Abstract
Recombinant adenoviruses (Ads) have been used as reagents for biological studies and therapeutic protocols for the treatment of human patients. The two most commonly used Ads, Ad2 and Ad5, infect a broad range of tissues through interaction with the coxsackie and adenovirus receptor CAR. Both mutational analyses and crystal structure data have established residues in the fiber knob and shaft critical for Ad-CAR binding. In this report we review the contributions of various residues to Ad-CAR binding, taking into consideration the documented cellular tropism of other Ad serotypes.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Adenoviruses, Human / chemistry*
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Adenoviruses, Human / classification
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Adenoviruses, Human / metabolism
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Amino Acid Sequence
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Amino Acid Substitution
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Binding Sites
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Coxsackie and Adenovirus Receptor-Like Membrane Protein
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Crystallization
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Molecular Sequence Data
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Protein Binding
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Protein Conformation
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Protein Structure, Secondary
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Receptors, Virus / chemistry*
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Receptors, Virus / metabolism
Substances
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CLMP protein, human
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Coxsackie and Adenovirus Receptor-Like Membrane Protein
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Receptors, Virus