Maturation of the Mfa1 Fimbriae in the Oral Pathogen Porphyromonas gingivalis
The Mfa1 fimbriae of the periodontal pathogen Porphyromonas gingivalis are involved in adhesion, including binding to synergistic species in oral biofilms. Mfa1 fimbriae are comprised of 5 proteins: the structural component Mfa1, the anchor Mfa2, and Mfa3-5 which constitute the fimbrial tip complex....
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| Materiálatiipa: | Artihkal |
| Giella: | English |
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Frontiers Media S.A.
2018-05-01
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| Ráidu: | Frontiers in Cellular and Infection Microbiology |
| Fáttát: | |
| Liŋkkat: | http://journal.frontiersin.org/article/10.3389/fcimb.2018.00137/full |
| _version_ | 1830360373465710592 |
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| author | Jae Y. Lee Daniel P. Miller Leng Wu Carolyn R. Casella Yoshiaki Hasegawa Richard J. Lamont |
| author_facet | Jae Y. Lee Daniel P. Miller Leng Wu Carolyn R. Casella Yoshiaki Hasegawa Richard J. Lamont |
| author_sort | Jae Y. Lee |
| collection | DOAJ |
| description | The Mfa1 fimbriae of the periodontal pathogen Porphyromonas gingivalis are involved in adhesion, including binding to synergistic species in oral biofilms. Mfa1 fimbriae are comprised of 5 proteins: the structural component Mfa1, the anchor Mfa2, and Mfa3-5 which constitute the fimbrial tip complex. Interactions among the Mfa proteins and the polymerization mechanism for Mfa1 are poorly understood. Here we show that Mfa3 can bind to Mfa1, 2, 4, and 5 in vitro, and may function as an adaptor protein interlinking other fimbrial subunits. Polymerization of Mfa1 is independent of Mfa3-5 and requires proteolytic processing mediated by the RgpA/B arginine gingipains of P. gingivalis. Both the N- and C- terminal regions of Mfa1 are necessary for polymerization; however, potential β-strand disrupting amino acid substitutions in these regions do not impair Mfa1 polymerization. In contrast, substitution of hydrophobic amino acids with charged residues in either the N- or C- terminal domains yielded Mfa1 proteins that failed to polymerize. Collectively, these results indicate that Mfa3 serves as an adaptor protein between Mfa1 and other accessory fimbrial proteins. Mfa1 fimbrial polymerization is dependent on hydrophobicity in both the N- and C-terminal regions, indicative of an assembly mechanism involving the terminal regions forming a hydrophobic binding interface between Mfa1 subunits. |
| first_indexed | 2024-12-20T03:16:57Z |
| format | Article |
| id | doaj.art-d6a48b5799b04fb7a1b6b8b3e3ce4fe5 |
| institution | Directory Open Access Journal |
| issn | 2235-2988 |
| language | English |
| last_indexed | 2024-12-20T03:16:57Z |
| publishDate | 2018-05-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Cellular and Infection Microbiology |
| spelling | doaj.art-d6a48b5799b04fb7a1b6b8b3e3ce4fe52022-12-21T19:55:20ZengFrontiers Media S.A.Frontiers in Cellular and Infection Microbiology2235-29882018-05-01810.3389/fcimb.2018.00137354764Maturation of the Mfa1 Fimbriae in the Oral Pathogen Porphyromonas gingivalisJae Y. Lee0Daniel P. Miller1Leng Wu2Carolyn R. Casella3Yoshiaki Hasegawa4Richard J. Lamont5Department of Oral Immunology and Infectious Diseases, University of Louisville, Louisville, KY, United StatesDepartment of Oral Immunology and Infectious Diseases, University of Louisville, Louisville, KY, United StatesDepartment of Oral Immunology and Infectious Diseases, University of Louisville, Louisville, KY, United StatesDepartment of Microbiology and Immunology, University of Louisville, Louisville, KY, United StatesDepartment of Microbiology, School of Dentistry, Aichi Gakuin University, Nagoya, JapanDepartment of Oral Immunology and Infectious Diseases, University of Louisville, Louisville, KY, United StatesThe Mfa1 fimbriae of the periodontal pathogen Porphyromonas gingivalis are involved in adhesion, including binding to synergistic species in oral biofilms. Mfa1 fimbriae are comprised of 5 proteins: the structural component Mfa1, the anchor Mfa2, and Mfa3-5 which constitute the fimbrial tip complex. Interactions among the Mfa proteins and the polymerization mechanism for Mfa1 are poorly understood. Here we show that Mfa3 can bind to Mfa1, 2, 4, and 5 in vitro, and may function as an adaptor protein interlinking other fimbrial subunits. Polymerization of Mfa1 is independent of Mfa3-5 and requires proteolytic processing mediated by the RgpA/B arginine gingipains of P. gingivalis. Both the N- and C- terminal regions of Mfa1 are necessary for polymerization; however, potential β-strand disrupting amino acid substitutions in these regions do not impair Mfa1 polymerization. In contrast, substitution of hydrophobic amino acids with charged residues in either the N- or C- terminal domains yielded Mfa1 proteins that failed to polymerize. Collectively, these results indicate that Mfa3 serves as an adaptor protein between Mfa1 and other accessory fimbrial proteins. Mfa1 fimbrial polymerization is dependent on hydrophobicity in both the N- and C-terminal regions, indicative of an assembly mechanism involving the terminal regions forming a hydrophobic binding interface between Mfa1 subunits.http://journal.frontiersin.org/article/10.3389/fcimb.2018.00137/fulldonor strand exchangepolymerizationhydrophobicityaccessory fimbrial proteinsperiodontal disease |
| spellingShingle | Jae Y. Lee Daniel P. Miller Leng Wu Carolyn R. Casella Yoshiaki Hasegawa Richard J. Lamont Maturation of the Mfa1 Fimbriae in the Oral Pathogen Porphyromonas gingivalis Frontiers in Cellular and Infection Microbiology donor strand exchange polymerization hydrophobicity accessory fimbrial proteins periodontal disease |
| title | Maturation of the Mfa1 Fimbriae in the Oral Pathogen Porphyromonas gingivalis |
| title_full | Maturation of the Mfa1 Fimbriae in the Oral Pathogen Porphyromonas gingivalis |
| title_fullStr | Maturation of the Mfa1 Fimbriae in the Oral Pathogen Porphyromonas gingivalis |
| title_full_unstemmed | Maturation of the Mfa1 Fimbriae in the Oral Pathogen Porphyromonas gingivalis |
| title_short | Maturation of the Mfa1 Fimbriae in the Oral Pathogen Porphyromonas gingivalis |
| title_sort | maturation of the mfa1 fimbriae in the oral pathogen porphyromonas gingivalis |
| topic | donor strand exchange polymerization hydrophobicity accessory fimbrial proteins periodontal disease |
| url | http://journal.frontiersin.org/article/10.3389/fcimb.2018.00137/full |
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