Open AccessCapsid destabilization is required for antibody-mediated disruption of poliovirus
Author(s) -
Ingrid Delaet,
Albert Boeyé
Publication year - 1994
Publication title -
journal of general virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.55
H-Index - 167
eISSN - 1465-2099
pISSN - 0022-1317
DOI - 10.1099/0022-1317-75-3-581
Subject(s) - capsid , neutralization , ionic strength , poliovirus , dissociation (chemistry) , monoclonal antibody , virology , biology , antigen , ionic bonding , antibody , biophysics , virus , chemistry , immunology , ion , organic chemistry , aqueous solution
Three out of 36 poliovirus type 1-specific monoclonal antibodies which, at 37 degrees C in a medium of normal ionic strength (mu = 0.16), caused only aggregative neutralization (reversible by immune complex dissociation at pH 2) shifted to cause disruptive, acid-irreversible neutralization when the temperature was raised to 39 degrees C or the ionic strength was lowered to 1/100 of normal. Under both conditions, the antigenic conversion was stoichiometric, but the efficiency was lower at 39 degrees C than at low ionic strength. Antigenic conversion and irreversible neutralization under both conditions were inhibited by WIN 51711, a capsid-stabilizing compound. Complete inhibition required filling of most of the virion's binding pockets by this compound.