Rhodanine resistance and dependence of echovirus 12: a possible consequence of capsid flexibility.
Recombinant viruses of echovirus 12 carrying mutations of a rhodanine-resistant or -dependent variant, were investigated, and five single mutations each inducing a rhodanine-resistant or -dependent phenotype were defined. Four mutations are localized in the capsid protein VP1, and the fifth exchange is in VP4. All original and recombinant viruses were shown to be stabilized by the antiviral drug rhodanine against heat inactivation. Hence, resistant and dependent variants still seem able to bind rhodanine, and apparently none of the exchanges affects the putative drug binding site. We hypothesize that drug resistance and dependence are consequences of an increased flexibility of the virus capsid.
Kraus
W
W
Institut fur Virologie der Universitat zu Koln, Cologne, Germany.
Zimmermann
H
H
Eggers
H J
HJ
Nelsen-Salz
B
B
D000595:Amino Acid Sequence; D002213:Capsid / Q000235:genetics*; D004351:Drug Resistance / Q000235:genetics*; D029822:Enterovirus B, Human / Q000187:drug effects / Q000235:genetics*; D016679:Genome, Viral; D008969:Molecular Sequence Data; D009154:Mutation; D012236:Rhodanine / Q000494:pharmacology*; D016415:Sequence Alignment
D012236:Rhodanine