バクテロイデーテス門細菌のIX型分泌機構およびV型線毛の研究
Bacteroidetes門にはBacteroides属, Prevotella属, Porphyromonas属等, ヒトに共生・寄生する多くの細菌が含まれる。私たちはPorphyromonas属に含まれる歯周病原細菌であるPorphyromonas gingivalisの主要な分泌性プロテアーゼであるジンジパインおよび宿主定着性に寄与する線毛について研究を進めてきた。その過程でジンジパインは従来報告されていない分泌機構で分泌されることがわかった。さらにこの分泌機構はBacteroidetes門細菌に広く存在する機構であることやBacteroidetes門細菌の滑走運動と密接な関係があること...
Saved in:
| Published in | Nihon saikingaku zasshi Vol. 72; no. 4; pp. 219 - 227 |
|---|---|
| Main Author | |
| Format | Journal Article |
| Language | Japanese |
| Published |
Tokyo
日本細菌学会
01.01.2017
Japan Science and Technology Agency |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0021-4930 1882-4110 |
| DOI | 10.3412/jsb.72.219 |
Cover
| Abstract | Bacteroidetes門にはBacteroides属, Prevotella属, Porphyromonas属等, ヒトに共生・寄生する多くの細菌が含まれる。私たちはPorphyromonas属に含まれる歯周病原細菌であるPorphyromonas gingivalisの主要な分泌性プロテアーゼであるジンジパインおよび宿主定着性に寄与する線毛について研究を進めてきた。その過程でジンジパインは従来報告されていない分泌機構で分泌されることがわかった。さらにこの分泌機構はBacteroidetes門細菌に広く存在する機構であることやBacteroidetes門細菌の滑走運動と密接な関係があることがわかり, Por分泌機構（のちにIX型分泌機構と改名）と命名された。また, 線毛については線毛タンパク質がリポタンパク質として菌体表面に輸送され, アルギニン・ジンジパインによって限定分解されることで線毛形成が生じることがわかった。この新規の形成機構を有する線毛はBacteroides属をはじめBacteroidetes門Bacteroidia綱の細菌に広く存在することがわかり, V型線毛と命名された。 |
|---|---|
| AbstractList | Bacteroidetes門にはBacteroides属, Prevotella属, Porphyromonas属等, ヒトに共生・寄生する多くの細菌が含まれる。私たちはPorphyromonas属に含まれる歯周病原細菌であるPorphyromonas gingivalisの主要な分泌性プロテアーゼであるジンジパインおよび宿主定着性に寄与する線毛について研究を進めてきた。その過程でジンジパインは従来報告されていない分泌機構で分泌されることがわかった。さらにこの分泌機構はBacteroidetes門細菌に広く存在する機構であることやBacteroidetes門細菌の滑走運動と密接な関係があることがわかり, Por分泌機構（のちにIX型分泌機構と改名）と命名された。また, 線毛については線毛タンパク質がリポタンパク質として菌体表面に輸送され, アルギニン・ジンジパインによって限定分解されることで線毛形成が生じることがわかった。この新規の形成機構を有する線毛はBacteroides属をはじめBacteroidetes門Bacteroidia綱の細菌に広く存在することがわかり, V型線毛と命名された。 Many bacteria symbiotic and parasitic in humans are included in the genera Bacteroides, Prevotella, Porphyromonas and others, which belong to the phylum Bacteroidetes. We have been studying gingipain, a major secretory protease of Porphyromonas gingivalis which is a periodontopathogenic bacterium belonging to the genus Porphyromonas, and pili which contribute to host colonization in the bacterium. In the process, it was found that gingipain was secreted by a system not reported previously. Furthermore, this secretion system was found to exist widely in the Bacteroidetes phylum bacteria and closely related to the gliding motility of bacteroidete bacteria, and it was named the Por secretion system (later renamed the type IX secretion system). Regarding P. gingivalis pili, it was found that the pilus protein is transported as a lipoprotein to the cell surface, and the pilus formation occurs due to degradation by arginine-gingipain. Pili with this novel formation mechanism was found to be widely present in bacteria belonging to the class Bacteroidia in the phylum Bacteroidetes and was named the type V pili. |
| Author | 中山, 浩次 |
| Author_xml | – sequence: 1 fullname: 中山, 浩次 organization: 長崎大学大学院医歯薬学総合研究科・口腔病原微生物学分野 |
| BookMark | eNo9kD9Lw1AUxR9SwVq7-BWcU-_70yYZHKT4p1BwqeIWXpIXbahtTdrBzSZQiy3oIA4K6iBIB61QUQS_zaOJfgtTKi7ncs79cS-cRZSqN-oCoWUMOcowWXV9M6eSHMH6HEpjTSMKwxhSKA1AsMJ0Cgso6_tVEwB0BhSraVSR4aUMRjLsyvBZBo8yPJPh19QGnz_Xp_Hb6_fFQHZeSvuTu_6k143Gg2h4Hz31ZedcBj3ZGe8li_jjJhrdJlj8cBUP35fQvMNrvsj-zQza3dyoFLeV8s5WqbheVlyiUlAcjlUbE2Jblq2xAnBeEFTnNs9jksfMdITt2EzlKsVMMJHQXAA3TbBBOEQr0Axamd1teo3jtvBbhttoe_XkpUEA54FSHSCh1maU67f4gTCaXvWIeycG91pVqyaMpDZDJQabStLdf24dcs9wOf0F6rGE4g |
| ContentType | Journal Article |
| Copyright | 2017 日本細菌学会 Copyright Japan Science and Technology Agency 2017 |
| Copyright_xml | – notice: 2017 日本細菌学会 – notice: Copyright Japan Science and Technology Agency 2017 |
| DBID | 7QL C1K K9. |
| DOI | 10.3412/jsb.72.219 |
| DatabaseName | Bacteriology Abstracts (Microbiology B) Environmental Sciences and Pollution Management ProQuest Health & Medical Complete (Alumni) |
| DatabaseTitle | ProQuest Health & Medical Complete (Alumni) Bacteriology Abstracts (Microbiology B) Environmental Sciences and Pollution Management |
| DatabaseTitleList | ProQuest Health & Medical Complete (Alumni) |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Biology |
| EISSN | 1882-4110 |
| EndPage | 227 |
| ExternalDocumentID | article_jsb_72_4_72_219_article_char_ja |
| GroupedDBID | 123 2WC ACPRK AFRAH ALMA_UNASSIGNED_HOLDINGS CS3 DU5 F5P JSF KQ8 MOJWN OK1 RJT 7QL C1K K9. |
| ID | FETCH-LOGICAL-j2730-fa17d122dccd8460aa6e39ada512514bfedfd47a7314e4ea17ae0abb0d0ef2863 |
| ISSN | 0021-4930 |
| IngestDate | Mon Jun 30 07:51:49 EDT 2025 Wed Sep 03 06:29:50 EDT 2025 |
| IsDoiOpenAccess | true |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 4 |
| Language | Japanese |
| LinkModel | OpenURL |
| MergedId | FETCHMERGED-LOGICAL-j2730-fa17d122dccd8460aa6e39ada512514bfedfd47a7314e4ea17ae0abb0d0ef2863 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 |
| OpenAccessLink | https://www.jstage.jst.go.jp/article/jsb/72/4/72_219/_article/-char/ja |
| PQID | 2015033900 |
| PQPubID | 2048499 |
| PageCount | 9 |
| ParticipantIDs | proquest_journals_2015033900 jstage_primary_article_jsb_72_4_72_219_article_char_ja |
| PublicationCentury | 2000 |
| PublicationDate | 20170101 |
| PublicationDateYYYYMMDD | 2017-01-01 |
| PublicationDate_xml | – month: 01 year: 2017 text: 20170101 day: 01 |
| PublicationDecade | 2010 |
| PublicationPlace | Tokyo |
| PublicationPlace_xml | – name: Tokyo |
| PublicationTitle | Nihon saikingaku zasshi |
| PublicationTitleAlternate | 日細菌誌 |
| PublicationYear | 2017 |
| Publisher | 日本細菌学会 Japan Science and Technology Agency |
| Publisher_xml | – name: 日本細菌学会 – name: Japan Science and Technology Agency |
| References | 40) Shoji, M., Sato, K., Yukitake, H., Kondo, Y., Narita, Y., Kadowaki, T., Naito, M., Nakayama, K. (2011): Por secretion system-dependent secretion and glycosylation of Porphyromonas gingivalis hemin-binding protein 35. PLoS One 6, e21372. 11) Kharade, S.S., McBride, M.J. (2015): Flavobacterium johnsoniae PorV is required for secretion of a subset of proteins targeted to the type IX secretion system. J. Bacteriol. 197, 147–158. 22) Nakayama, K. (2015): Porphyromonas gingivalis and related bacteria: from colonial pigmentation to the type IX secretion system and gliding motility. J. Periodontal Res. 50, 1–8. 42) Shoji, M., Shibata, Y., Shiroza, T., Yukitake, H., Peng, B., Chen, Y.-Y., Sato, K., Naito, M., Abiko, Y., Reynolds, E.C., Nakayama, K. (2010): Characterization of hemin-binding protein 35 (HBP35) in Porphyromonas gingivalis: its cellular distribution, thioredoxin activity and role in heme utilization. BMC Microbiol. 10, 152. 33) Sato, K., Sakai, E., Veith, P.D., Shoji, M., Kikuchi, Y., Yukitake, H., Ohara, N., Naito, M., Okamoto, K., Reynolds, E.C., Nakayama, K. (2005): Identification of a new membrane-associated protein which influences transport/maturation of gingipains and adhesins of Porphyromonas gingivalis. J. Biol. Chem. 280, 8668–8677. 4) Fujimura, Y., Hotokezaka, H., Ohara, N., Naito, M., Sakai, E., Yoshimura, M., Narita, Y., Kitaura, H., Yoshida, N., Nakayama, K. (2006): Hemoglobin receptor protein (HbR) of Porphyromonas gingivalis inhibits receptor activator NF-κB ligand-induced osteoclastogenesis from bone marrow macrophages. Infect. Immun. 74, 2544–2551. 15) Lourbakos, A., Yuan, Y.P., Jenkins, A.L., Travis, J., Andrade-Gordon, P., Santulli, R., Potempa, J., Pike, R.N. (2001): Activation of protease-activated receptors by gingipains from Porphyromonas gingivalis leads to platelet aggregation: a new trait in microbial pathogenicity. Blood 97, 3790–3797. 17) Naito, M., Ogura, Y., Itoh, T., Shoji, M., Okamoto, M., Hayashi, T., Nakayama, K. (2016): The complete genome sequencing of Prevotella intermedia strain OMA14 and a subsequent fine-scale, intra-species genomic comparison reveal an unusual amplification of conjugative and mobile transposons and identify a novel Prevotella-lineage-specific repeat. DNA Res. 23, 11–19. 38) Shoji, M., Nakayama, K. (2016): Glycobiology of the oral pathogen Porphyromonas gingivalis and related species. Microb. Pathog. 94, 35–41. 43) Veith, P.D., Glew, M.D., Gorasia, D.G., Reynolds, E.C. (2017): Type IX Secretion: the generation of bacterial cell surface coatings involved in virulence, gliding motility and the degradation of complex biopolymers. Mol. Microbiol. doi: 10.1111/mmi.13752. [Epub ahead of print]. 21) Nakayama, K. (2010): Porphyromonas gingivalis cell-induced hemagglutination and platelet aggregation. Periodontology 2000 54, 45–52. 35) Shi, Y., Ratnayake, D.B., Okamoto, K., Abe, N., Yamamoto, K., Nakayama, K. (1999): Genetic analyses of proteolysis, hemoglobin binding, and hemagglutination of Porphyromonas gingivalis. Construction of mutants with a combination of rgpA, rgpB, kgp, and hagA. J. Biol. Chem. 274, 17955–17960. 9) Kelly, C. G., Booth, V., Kendal, H., Slaney, J.M., Curtis, M.A., Lehner, T. (1997): The relationship between colonization and haemagglutination inhibiting and B cell epitopes of Porphyromonas gingivalis. Clin. Exp. Immunol. 110, 285–291. 20) 中山浩次（2001）: 口腔偏性嫌気性細菌Porphyromonas gingivalisの病原性に関する分子遺伝学的研究. 日本細菌学雑誌 56, 573–585. 8) Kadowaki, T., Yukitake, H., Naito, M., Sato, K., Kikuchi, Y., Kondo, Y., Shoji, M., Nakayama, K. (2016): A two-component system regulates gene expression of the type IX secretion component proteins via an ECF sigma factor. Sci. Rep. 6, 23288. 6) Hospenthal, M.K., Costa, T.R.D., Waksman, G. (2017): A comprehensive guide to pilus biogenesis in Gram-negative bacteria. Nat. Rev. Microbiol. 15, 365–379. 12) Kita, D., Shibata, S., Kikuchi, Y., Kokubu, E., Nakayama, K., Saito, A., Ishihara, K. (2016): Involvement of the type IX secretion system in the gliding motility and biofilm formation of Capnocytophaga ochracea. Appl. Environ. Microbiol. 82, 1756–1766. 2) Booth, V., Lehner, T. (1997): Characterization of the Porphyromonas gingivalis antigen recognized by a monoclonal antibody which prevents colonization by the organism. J. Periodontal Res. 32, 54–60. 45) Wang, Y., Wang, Z., Cao, J., Guan, Z., Lu, X. (2014): FLP-FRT-based method to obtain unmarked deletions of CHU_3237 (porU) and large genomic fragments of Cytophaga hutchinsonii. Appl. Environ. Microbiol. 80, 6037–6045. 24) Narita, Y., Sato, K., Yukitake, H., Shoji, M., Nakane, D., Nagano, K., Yoshimura, F., Naito, M., Nakayama, K. (2014): Lack of a surface layer in Tannerella forsythia mutants deficient in the type IX secretion system. Microbiology 160, 2295–2303. 44) Vincent, M.S., Durand, E., Cascales, E. (2016): The PorX Response Regulator of the Porphyromonas gingivalis PorXY Two-Component System Does Not Directly Regulate the Type IX Secretion Genes but Binds the PorL Subunit. Front. Cell. Infect. Microbiol. 6, 96. 13) Kondo, Y., Ohara, N., Sato, K., Yoshimura, M., Yukitake, H., Naito, M., Fujiwara, T., Nakayama, K. (2010): Tetratricopeptide repeat protein-associated proteins contribute to the virulence of Porphyromonas gingivalis. Infect. Immun. 78, 2846–2856. 25) Nelson, K.E., Fleischmann, R.D., DeBoy, R.T., Paulsen, I.T., Fouts, D.E., Eisen, J.A., Daugherty, S.C., Dodson, R.J., Durkin, A.S., Gwinn, M., Haft, D.H., Kolonay, J.F., Nelson, W.C., Mason, T., Tallon, L., Gray, J., Granger, D., Tettelin, H., Dong, H., Galvin, J.L., Duncan, M.J., Dewhirst, F.E., Fraser, C.M. (2003): Complete genome sequence of the oral pathogenic Bacterium Porphyromonas gingivalis strain W83. J. Bacteriol. 185, 5591–5601. 7) Kadowaki, T., Nakayama, K., Yoshimura, F., Okamoto, K., Abe, N., Yamamoto, K. (1998): Arg-gingipain acts as a major processing enzyme for various cell surface proteins in Porphyromonas gingivalis. J. Biol. Chem. 273, 29072–29076. 28) Onoe, T., Hoover, C. I., Nakayama, K., Ikeda, T., Nakamura, H., Yoshimura, F. (1995): Identification of Porphyromonas gingivalis prefimbrilin possessing a long leader peptide: possible involvement of trypsin-like protease in fimbrilin maturation. Microb. Pathog. 19, 351–364. 31) Sakai, E., Naito, M., Sato, K., Hotokezaka, H., Kadowaki, T., Kamaguchi, A., Yamamoto, K., Okamoto, K., Nakayama, K. (2007): Construction of recombinant hemagglutinin derived from the gingipain-encoding gene of Porphyromonas gingivalis, identification of its target protein on erythrocytes, and inhibition of hemagglutination by an inter-domain regional peptide. J. Bacteriol. 189, 3977–3986. 27) Nonaka, M., Shoji, M., Kadowaki, T., Sato, K., Yukitake, H., Naito, M., Nakayama, K. (2014): Analysis of a Lys-specific serine endopeptidase secreted via the type IX secretion system in Porphyromonas gingivalis. FEMS Microbiol. Lett. 354, 60–68. 16) Naito, M., Hirakawa, H., Yamashita, A., Ohara, N., Shoji, M., Yukitake, H., Nakayama, K., Toh, H., Yoshimura, F., Kuhara, S., Hattori, M., Hayashi, T., Nakayama, K. (2008): Determination of the genome sequence of Porphyromonas gingivalis strain ATCC 33277 and genomic comparison with strain W83 revealed extensive genome rearrangements in P. gingivalis. DNA Res. 15, 215–225. 34) Seers, C.A., Slakeski, N., Veith, P.D., Nikolof, T., Chen, Y.Y., Dashper, S.G., Reynolds, E.C. (2006): The RgpB C-terminal domain has a role in attachment of RgpB to the outer membrane and belongs to a novel C-terminal-domain family found in Porphyromonas gingivalis. J. Bacteriol. 188, 6376–6386. 26) Nelson, S.S., Bollampalli, S., McBride, M.J. (2008): SprB is a cell surface component of the Flavobacterium johnsoniae gliding motility machinery. J. Bacteriol. 190, 2851–2857. 14) Lasica, A.M., Ksiazek, M., Madej, M., Potempa, J. (2017): The Type IX Secretion System (T9SS): Highlights and Recent Insights into Its Structure and Function. Front. Cell. Infect. Microbiol. 7, 215. 18) Naito, M., Sakai, E., Shi, Y., Ideguchi, H., Shoji, M., Ohara, N., Yamamoto, K., Nakayama, K. (2006): Porphyromonas gingivalis-induced platelet aggregation in plasma depends on Hgp44 adhesin but not Rgp proteinase. Mol. Microbiol. 59, 152–167. 29) Paramonov, N., Rangarajan, M., Hashim, A., Gallagher, A., Aduse-Opoku, J., Slaney, J.M., Hounsell, E., Curtis, M.A. (2005): Structural analysis of a novel anionic polysaccharide from Porphyromonas gingivalis strain W50 related to Arg-gingipain glycans. Mol. Microbiol. 58, 847–863. 30) Rangarajan, M., Aduse-Opoku, J., Paramonov, N., Hashim, A., Bostanci, N., Fraser, O.P., Tarelli, E., Curtis, M.A. (2008): Identification of a second lipopolysaccharide in Porphyromonas gingivalis W50. J. Bacteriol. 190, 2920–2932. 19) Nakane, D., Sato, K., Wada, H., McBride, M.J., Nakayama, K. (2013): Helical flow of surface protein required for bacterial gliding motility. Proc. Nat. Acad. Sci. U S A 110, 11145–11150. 10) Kharade, S.S., McBride, M.J. (2014): Flavobacterium johnsoniae chitinase ChiA is required for chitin utilization and is secreted by the type IX secretion system. J. Bacteriol. 196, 961–970. 32) Sato, K., Naito, M., Yukitake, H., Hirakawa, H., Shoji, M., McBride, M.J., Rhodes, R.G., Nakayama, K. (2010): A protein secretion system linked to bacteroidete gliding motility and pathogenesis. Proc. Natl. Acad. Sci. U S A 107, 276–281. 47) Yamaguchi, M., Sato, K., Yukitake, H., Noiri, Y., Ebisu, S., Nakayama, K. (2010): Porphyromonas gingivalis mutant defective in a putative glycosyltransferase exhibits defect in biosynthesis of polysaccharide portions of lipopolysaccharide, decreased gingipain activities, strong autoaggregation and increased biofilm formation. Infect. Immun. 78, 3801–3812. 46) Xu, Q., Shoji, M., Shibata, S., Naito, M., Sato, K., Elsliger, M.A., Grant, J.C., Axelrod, H.L., Chiu, H.J., Farr, C.L., Jaroszewski, L., Knuth, M.W., Deacon, A.M., Godzik, A., Lesley, S.A., Curtis, M.A., Nakayama, K., Wilson, I.A. (2016): A distinct type of pilus from the human microbiom |
| References_xml | – reference: 6) Hospenthal, M.K., Costa, T.R.D., Waksman, G. (2017): A comprehensive guide to pilus biogenesis in Gram-negative bacteria. Nat. Rev. Microbiol. 15, 365–379. – reference: 12) Kita, D., Shibata, S., Kikuchi, Y., Kokubu, E., Nakayama, K., Saito, A., Ishihara, K. (2016): Involvement of the type IX secretion system in the gliding motility and biofilm formation of Capnocytophaga ochracea. Appl. Environ. Microbiol. 82, 1756–1766. – reference: 27) Nonaka, M., Shoji, M., Kadowaki, T., Sato, K., Yukitake, H., Naito, M., Nakayama, K. (2014): Analysis of a Lys-specific serine endopeptidase secreted via the type IX secretion system in Porphyromonas gingivalis. FEMS Microbiol. Lett. 354, 60–68. – reference: 43) Veith, P.D., Glew, M.D., Gorasia, D.G., Reynolds, E.C. (2017): Type IX Secretion: the generation of bacterial cell surface coatings involved in virulence, gliding motility and the degradation of complex biopolymers. Mol. Microbiol. doi: 10.1111/mmi.13752. [Epub ahead of print]. – reference: 5) Holt, S.C., Ebersole, J., Felton, J., Brunsvold, M., Kornman, K.S. (1988): Implantation of Bacteroides gingivalis in nonhuman primates initiates progression of periodontitis. Science 239, 55–57. – reference: 36) Shibata, Y., Hayakawa, M., Takiguchi, H., Shiroza, T., Abiko, Y. (1999): Determination and characterization of the hemagglutinin-associated short motifs found in Porphyromonas gingivalis multiple gene products. J. Biol. Chem. 274, 5012–5020. – reference: 3) Costa, T.R., Felisberto-Rodrigues, C., Meir, A., Prevost, M.S., Redzej, A., Trokter, M., Waksman, G. (2015): Secretion systems in Gram-negative bacteria: structural and mechanistic insights. Nat. Rev. Microbiol. 13, 343–359. – reference: 2) Booth, V., Lehner, T. (1997): Characterization of the Porphyromonas gingivalis antigen recognized by a monoclonal antibody which prevents colonization by the organism. J. Periodontal Res. 32, 54–60. – reference: 38) Shoji, M., Nakayama, K. (2016): Glycobiology of the oral pathogen Porphyromonas gingivalis and related species. Microb. Pathog. 94, 35–41. – reference: 31) Sakai, E., Naito, M., Sato, K., Hotokezaka, H., Kadowaki, T., Kamaguchi, A., Yamamoto, K., Okamoto, K., Nakayama, K. (2007): Construction of recombinant hemagglutinin derived from the gingipain-encoding gene of Porphyromonas gingivalis, identification of its target protein on erythrocytes, and inhibition of hemagglutination by an inter-domain regional peptide. J. Bacteriol. 189, 3977–3986. – reference: 14) Lasica, A.M., Ksiazek, M., Madej, M., Potempa, J. (2017): The Type IX Secretion System (T9SS): Highlights and Recent Insights into Its Structure and Function. Front. Cell. Infect. Microbiol. 7, 215. – reference: 41) Shoji, M., Sato, K., Yukitake, H., Naito, M., Nakayama, K. (2014): Involvement of the Wbp pathway in the biosynthesis of Porphyromonas gingivalis lipopolysaccharide with anionic polysaccharide. Sci. Rep. 4, 5056. – reference: 39) Shoji, M., Ratnayake, D.B., Shi, Y., Kadowaki, T., Yamamoto, K., Yoshimura, F., Akamine, A., Curtis, M.A., Nakayama, K. (2002): Construction and characterization of a nonpigmented mutant of Porphyromonas gingivalis: cell surface polysaccharide as an anchorage for gingipains. Microbiology 148, 1183–1191. – reference: 4) Fujimura, Y., Hotokezaka, H., Ohara, N., Naito, M., Sakai, E., Yoshimura, M., Narita, Y., Kitaura, H., Yoshida, N., Nakayama, K. (2006): Hemoglobin receptor protein (HbR) of Porphyromonas gingivalis inhibits receptor activator NF-κB ligand-induced osteoclastogenesis from bone marrow macrophages. Infect. Immun. 74, 2544–2551. – reference: 28) Onoe, T., Hoover, C. I., Nakayama, K., Ikeda, T., Nakamura, H., Yoshimura, F. (1995): Identification of Porphyromonas gingivalis prefimbrilin possessing a long leader peptide: possible involvement of trypsin-like protease in fimbrilin maturation. Microb. Pathog. 19, 351–364. – reference: 33) Sato, K., Sakai, E., Veith, P.D., Shoji, M., Kikuchi, Y., Yukitake, H., Ohara, N., Naito, M., Okamoto, K., Reynolds, E.C., Nakayama, K. (2005): Identification of a new membrane-associated protein which influences transport/maturation of gingipains and adhesins of Porphyromonas gingivalis. J. Biol. Chem. 280, 8668–8677. – reference: 25) Nelson, K.E., Fleischmann, R.D., DeBoy, R.T., Paulsen, I.T., Fouts, D.E., Eisen, J.A., Daugherty, S.C., Dodson, R.J., Durkin, A.S., Gwinn, M., Haft, D.H., Kolonay, J.F., Nelson, W.C., Mason, T., Tallon, L., Gray, J., Granger, D., Tettelin, H., Dong, H., Galvin, J.L., Duncan, M.J., Dewhirst, F.E., Fraser, C.M. (2003): Complete genome sequence of the oral pathogenic Bacterium Porphyromonas gingivalis strain W83. J. Bacteriol. 185, 5591–5601. – reference: 15) Lourbakos, A., Yuan, Y.P., Jenkins, A.L., Travis, J., Andrade-Gordon, P., Santulli, R., Potempa, J., Pike, R.N. (2001): Activation of protease-activated receptors by gingipains from Porphyromonas gingivalis leads to platelet aggregation: a new trait in microbial pathogenicity. Blood 97, 3790–3797. – reference: 46) Xu, Q., Shoji, M., Shibata, S., Naito, M., Sato, K., Elsliger, M.A., Grant, J.C., Axelrod, H.L., Chiu, H.J., Farr, C.L., Jaroszewski, L., Knuth, M.W., Deacon, A.M., Godzik, A., Lesley, S.A., Curtis, M.A., Nakayama, K., Wilson, I.A. (2016): A distinct type of pilus from the human microbiome. Cell 165, 690–703. – reference: 7) Kadowaki, T., Nakayama, K., Yoshimura, F., Okamoto, K., Abe, N., Yamamoto, K. (1998): Arg-gingipain acts as a major processing enzyme for various cell surface proteins in Porphyromonas gingivalis. J. Biol. Chem. 273, 29072–29076. – reference: 22) Nakayama, K. (2015): Porphyromonas gingivalis and related bacteria: from colonial pigmentation to the type IX secretion system and gliding motility. J. Periodontal Res. 50, 1–8. – reference: 16) Naito, M., Hirakawa, H., Yamashita, A., Ohara, N., Shoji, M., Yukitake, H., Nakayama, K., Toh, H., Yoshimura, F., Kuhara, S., Hattori, M., Hayashi, T., Nakayama, K. (2008): Determination of the genome sequence of Porphyromonas gingivalis strain ATCC 33277 and genomic comparison with strain W83 revealed extensive genome rearrangements in P. gingivalis. DNA Res. 15, 215–225. – reference: 23) Nakayama, K., Yoshimura, F., Kadowaki, T., Yamamoto, K. (1996): Involvement of arginine-specific cysteine proteinase (Arg-gingipain) in fimbriation of Porphyromonas gingivalis. J. Bacteriol. 178, 2818–2824. – reference: 40) Shoji, M., Sato, K., Yukitake, H., Kondo, Y., Narita, Y., Kadowaki, T., Naito, M., Nakayama, K. (2011): Por secretion system-dependent secretion and glycosylation of Porphyromonas gingivalis hemin-binding protein 35. PLoS One 6, e21372. – reference: 37) Shoji, M., Naito, M., Yukitake, H., Sato, K., Sakai, E., Ohara, N., Nakayama, K. (2004): The major structural components of two cell-surface filaments of Porphyromonas gingivalis are matured through lipoprotein precursors. Mol. Microbiol. 52, 1513–1525. – reference: 24) Narita, Y., Sato, K., Yukitake, H., Shoji, M., Nakane, D., Nagano, K., Yoshimura, F., Naito, M., Nakayama, K. (2014): Lack of a surface layer in Tannerella forsythia mutants deficient in the type IX secretion system. Microbiology 160, 2295–2303. – reference: 30) Rangarajan, M., Aduse-Opoku, J., Paramonov, N., Hashim, A., Bostanci, N., Fraser, O.P., Tarelli, E., Curtis, M.A. (2008): Identification of a second lipopolysaccharide in Porphyromonas gingivalis W50. J. Bacteriol. 190, 2920–2932. – reference: 45) Wang, Y., Wang, Z., Cao, J., Guan, Z., Lu, X. (2014): FLP-FRT-based method to obtain unmarked deletions of CHU_3237 (porU) and large genomic fragments of Cytophaga hutchinsonii. Appl. Environ. Microbiol. 80, 6037–6045. – reference: 8) Kadowaki, T., Yukitake, H., Naito, M., Sato, K., Kikuchi, Y., Kondo, Y., Shoji, M., Nakayama, K. (2016): A two-component system regulates gene expression of the type IX secretion component proteins via an ECF sigma factor. Sci. Rep. 6, 23288. – reference: 10) Kharade, S.S., McBride, M.J. (2014): Flavobacterium johnsoniae chitinase ChiA is required for chitin utilization and is secreted by the type IX secretion system. J. Bacteriol. 196, 961–970. – reference: 35) Shi, Y., Ratnayake, D.B., Okamoto, K., Abe, N., Yamamoto, K., Nakayama, K. (1999): Genetic analyses of proteolysis, hemoglobin binding, and hemagglutination of Porphyromonas gingivalis. Construction of mutants with a combination of rgpA, rgpB, kgp, and hagA. J. Biol. Chem. 274, 17955–17960. – reference: 49) Zhu, Y., McBride, M.J. (2014): Deletion of the Cytophaga hutchinsonii type IX secretion system gene sprP results in defects in gliding motility and cellulose utilization. Appl. Microbiol. Biotechnol. 98, 763–775. – reference: 29) Paramonov, N., Rangarajan, M., Hashim, A., Gallagher, A., Aduse-Opoku, J., Slaney, J.M., Hounsell, E., Curtis, M.A. (2005): Structural analysis of a novel anionic polysaccharide from Porphyromonas gingivalis strain W50 related to Arg-gingipain glycans. Mol. Microbiol. 58, 847–863. – reference: 11) Kharade, S.S., McBride, M.J. (2015): Flavobacterium johnsoniae PorV is required for secretion of a subset of proteins targeted to the type IX secretion system. J. Bacteriol. 197, 147–158. – reference: 21) Nakayama, K. (2010): Porphyromonas gingivalis cell-induced hemagglutination and platelet aggregation. Periodontology 2000 54, 45–52. – reference: 44) Vincent, M.S., Durand, E., Cascales, E. (2016): The PorX Response Regulator of the Porphyromonas gingivalis PorXY Two-Component System Does Not Directly Regulate the Type IX Secretion Genes but Binds the PorL Subunit. Front. Cell. Infect. Microbiol. 6, 96. – reference: 47) Yamaguchi, M., Sato, K., Yukitake, H., Noiri, Y., Ebisu, S., Nakayama, K. (2010): Porphyromonas gingivalis mutant defective in a putative glycosyltransferase exhibits defect in biosynthesis of polysaccharide portions of lipopolysaccharide, decreased gingipain activities, strong autoaggregation and increased biofilm formation. Infect. Immun. 78, 3801–3812. – reference: 20) 中山浩次（2001）: 口腔偏性嫌気性細菌Porphyromonas gingivalisの病原性に関する分子遺伝学的研究. 日本細菌学雑誌 56, 573–585. – reference: 26) Nelson, S.S., Bollampalli, S., McBride, M.J. (2008): SprB is a cell surface component of the Flavobacterium johnsoniae gliding motility machinery. J. Bacteriol. 190, 2851–2857. – reference: 32) Sato, K., Naito, M., Yukitake, H., Hirakawa, H., Shoji, M., McBride, M.J., Rhodes, R.G., Nakayama, K. (2010): A protein secretion system linked to bacteroidete gliding motility and pathogenesis. Proc. Natl. Acad. Sci. U S A 107, 276–281. – reference: 19) Nakane, D., Sato, K., Wada, H., McBride, M.J., Nakayama, K. (2013): Helical flow of surface protein required for bacterial gliding motility. Proc. Nat. Acad. Sci. U S A 110, 11145–11150. – reference: 9) Kelly, C. G., Booth, V., Kendal, H., Slaney, J.M., Curtis, M.A., Lehner, T. (1997): The relationship between colonization and haemagglutination inhibiting and B cell epitopes of Porphyromonas gingivalis. Clin. Exp. Immunol. 110, 285–291. – reference: 34) Seers, C.A., Slakeski, N., Veith, P.D., Nikolof, T., Chen, Y.Y., Dashper, S.G., Reynolds, E.C. (2006): The RgpB C-terminal domain has a role in attachment of RgpB to the outer membrane and belongs to a novel C-terminal-domain family found in Porphyromonas gingivalis. J. Bacteriol. 188, 6376–6386. – reference: 17) Naito, M., Ogura, Y., Itoh, T., Shoji, M., Okamoto, M., Hayashi, T., Nakayama, K. (2016): The complete genome sequencing of Prevotella intermedia strain OMA14 and a subsequent fine-scale, intra-species genomic comparison reveal an unusual amplification of conjugative and mobile transposons and identify a novel Prevotella-lineage-specific repeat. DNA Res. 23, 11–19. – reference: 18) Naito, M., Sakai, E., Shi, Y., Ideguchi, H., Shoji, M., Ohara, N., Yamamoto, K., Nakayama, K. (2006): Porphyromonas gingivalis-induced platelet aggregation in plasma depends on Hgp44 adhesin but not Rgp proteinase. Mol. Microbiol. 59, 152–167. – reference: 42) Shoji, M., Shibata, Y., Shiroza, T., Yukitake, H., Peng, B., Chen, Y.-Y., Sato, K., Naito, M., Abiko, Y., Reynolds, E.C., Nakayama, K. (2010): Characterization of hemin-binding protein 35 (HBP35) in Porphyromonas gingivalis: its cellular distribution, thioredoxin activity and role in heme utilization. BMC Microbiol. 10, 152. – reference: 1) Allen, W.J., Phan, G., Waksman, G. (2012): Pilus biogenesis at the outer membrane of Gram-negative bacterial pathogens. Curr. Opin. Struct. Biol. 22, 500–506. – reference: 13) Kondo, Y., Ohara, N., Sato, K., Yoshimura, M., Yukitake, H., Naito, M., Fujiwara, T., Nakayama, K. (2010): Tetratricopeptide repeat protein-associated proteins contribute to the virulence of Porphyromonas gingivalis. Infect. Immun. 78, 2846–2856. – reference: 48) Yoshimura, M., Ohara, N., Kondo, Y., Shoji, M., Okano, S., Nakano, Y., Abiko, Y., Nakayama, K. (2008): Proteome analysis of Porphyromonas gingivalis cells placed in a subcutaneous chamber of mice. Oral Microbiol. Immunol. 23, 413–418. |
| SSID | ssib000940317 ssib058493887 ssib005879753 ssj0060310 ssib002484619 |
| Score | 2.0742064 |
| Snippet | Bacteroidetes門にはBacteroides属, Prevotella属, Porphyromonas属等, ヒトに共生・寄生する多くの細菌が含まれる。私たちはPorphyromonas属に含まれる歯周病原細菌であるPorphyromonas... Many bacteria symbiotic and parasitic in humans are included in the genera Bacteroides, Prevotella, Porphyromonas and others, which belong to the phylum... |
| SourceID | proquest jstage |
| SourceType | Aggregation Database Publisher |
| StartPage | 219 |
| SubjectTerms | Arginine Bacteria Bacteroidetes Biodegradation Cell surface Colonization Gingipain Gliding Pathogens Periodontics Pili Protein transport Secretion |
| Title | バクテロイデーテス門細菌のIX型分泌機構およびV型線毛の研究 |
| URI | https://www.jstage.jst.go.jp/article/jsb/72/4/72_219/_article/-char/ja https://www.proquest.com/docview/2015033900 |
| Volume | 72 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| ispartofPNX | 日本細菌学雑誌, 2017, Vol.72(4), pp.219-227 |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Pa9RAFB9qRfAi_sVqlR6cU9k1mcxmZo5JzdJ_VoRtWU9hksy2u0Irtj3Yk92FWmxBD-JBQT0I0oNWqCiCn8KvELqr38I3SXY3bUXUy_Dy5mUmmTd5-b2ZeTMIXROGDAwuw4JikV2gzJAFEYGzwgJLqZCzGlU6OPnmjD0-SyerperAwPfcqqXVlaAYrv02ruR_tAo80KuOkv0HzfYKBQbQoF9IQcOQ_pWOsWdhbmFhJATBTjnjcDsjnBvdLNrNYhnhjh0UJtgV2BNY2Hr1g8ewS7ELBMe8jHkqbGLHm6hir4SFh7mrCc6TAmzsWomUjR0oo5wQLJFJ7uNOVgnIpxzXmssVBNUxLJzktjIWbq86neUYWNCEENi183h6pr4A3XdZ1vWIv7y7OroGzsBCvTfE7Uw5d_QkgjZnS416fozDZIfGOCYBN_SNnZ5Q6M87jDpJjGrexhPwikU226NSs679CGpmC2gzu89Irn_To0b88M8F_vd6s9rGclBkpNi19Ad28J655Zdnp6f9iletHEPHCWPJ0oGp2znIKyjY0byLDAgwt6VeibN8rDPgQ2ElEDpFF_pQ8DSsKnvLdMtd_WzX-08GcKoBzsX8UYSRwKbKaXQq83dGnLTznkEDDXkWnUhPQH1wDlXi1tO4uRu3NuLW-7j5Nm49ilvf9GXz68_nDzufPv54sh2vf5io7r_a2t_caO9tt3det99txeuP4-ZmvL43BxmdLy_auy9BrPPmWWfn83k0W_YqY-OF7KCPQgPQs1GoSZNFJiFRGEbQGoaUtrKEjGRJw28a1FRUiyiTzDKpogqkpQIbExiRoWqE29YFNLi4tKguohEVcBLaoZDECKgwpSA1agZmEJUUC8KIDiE7bRn_Xrqbi599vT60ns-IT3UCTdjj6-hHvyGH0HC3Jf3MBCz7RI8XWpYwjEt_zr6MTvb79TAaXLm_qq4Aml0Jribd4xfrX5W9 |
| linkProvider | Colorado Alliance of Research Libraries |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=%E3%83%90%E3%82%AF%E3%83%86%E3%83%AD%E3%82%A4%E3%83%87%E3%83%BC%E3%83%86%E3%82%B9%E9%96%80%E7%B4%B0%E8%8F%8C%E3%81%AEIX%E5%9E%8B%E5%88%86%E6%B3%8C%E6%A9%9F%E6%A7%8B%E3%81%8A%E3%82%88%E3%81%B3V%E5%9E%8B%E7%B7%9A%E6%AF%9B%E3%81%AE%E7%A0%94%E7%A9%B6&rft.jtitle=Nihon+saikingaku+zasshi&rft.au=NAKAYAMA%2C+Koji&rft.date=2017-01-01&rft.pub=Japan+Science+and+Technology+Agency&rft.issn=0021-4930&rft.eissn=1882-4110&rft.volume=72&rft.issue=4&rft.spage=219&rft_id=info:doi/10.3412%2Fjsb.72.219&rft.externalDBID=NO_FULL_TEXT |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0021-4930&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0021-4930&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0021-4930&client=summon |