ArticleInfection and immunity2004
Multiple functions of the leucine-rich repeat protein LrrA of Treponema denticola.
Article in Infection and immunity, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 88 citations in OpenAlex.
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- New insights into the putative role of leucine-rich repeat proteins ofFrontiers in cellular and infection microbiology · 2024Review
- Unusual structural and functional features of TpLRR/BspA-like LRR proteins.Journal of structural biology · 2023Review
- Periodontal Pathogens and Their Links to Neuroinflammation and Neurodegeneration.Microorganisms · 2023Review
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- Investigation of the potential regulator proteins associated with the expression of major surface protein and dentilisin inJournal of oral microbiology · 2020Article
- The Type IX Secretion System Is Required for Virulence of the Fish Pathogen Flavobacterium psychrophilum.Applied and environmental microbiology · 2020Article
- Analysis of oral microbiome from fossil human remains revealed the significant differences in virulence factors of modern and ancient Tannerella forsythia.BMC genomics · 2020Article
- Red complex: Polymicrobial conglomerate in oral flora: A review.Journal of family medicine and primary care · 2019Review
- An extracellular Leptospira interrogans leucine-rich repeat protein binds human E- and VE-cadherins.Cellular microbiology · 2019Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The gene lrrA, encoding a leucine-rich repeat protein, LrrA, that contains eight consensus tandem repeats of 23 amino acid residues, has been identified in Treponema denticola ATCC 35405. A leucine-rich repeat is a generally useful protein-binding motif, and proteins containing this repeat are typically involved in protein-protein interactions. Southern blot analysis demonstrated that T. denticola ATCC 35405 expresses the lrrA gene, but the gene was not identified in T. denticola ATCC 33520. In order to analyze the functions of LrrA in T. denticola, an lrrA-inactivated mutant of strain ATCC 35405 and an lrrA gene expression transformant of strain ATCC 33520 were constructed. Characterization of the mutant and transformant demonstrated that LrrA is associated with the extracytoplasmic fraction of T. denticola and expresses multifunctional properties. It was demonstrated that the attachment of strain ATCC 35405 to HEp-2 cell cultures and coaggregation with Tannerella forsythensis were attenuated by the lrrA mutation. In addition, an in vitro binding assay demonstrated specific binding of LrrA to a portion of the Tannerella forsythensis leucine-rich repeat protein, BspA, which is mediated by the N-terminal region of LrrA. It was also observed that the lrrA mutation caused a reduction of swarming in T. denticola ATCC 35405 and consequently attenuated tissue penetration. These results suggest that the leucine-rich repeat protein LrrA plays a role in the attachment and penetration of human epithelial cells and coaggregation with Tannerella forsythensis. These properties may play important roles in the virulence of T. denticola.
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