Open AccessIntegrinα3β1 Is an Alternative Cellular Receptor for AdenovirusSerotype5
Author(s) -
B. Salone,
Yuri Martina,
Stefania Piersanti,
Enrico Cundari,
Gioia Cherubini,
Laure Franqueville,
Cristina Maria Failla,
Pierre Boulanger,
Isabella Saggio
Publication year - 2003
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.77.24.13448-13454.2003
Subject(s) - biology , internalization , integrin , rgd motif , transduction (biophysics) , receptor , coxsackievirus , microbiology and biotechnology , capsid , adenoviridae , mutant , binding site , virology , virus , biochemistry , enterovirus , recombinant dna , gene
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 alpha3beta1 for adenovirus serotype 5 (Ad5). We found that penton base and integrin alpha3beta1 could interact in vitro. In vivo, both Ad5-cell binding and virus-mediated transduction were inhibited in the presence of anti-alpha3 and anti-beta1 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 alpha3beta1, which involved multiple additional contact sites.