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Thomas Vorup-Jensen

Identification of αLβ2, αMβ2, and αXβ2 integrins as receptors for Actinobacillus actinomycetemcomitans leukotoxin

Publikation: KonferencebidragPosterForskning

  • Institut for Medicinsk Mikrobiologi og Immunologi
  • Odontologisk Institut, Tandlægeskolen
A suspected virulence factor of Actinobacillus actinomycetemcomitans (A.a.) is an RTX-type of toxin that kills a variety of human leukocytes, hence referred to as leukotoxin (LtxA). Production of the toxin varies among A.a. strains. It is abundant in the so called JP2 clone, which is strongly associated with a highly aggressive form of disease in adolescents of African descent (1). An earlier report (2) identified the β2 integrin LFA-1 (αLβ2) as a cell surface receptor for LtxA. Whether the LtxA-reactive site involves αL (CD11a), β2 (CD18), or both of these subunits, is unknown.  Notably, the potential role of the integrins αMβ2 and αXβ2 (both of which include the β2 subunit) in reactions with LtxA has not been examined. The binding of endogenous ligands by integrins is regulated through conformational changes in the extracellular part of the receptor (3). The possibility that such changes affect also interaction with LtxA has not been addressed. Activity of LtxA on test target cells has been evaluated by enumeration of dead cells stained with trypan blue. This is a tedious and error-prone method, particularly in titration assays. By the present study, we wanted to characterize in more detail the cell surface molecular structure(s) that serve as receptor(s) for LtxA. We also wanted to establish a more reliable and convenient assay for the cytotoxicity of LtxA
StatusUdgivet - 2006
BegivenhedPeriodontal Diseases Gordon Research Conference - Il Ciocco, Italien
Varighed: 4 jun. 20069 jun. 2006


KonferencePeriodontal Diseases Gordon Research Conference
ByIl Ciocco

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