Genomic Recombination through Plasmid-Encoded Recombinase Enhances Hemolytic Activity and Adherence to Epithelial Cells in the Periodontopathogenic Bacterium<i>Eikenella corrodens</i>

Matsunaga, Tetsuro; Nakayuki, Ayumi; Saito, Yuki; Kato, Akio; Noiri, Yuichiro; Ebisu, Shigeyuki; Azakami, Hiroyuki

doi:10.1271/bbb.100866

Cited by 4 publications

(4 citation statements)

References 39 publications

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“…In healthy human serum, extracellular Hb concentrations up to 3 μM have been observed and this probably increases during infection due to increased haemolysis 47 . Significantly, both Kingella species and E. corrodens are β-haemolytic 48 49 and E. corrodens is commonly observed in coinfections with haemolytic Gram-positive bacteria 50 51 . Although the meningococcus is not observed to be haemolytic, even a small amount of haemolysis as a consequence of sepsis would significantly increase serum Hb levels.…”

Section: Discussionmentioning

confidence: 99%

Structural analysis of haemoglobin binding by HpuA from the Neisseriaceae family

Wong

Gupta

et al. 2015

Nat Commun

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The Neisseriaceae family of bacteria causes a range of diseases including meningitis, septicaemia, gonorrhoea and endocarditis, and extracts haem from haemoglobin as an important iron source within the iron-limited environment of its human host. Herein we report crystal structures of apo- and haemoglobin-bound HpuA, an essential component of this haem import system. The interface involves long loops on the bacterial receptor that present hydrophobic side chains for packing against the surface of haemoglobin. Interestingly, our structural and biochemical analyses of Kingella denitrificans and Neisseria gonorrhoeae HpuA mutants, although validating the interactions observed in the crystal structure, show how Neisseriaceae have the fascinating ability to diversify functional sequences and yet retain the haemoglobin binding function. Our results present the first description of HpuA's role in direct binding of haemoglobin.

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Section: Discussionmentioning

confidence: 99%

Structural analysis of haemoglobin binding by HpuA from the Neisseriaceae family

Wong

Gupta

et al. 2015

Nat Commun

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“…Previously, we have reported that genomic recombination by a plasmid-mediated recombinase enhances the GalNAc-dependent lectin activity in parallel with the hemolytic activity in E. corrodens ATCC 23834. 11,12) These data suggested that the hemolytic activity is correlated with the lectin activity. To elucidate this, we measured the hemolytic activity of recombinant HlyA in the absence and presence of 3-mM GalNAc.…”

Section: Relationship Between Galnac-dependent Lectin Activity and Hementioning

confidence: 83%

“…11) Moreover, we have reported that this genomic recombination enhances the GalNAc-dependent lectin activity in parallel with the hemolytic activity of E. corrodens ATCC 23834. 11,12) However, the relationship between the Gal-NAc-dependent lectin activity and hemolytic activity of E. corrodens has not been understood yet.…”

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confidence: 99%

Purification and characterization of hemolysin from periodontopathogenic bacterium Eikenella corrodens strain 1073

Mansur

Takahara

Yamamoto

et al. 2017

Bioscience, Biotechnology, and Biochemistry

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Eikenella corrodens 1073 was found to show hemolytic activity when grown on sheep blood agar. A high and dose-dependent hemolytic activity was detected in the cell envelope fraction, which was further purified by ion-exchange and gel-filtration chromatography. Consequently, a 65-kDa protein with hemolytic activity was obtained, suggesting that this protein might be a hemolysin. Its N-terminal amino acid sequence was nearly identical to that of X-prolyl aminopeptidase from E. corrodens ATCC 23834. To confirm that X-prolyl aminopeptidase functions as a hemolytic factor, we expressed the hlyA gene, encoding X-prolyl aminopeptidase, in Escherichia coli. After induction with isopropyl β-D-1-thiogalactopyranoside, a protein of about 65 kDa was purified on a Ni column, and its hemolytic activity was confirmed. Meanwhile, a strain with a disrupted hlyA gene, which was constructed by homologous recombination, did not show any hemolytic activity. These results suggested that X-prolyl aminopeptidase might function as a hemolysin in E. corrodens.

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“…We reported previously that genomic recombination by plasmid-mediated recombinase stimulated simultaneous GalNAc-dependent lectin activity and hemolytic activity in E. corrodens 23834 [11] [12]. Recently, we demonstrated that hemolytic activity decreased upon addition of GalNAc [21].…”

Section: Effect Of Orf4 On Hemagglutination Activitymentioning

confidence: 99%

Genomic Recombination Enhances Pathogenic Factors in the Periodontopathogenic Bacterium <i>Eikenella corrodens</i>

Mansur¹,

Yamada²,

Morishige³

et al. 2017

AiM

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We reported previously that plasmid-mediated genomic recombination at the pilin gene locus increased hemagglutination activity, growth rate, biofilm formation, hemolytic activity, and adherence to epithelial cells in Eikenella corrodens 23834. To determine whether these enhancements were common in this bacterium, we introduced the recombinase gene ORF4 into seven clinically isolated strains. Genomic recombination at the type IV pilin gene locus was observed in strains 1080, L9B6, L8Ao3, and RV2 (group A), but not in strains 261-2, 612-L, and 257-4 (group B). Similarly, group A strains displayed changed colony morphology following loss of type IV pili, which was not observed in group B. Group A strains showed also enhanced hemagglutination activity, growth rate, hemolytic, activity and biofilm formation. These results suggest that ORF4-induced genomic recombination at the pilin gene locus is a general phenomenon in a part of E. corrodens, which likely stimulates pathogenicity and virulence.

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Genomic Recombination through Plasmid-Encoded Recombinase Enhances Hemolytic Activity and Adherence to Epithelial Cells in the Periodontopathogenic BacteriumEikenella corrodens

Cited by 4 publications

References 39 publications

Structural analysis of haemoglobin binding by HpuA from the Neisseriaceae family

Structural analysis of haemoglobin binding by HpuA from the Neisseriaceae family

Purification and characterization of hemolysin from periodontopathogenic bacterium Eikenella corrodens strain 1073

Genomic Recombination Enhances Pathogenic Factors in the Periodontopathogenic Bacterium <i>Eikenella corrodens</i>

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Genomic Recombination through Plasmid-Encoded Recombinase Enhances Hemolytic Activity and Adherence to Epithelial Cells in the Periodontopathogenic BacteriumEikenella corrodens

Cited by 4 publications

References 39 publications

Structural analysis of haemoglobin binding by HpuA from the Neisseriaceae family

Structural analysis of haemoglobin binding by HpuA from the Neisseriaceae family

Purification and characterization of hemolysin from periodontopathogenic bacterium Eikenella corrodens strain 1073

Genomic Recombination Enhances Pathogenic Factors in the Periodontopathogenic Bacterium &lt;i&gt;Eikenella corrodens&lt;/i&gt;

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Genomic Recombination Enhances Pathogenic Factors in the Periodontopathogenic Bacterium <i>Eikenella corrodens</i>