• Medientyp: E-Artikel
  • Titel: Multiple Functions of the Leucine-Rich Repeat Protein LrrA of Treponema denticola
  • Beteiligte: Ikegami, Akihiko; Honma, Kiyonobu; Sharma, Ashu; Kuramitsu, Howard K.
  • Erschienen: American Society for Microbiology, 2004
  • Erschienen in: Infection and Immunity
  • Sprache: Englisch
  • DOI: 10.1128/iai.72.8.4619-4627.2004
  • ISSN: 0019-9567; 1098-5522
  • Schlagwörter: Infectious Diseases ; Immunology ; Microbiology ; Parasitology
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  • Beschreibung: <jats:title>ABSTRACT</jats:title> <jats:p> The gene <jats:italic>lrrA</jats:italic> , encoding a leucine-rich repeat protein, LrrA, that contains eight consensus tandem repeats of 23 amino acid residues, has been identified in <jats:italic>Treponema denticola</jats:italic> 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 <jats:italic>T. denticola</jats:italic> ATCC 35405 expresses the <jats:italic>lrrA</jats:italic> gene, but the gene was not identified in <jats:italic>T. denticola</jats:italic> ATCC 33520. In order to analyze the functions of LrrA in <jats:italic>T. denticola</jats:italic> , an <jats:italic>lrrA</jats:italic> -inactivated mutant of strain ATCC 35405 and an <jats:italic>lrrA</jats:italic> 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 <jats:italic>T. denticola</jats:italic> and expresses multifunctional properties. It was demonstrated that the attachment of strain ATCC 35405 to HEp-2 cell cultures and coaggregation with <jats:italic>Tannerella forsythensis</jats:italic> were attenuated by the <jats:italic>lrrA</jats:italic> mutation. In addition, an in vitro binding assay demonstrated specific binding of LrrA to a portion of the <jats:italic>Tannerella forsythensis</jats:italic> leucine-rich repeat protein, BspA, which is mediated by the N-terminal region of LrrA. It was also observed that the <jats:italic>lrrA</jats:italic> mutation caused a reduction of swarming in <jats:italic>T. denticola</jats:italic> 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 <jats:italic>Tannerella forsythensis</jats:italic> . These properties may play important roles in the virulence of <jats:italic>T. denticola</jats:italic> . </jats:p>
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