Shortening adenovirus type 5 fiber shaft decreases the efficiency of postbinding steps in CAR-expressing and nonexpressing cells.
The coxsackie B virus and adenovirus receptor (CAR) functions as an attachment receptor for multiple adenovirus serotypes. It has been shown that apart from virus-cellular receptor interactions, the fiber shaft length also influences viral tropism. We therefore generated Ad5FbDelta639 virus with 8beta-repeats in the shaft, instead of the 22beta-repeats present in the wild-type. Here, we show that the extent of attachment of the virus with shortened fiber to CAR-expressing cells was three- to fivefold lower than that of the wild-type. Transduction studies, however, clearly showed that infection of CAR-expressing cells with Ad5FbDelta639 was strongly impaired by comparison with the wild-type virus. Since this impairment was not linked to a proportional reduction in binding to cells, it appeared to be linked to subsequent/later events in infection. A similar decrease in efficacy of postbinding steps was also evidenced in cells that did not express CAR.
Ambriović-Ristov
Andreja
A
Laboratory for Genotoxic Agents, Department for Molecular Genetics, Ruğer Bosković Institute, Bijenicka 54, 10000 Zagreb, Croatia.
Mercier
Stephanie
S
Eloit
Marc
M
D000256:Adenoviridae / Q000254:growth & development / Q000378:metabolism*; D000818:Animals; D036022:Capsid Proteins / Q000737:chemistry* / Q000378:metabolism*; D002460:Cell Line; D062727:Coxsackie and Adenovirus Receptor-Like Membrane Protein; D006224:Cricetinae; D009154:Mutation; D011991:Receptors, Virus / Q000235:genetics / Q000378:metabolism*; D014161:Transduction, Genetic
D036022:Capsid Proteins; D062727:Coxsackie and Adenovirus Receptor-Like Membrane Protein; D011991:Receptors, Virus; C018315:hexon capsid protein, Adenovirus