Functional Analysis of the Thioredoxin Domain in<i>Porphyromonas gingivalis</i>HBP35

Shiroza, Teruaki; Okano, Soichiro; Shibata, Yasuko; Hayakawa, Mitsuo; Fujita, Ken‐ichi; Yamaguchi, Kosuke; Abiko, Yoshimitsu

doi:10.1271/bbb.80101

Cited by 8 publications

(10 citation statements)

References 21 publications

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“…[12] have shown that an hbp35 gene-containing plasmid complemented the defects in motility and alkaline phosphatase activity of an E. coli dsbA mutant. This finding indicates that HBP35 is exported to the periplasm in a dsbA mutant and plays a role in the disulfide bond formation [13].…”

Section: Resultsmentioning

confidence: 99%

Characterization of hemin-binding protein 35 (HBP35) in Porphyromonas gingivalis: its cellular distribution, thioredoxin activity and role in heme utilization

et al. 2010

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BackgroundThe periodontal pathogen Porphyromonas gingivalis is an obligate anaerobe that requires heme for growth. To understand its heme acquisition mechanism, we focused on a hemin-binding protein (HBP35 protein), possessing one thioredoxin-like motif and a conserved C-terminal domain, which are proposed to be involved in redox regulation and cell surface attachment, respectively.ResultsWe observed that the hbp35 gene was transcribed as a 1.1-kb mRNA with subsequent translation resulting in three proteins with molecular masses of 40, 29 and 27 kDa in the cytoplasm, and one modified form of the 40-kDa protein on the cell surface. A recombinant 40-kDa HBP35 exhibited thioredoxin activity in vitro and mutation of the two putative active site cysteine residues abolished this activity. Both recombinant 40- and 27-kDa proteins had the ability to bind hemin, and growth of an hbp35 deletion mutant was substantially retarded under hemin-depleted conditions compared with growth of the wild type under the same conditions.ConclusionP. gingivalis HBP35 exhibits thioredoxin and hemin-binding activities and is essential for growth in hemin-depleted conditions suggesting that the protein plays a significant role in hemin acquisition.

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Section: Resultsmentioning

confidence: 99%

Characterization of hemin-binding protein 35 (HBP35) in Porphyromonas gingivalis: its cellular distribution, thioredoxin activity and role in heme utilization

et al. 2010

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“…HBP35 is a hemin-binding T9SS substrate that is necessary for efficient growth under limited hemin conditions (Shibata et al, 2003;Shoji et al, 2010). Furthermore, HBP35 was shown to exhibit thioredoxin activity (Shiroza et al, 2008;Shoji et al, 2010). Anti-HBP35 antibodies inhibit P. gingivalis hemagglutination, adherence to epithelial cells, hemin binding and cell growth (Hiratsuka et al, 2010;Shibata et al, 2011).…”

Section: Structure and Function Of T9ss Substratesmentioning

confidence: 99%

Type IX secretion: the generation of bacterial cell surface coatings involved in virulence, gliding motility and the degradation of complex biopolymers

Veith

Glew

Gorasia

et al. 2017

Molecular Microbiology

121

124

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Summary The Type IX secretion system (T9SS) is present in over 1000 sequenced species/strains of the Fibrobacteres‐Chlorobi‐Bacteroidetes superphylum. Proteins secreted by the T9SS have an N‐terminal signal peptide for translocation across the inner membrane via the SEC translocon and a C‐terminal signal for secretion across the outer membrane via the T9SS. Nineteen protein components of the T9SS have been identified including three, SigP, PorX and PorY that are involved in regulation. The inner membrane proteins PorL and PorM and the outer membrane proteins PorK and PorN interact and a complex comprising PorK and PorN forms a large ring structure of 50 nm in diameter. PorU, PorV, PorQ and PorZ form an attachment complex on the cell surface of the oral pathogen, Porphyromonas gingivalis. P. gingivalis T9SS substrates bind to PorV suggesting that after translocation PorV functions as a shuttle protein to deliver T9SS substrates to the attachment complex. The PorU component of the attachment complex is a novel Gram negative sortase which catalyses the cleavage of the C‐terminal signal and conjugation of the protein substrates to lipopolysaccharide, anchoring them to the cell surface. This review presents an overview of the T9SS focusing on the function of T9SS substrates and machinery components.

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“…A computer‐aided motif search indicated that HBP35 was composed of several functional domains, including the most prominent amino‐acid stretch, WCGYCP, which was identified near the N‐terminal end, whereas the conserved motif of the active center, WCGxCx, has been found in many thioredoxins (13; Fig. 2A).…”

Section: Resultsmentioning

confidence: 99%

“…The reversible redox reaction occurring at the Cys residues provides chemical potential for a number of biological reactions. We further characterized HBP35 by amino‐acid substitution, and our findings clearly suggested that it is involved in disulfide bond formation in P. gingivalis (13).…”

mentioning

confidence: 75%

“…Six kinds of Cys residue‐mutated rHBP35 proteins ( 48 Cys to Ser, 51 Cys to Ser, 113 Cys to Ser, 161 Cys to Ser, both 48 Cys and 51 Cys to Ser, and both 113 Cys and 161 Cys to Ser) were constructed using the method of Shiroza et al. (13). The Cys‐modified rHBP35 proteins were purified to near homogeneity from sonicates of E. coli transformants harboring the respective plasmids, as previously reported (8).…”

Section: Methodsmentioning

confidence: 99%

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Characterization of human‐type monoclonal antibodies against reduced form of hemin binding protein 35 from Porphyromonas gingivalis

Shibata¹,

Okano²,

Shiroza

et al. 2011

J of Periodontal Research

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Functional Analysis of the Thioredoxin Domain inPorphyromonas gingivalisHBP35

Cited by 8 publications

References 21 publications

Characterization of hemin-binding protein 35 (HBP35) in Porphyromonas gingivalis: its cellular distribution, thioredoxin activity and role in heme utilization

Characterization of hemin-binding protein 35 (HBP35) in Porphyromonas gingivalis: its cellular distribution, thioredoxin activity and role in heme utilization

Type IX secretion: the generation of bacterial cell surface coatings involved in virulence, gliding motility and the degradation of complex biopolymers

Characterization of human‐type monoclonal antibodies against reduced form of hemin binding protein 35 from Porphyromonas gingivalis

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