Open AccessAcid-induced structural changes in human rhinovirus 14: possible role in uncoating.
Author(s) -
Vincent L. Giranda,
Beverly A. Heinz,
Marcos Antônio de Oliveira,
Iwona Minor,
Kyung Hyun Kim,
Prasanna R. Kolatkar,
Michael G. Rossmann,
Roland R. Rueckert
Publication year - 1992
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.89.21.10213
Subject(s) - pentamer , rhinovirus , mutant , chemistry , biophysics , crystallography , protein structure , virology , virus , biology , biochemistry , gene
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.