Integrin α3β1 is an Alternative Cellular Receptor for Adenovirus Serotype 5

Barbara Salone, Yuri Martina, Stefania Piersanti, Enrico Cundari, Gioia Cherubini, Laure Franqueville, Cristina M. Failla, Pierre Boulanger, Isabella Saggio

Research output: Contribution to journalArticlepeer-review

Abstract

Many adenovirus serotypes enter cells by high-affinity binding to the coxsackievirus-adenovirus receptor (CAR) and integrin-mediated internalization. In the present study, we analyzed the possible receptor function of α3β1 for adenovirus serotype 5 (Ad5). We found that penton base and integrin α3β1 could interact in vitro. In vivo, both Ad5-cell binding and virus-mediated transduction were inhibited in the presence of anti-α3 and anti-β1 function-blocking antibodies, and this occurred in both CAR-positive and CAR-negative cell lines. Peptide library screenings and data from binding experiments with wild-type and mutant penton base proteins suggest that the Arg-Gly-Asp (RGD) in the penton base protein, the best known integrin binding motif, is only part of the binding interface with α3β1, which involved multiple additional contact sites.

Original languageEnglish
Pages (from-to)13448-13454
Number of pages7
JournalJournal of Virology
Volume77
Issue number24
DOIs
Publication statusPublished - Dec 2003

ASJC Scopus subject areas

  • Immunology

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