Interactions of soluble recombinant integrin αvβ5 with human adenoviruses

alpha v integrins have been identified as coreceptors for adenovirus (Ad) internalization; however, direct interactions of these molecules with Ad have not been demonstrated. We report here the expression of soluble integrin alpha v beta 5, which retains the ability to recognize the Ad penton base as well as vitronectin, an Arg Gig Asp (RGD)-containing extracellular matrix protein. Soluble integrin alpha v beta 5 reacted with seven different Ad serotypes (subgroups A to E) in solid phase binding assays. The soluble integrin exhibited different levels of binding to each Ad serotype; however, binding to multiple Ad types required the presence of divalent metal cations and was inhibited by a synthetic RGD peptide, indicating that RGD and cation-binding sequences regulate Ad interactions with alpha v beta 5, Incubation of Ad particles with soluble alpha v beta 5 integrin also inhibited subsequent Ad internalization into epithelial cells as well as virus attachment to monocytic cells, These findings suggest that soluble alpha v integrins or antagonists of these coreceptors could be used to limit infection by multiple Ad types. The generation of soluble av integrins should also permit further detailed kinetic and structural analysis of Ad interactions with its coreceptors.