Variation in liposome binding among enteroviruses.
Liposome-binding properties of native virions and in vitro generated 135S particles of eight enteroviruses were studied. The temperature required for the structural transition from the native 160S virion to a 135S particle was virus-specific, ranging from +38 degrees C to more than +50 degrees C. While the 135S particles of poliovirus 1/Mahoney (PV1) and coxsackievirus A21 (CAV21) were capable of binding to liposomes, the other viruses showed minimal binding. Both of the viruses that bound to liposomes as 135S particles also bound as native virions. In addition, PV3/Sabin bound to liposomes as native virions but not as 135S particles, and the flotation patterns were different from those of PV1 and CAV21. The nonbinding viruses included coxsackieviruses A7, A9, A16, and B5, and enterovirus 68. The results follow the new classification of enteroviruses, as CAV21 is a member of the human enterovirus C species, which is genetically close to the poliovirus species.
Airaksinen
A
A
Enterovirus Laboratory, National Public Health Institute (KTL), Mannerheimintie 166, Helsinki, FIN-00300, Finland. airaksinen@cbm.uam.es
Somerharju
P
P
Hovi
T
T
D002499:Centrifugation, Density Gradient; D004770:Enterovirus / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008081:Liposomes / Q000032:analysis / Q000378:metabolism*; D017955:Poliovirus / Q000378:metabolism; D013045:Species Specificity; D013696:Temperature; D014771:Virion / Q000378:metabolism
D008081:Liposomes