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- W2000558189 abstract "TRENDS IN MICROBIOLOGY 393 VOL. 8 NO. 9 SEPTEMBER 2000 0966-842X/00/$ see front matter © 2000 Elsevier Science Ltd. All rights reserved. PII: S0966-842X(00)01820-5 Our paper in Science 1 was the first to demonstrate that the fibers of the coxsackie–adenovirus receptor (CAR) recognizing adenovirus (Ad) serotypes Ad5, Ad9 and Ad41 (the long fiber) do so with a more or less conserved binding site that maps to the side of the threefold symmetrical fiber protein1. This was independently confirmed by the mutagenesis and structural analysis study of the Ad5 fiber by Kirby et al.2 Additionally, Bewley et al. identified the CAR-binding site by co-crystallizing the Ad12 fiber with the amino-terminal D1 domain of the CAR protein3. Structural analysis of the Ad2 fiber has resulted in the identification of a putative, similar binding site on the side of the Ad2 fiber4. Mutations that ablate CAR binding are not limited to the AB loop per se. Indeed, we and others have shown that replacement mutations as well as deletions in structures such as the B-b sheet, the DE and the FG loops (also referred to as the DG loop) can result in ablation of CAR binding1–3,5. As was noted in our paper, mutagenesis of critical residues in the Ad5 fiber AB loop does not consistently result in complete ablation of gene transfer by Ad5. Indeed, in a typical assay, the fiber-mutated Ad vector will transduce 1–2% of cells. We have determined that this transduction results from the interaction of the Ad vector penton base protein with cellular av integrins, which have been shown to be the Ad internalization receptors6. This is not surprising, as integrins have previously been shown to function Adenoviral vectors – new insights: Response" @default.
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- W2000558189 title "Adenoviral vectors – new insights: Response" @default.
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- W2000558189 doi "https://doi.org/10.1016/s0966-842x(00)01820-5" @default.
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