Acid-induced structural changes in human rhinovirus 14: possible role in uncoating.
X-ray diffraction data were collected from human rhinovirus 14 crystals a few minutes after exposure to acid vapor and prior to excessive crystalline disorder. Conformational changes occurred (i) in the GH loop of viral protein (VP) 1, (ii) at the ion binding site on the outer surface of the pentamer center, and (iii) in VP3 and VP4 on the virion's interior in the vicinity of the fivefold axis. Amino acid substitutions in mutants resistant to low pH, or to drugs that inhibit uncoating, were concentrated in the vicinity of the GH loop. It is proposed that the acid-induced changes reflect processes that trigger uncoating.
Giranda
V L
VL
Department of Biological Sciences, Purdue University, West Lafayette, IN 47907.
Heinz
B A
BA
Oliveira
M A
MA
Minor
I
I
Kim
K H
KH
Kolatkar
P R
PR
Rossmann
M G
MG
Rueckert
R R
RR
D000595:Amino Acid Sequence; D002213:Capsid / Q000737:chemistry* / Q000235:genetics / Q000648:ultrastructure; D036022:Capsid Proteins; D006367:HeLa Cells; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D009154:Mutation; D011487:Protein Conformation; D012229:Rhinovirus / Q000737:chemistry* / Q000648:ultrastructure*; D010948:Viral Plaque Assay; D014961:X-Ray Diffraction / Q000379:methods
D036022:Capsid Proteins