학술논문
A pleiotropic role of sialidase in the pathogenicity of Porphyromonas gingivalis .
Document Type
Academic Journal
Author
Pham C; Department of Oral Craniofacial Molecular Biology, Virginia Commonwealth University, Richmond, Virginia, USA.; Guo S; Department of Microbial Pathogenesis, Yale School of Medicine, New Haven, Connecticut, USA.; Microbial Sciences Institute, Yale University, West Haven, Connecticut, USA.; Han X; Department of Oral Craniofacial Molecular Biology, Virginia Commonwealth University, Richmond, Virginia, USA.; Coleman L; Department of Oral Craniofacial Molecular Biology, Virginia Commonwealth University, Richmond, Virginia, USA.; Sze CW; Department of Oral Craniofacial Molecular Biology, Virginia Commonwealth University, Richmond, Virginia, USA.; Wang H; Department of Oral Craniofacial Molecular Biology, Virginia Commonwealth University, Richmond, Virginia, USA.; Liu J; Department of Microbial Pathogenesis, Yale School of Medicine, New Haven, Connecticut, USA.; Microbial Sciences Institute, Yale University, West Haven, Connecticut, USA.; Li C; Department of Oral Craniofacial Molecular Biology, Virginia Commonwealth University, Richmond, Virginia, USA.; Department of Microbiology and Immunology, Virginia Commonwealth University, Richmond, Virginia, USA.
Source
Publisher: American Society For Microbiology Country of Publication: United States NLM ID: 0246127 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1098-5522 (Electronic) Linking ISSN: 00199567 NLM ISO Abbreviation: Infect Immun Subsets: MEDLINE
Subject
Language
English
Abstract
As one of the keystone pathogens of periodontitis, the oral bacterium Porphyromonas gingivalis produces an array of virulence factors, including a recently identified sialidase (PG0352). Our previous report involving loss-of-function studies indicated that PG0352 plays an important role in the pathophysiology of P. gingivalis . However, this report had not been corroborated by gain-of-function studies or substantiated in different P. gingivalis strains. To fill these gaps, herein we first confirm the role of PG0352 in cell surface structures (e.g., capsule) and serum resistance using P. gingivalis W83 strain through genetic complementation and then recapitulate these studies using P. gingivalis ATCC33277 strain. We further investigate the role of PG0352 and its counterpart (PGN1608) in ATCC33277 in cell growth, biofilm formation, neutrophil killing, cell invasion, and P. gingivalis -induced inflammation. Our results indicate that PG0352 and PGN1608 are implicated in P. gingivalis cell surface structures, hydrophobicity, biofilm formation, resistance to complement and neutrophil killing, and host immune responses. Possible molecular mechanisms involved are also discussed. In summary, this report underscores the importance of sialidases in the pathophysiology of P. gingivalis and opens an avenue to elucidate their underlying molecular mechanisms.
Competing Interests: The authors declare no conflict of interest.
Competing Interests: The authors declare no conflict of interest.