NDLI: Dentilisin Activity Affects the Organization of the Outer Sheath of Treponema denticola

Content Provider	PubMed Central
Author	Ishihara, Kazuyuki Kuramitsu, Howard K. Miura, Tadashi Okuda, Katsuji
Copyright Year	1998
Abstract	Prolyl-phenylalanine-specific serine protease (dentilisin) is a major extracellular protease produced by Treponema denticola. The gene, prtP, coding for the protease was recently cloned and sequenced (K. Ishihara, T. Miura, H. K. Kuramitsu, and K. Okuda, Infect. Immun. 64:5178–5186, 1996). In order to determine the role of this protease in the physiology and virulence of T. denticola, a dentilisin-deficient mutant, K1, was constructed following electroporation with a prtP-inactivated DNA fragment. No chymotrypsin-like protease activity was detected in the dentilisin-deficient mutant. In addition, the high-molecular-mass oligomeric protein characteristic of the outer sheath of the organism decreased in the mutant. Furthermore, the hydrophobicity of the mutant was decreased, and coaggregation of the mutant with Fusobacterium nucleatum was enhanced compared to that of the wild-type organism. The results obtained with a mouse abscess model system indicated that the virulence of the mutant was attenuated relative to that of the wild-type organism. These results suggest that dentilisin activity plays a major role in the structural organization of the outer sheath of T. denticola. The loss of dentilsin activity and the structural change in the outer sheath affect the pathogenicity of T. denticola.
Starting Page	3837
File Format	PDF
ISSN	10985530
e-ISSN	10985530
Journal	Journal of Bacteriology
Issue Number	15
Volume Number	180
Language	English
Publisher	American Society for Microbiology
Publisher Date	1998-08-01
Access Restriction	Open
Rights Holder	American Society for Microbiology
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Microbiology

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The Antibacterial Activity of LL-37 against Treponema denticola Is Dentilisin Protease Independent and Facilitated by the Major Outer Sheath Protein Virulence Factor

Intracellular localization of Treponema denticola chymotrypsin-like proteinase in chronic periodontitis

Treponema denticola PrcB Is Required for Expression and Activity of the PrcA-PrtP (Dentilisin) Complex▿

Sequence analysis, expression, and binding activity of recombinant major outer sheath protein (Msp) of Treponema denticola.

Chemical and biological activities of a 64-kilodalton outer sheath protein from Treponema denticola strains.

The Major Outer Sheath Protein (Msp) of Treponema denticola Has a Bipartite Domain Architecture and Exists as Periplasmic and Outer Membrane-Spanning Conformers

Proteases of Treponema denticola outer sheath and extracellular vesicles.

Correction for Anand et al., The Major Outer Sheath Protein (Msp) of Treponema denticola Has a Bipartite Domain Architecture and Exists as Periplasmic and Outer Membrane-Spanning Conformers

Approaches to Understanding Mechanisms of Dentilisin Protease Complex Expression in Treponema denticola

Dentilisin Activity Affects the Organization of the Outer Sheath of Treponema denticola

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