in controlling multiple unrelated cellular behaviors via acquisition of a new domain in CheA1 and production of distinct functional isoforms.IMPORTANCE Chemotaxis provides a significant competitive advantage to bacteria in the environment, and this function has been transferred laterally multiple times, with evidence of functional divergence in different genomic contexts. The molecular principles that underlie functional diversification of chemotaxis in various genomic contexts are unknown. Here, we provide a molecular mechanism by which a single CheA protein controls two unrelated functions: chemotaxis and cell length. Acquisition of this multifunctionality is seemingly a recent evolutionary event. The findings illustrate a mechanism by which chemotaxis function may be co-opted to regulate additional cellular functions.

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Section: Discussionmentioning

confidence: 99%

Distinct Domains of CheA Confer Unique Functions in Chemotaxis and Cell Length in Azospirillum brasilense Sp7

2017

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“…The type III hemolysin, a virulence factor in numerous pathogenesis, is an integral outer membrane protein with hemolytic activity. 100,101 Lipopolysaccarides (LPS) is an outer membrane virulence factor of C. sakazakii, which interacts with enterocytes through LPS mediated binding to TLR4 inducing NEC in animals. [102][103][104][105] In the NEC patients, the elevated level of LPS in serum and stools has been reported.…”

Section: Biofilm Formationmentioning

confidence: 99%

Insights into virulence factors determining the pathogenicity ofCronobacter sakazakii

2015

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“…P. falciparum hemolysin III (PfHly III) is located on chromosome 14. Homologues have been identified in all Plasmodium genomes sequenced, including P. vivax, P. yoelii, P. berghei, and P. knowlesi, as well as Toxoplasma and Babesia genomes.…”

mentioning

confidence: 99%

“…Mass spectrometry detected PfHly III in gametocytes (11). From Bacillus cereus and Vibrio vulnificus Hly III studies, Hly III was shown to be a pore-forming protein, 3 to 3.5 nm in diameter, with optimal hemolysis at 37°C (12)(13)(14). Over evolutionary time, hemolysins have adapted essential transport roles in Plasmodium, contrasting with their ancient bacterial pore-forming cytotoxic effect.…”

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confidence: 99%

Erythrocyte Lysis and Xenopus laevis Oocyte Rupture by Recombinant Plasmodium falciparum Hemolysin III

et al. 2014

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Malaria kills more than 1 million people per year worldwide, with severe malaria anemia accounting for the majority of the deaths. Malaria anemia is multifactorial in etiology, including infected erythrocyte destruction and decrease in erythrocyte production, as well as destruction or clearance of noninfected erythrocytes. We identified a panspecies Plasmodium hemolysin type III related to bacterial hemolysins. The identification of a hemolysin III homologue in Plasmodium suggests a potential role in host erythrocyte lysis. Here, we report the first characterization of Plasmodium falciparum hemolysin III, showing that the soluble recombinant P. falciparum hemolysin III is a pore-forming protein capable of lysing human erythrocytes in a dose-, time-, and temperature-dependent fashion. The recombinant P. falciparum hemolysin III-induced hemolysis was partially inhibited by glibenclamide, a known channel antagonist. Studies with polyethylene glycol molecules of different molecular weights indicated a pore size of approximately 3.2 nm. Heterologous expression of recombinant P. falciparum hemolysin III in Xenopus oocytes demonstrated early hypotonic lysis similar to that of the pore-forming aquaporin control. Live fluorescence microscopy localized transfected recombinant green fluorescent protein (GFP)-tagged P. falciparum hemolysin III to the essential digestive vacuole of the P. falciparum parasite. These transfected trophozoites also possessed a swollen digestive vacuole phenotype. Native Plasmodium hemolysin III in the digestive vacuole may contribute to lysis of the parasitophorous vacuole membrane derived from the host erythrocyte. After merozoite egress from infected erythrocytes, remnant P. falciparum hemolysin III released from digestive vacuoles could potentially contribute to lysis of uninfected erythrocytes to contribute to severe life-threatening anemia.

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Characterization and Virulence of Hemolysin III from Vibrio vulnificus

Cited by 49 publications

References 27 publications

Distinct Domains of CheA Confer Unique Functions in Chemotaxis and Cell Length in Azospirillum brasilense Sp7

Distinct Domains of CheA Confer Unique Functions in Chemotaxis and Cell Length in Azospirillum brasilense Sp7

Insights into virulence factors determining the pathogenicity ofCronobacter sakazakii

Erythrocyte Lysis and Xenopus laevis Oocyte Rupture by Recombinant Plasmodium falciparum Hemolysin III

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