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Vitronectin receptors, V-integrins, are recognized by several non-RGD containing echoviruses in a continuous laboratory cell line and also in primary human Langerhans' islets and endothelial cells

¹ National Institute for Health and Welfare;
² University of Helsinki

³ E-mail: merja.roivainen{at}thl.fi

Previously published data suggest that the RGD recognizing integrin, Vβ3, known as the vitronectin receptor, acts as a cellular receptor for RGD containing enteroviruses, coxsackievirus A9 and echovirus 9, in several continuous cell lines as well as in primary human Langerhans' islets. Since this receptor is also capable of binding the ligands by non-RGD-dependent mechanism we investigated here whether vitronectin receptors, V-integrins, might act as a receptor for other echoviruses which do not have RGD motif. Blocking experiments with polyclonal anti-Vβ3 antibody showed that both primary human islets and a continuous laboratory cell line of green monkey kidney origin (GMK) are similarly protected from adverse effects of several non-RGD containing echovirus (E-7, 11, 25, 30, 3) infections. In contrast, the corresponding studies on primary human endothelial cells showed that the receptor works only for E-25, E-30, E-32 and CAV-9. The inhibitory effect of the antibody was not restricted to prototype strains of echoviruses since GMK cells infected with several field isolates of the corresponding serotypes were also protected from virus induced cytopathic effects. Colocalization of virus particles with the receptor molecules in both GMK and primary human endothelial cells was demonstrated by live cell stainings in confocal microscopy. Remarkably in spite of similar virus-receptor colocalization and comparable protective effect of the Vβ3 antibody, the entry pathways of the studied virus strains seemed to be divergent.

Received 14 June 2009; accepted 22 September 2009.