The Positively Charged Structural Virus Protein (VP1) of Foot-and-Mouth Disease Virus (Type O1) Contains a Highly Basic Part which may be Involved in Early Virus-Cell Interaction
Polypeptides of ‘trypsin-resistant’ (TR) variants of foot-and-mouth disease virus type O1 (BFS 1860) were analysed by electrofocusing and two-dimensional gel electrophoresis. In contrast to parent O1 virus, trypsin treatment of these variants did not reduce their infectivity and their ability to attach to susceptible cells, although VP1 was cleaved as in the parent virus. In OTR1, one of the cloned isolates, an additional polypeptide (VPa) with a mol. wt. approx. 31 × 103 (31K), was found which resembled VP1 (28K) in being positively charged and cleaved by trypsinization of the virus into a neutral 18K polypeptide (P18) and a strongly basic fragment (pI > 10) with a mol. wt. of approx. 6K (P6). These findings substantiate the hypothesis that VPa is an elongated VP1. While P18 fragments of both trypsin-treated parent virus and OTR progeny viruses focused at identical (neutral) pH. P6 fragments of trypsinized OTR variants (including OTR1) were even more positively charged than P6 of parent virus. This difference in charge of the P6 polypeptide may be responsible for the retained cell attachment ability of trypsinized OTR viruses. The data are discussed with respect to the known amino acid sequence of VP1 of the closely related O1 Kaufbeuren.
BartelingS. J.,
MeloenR. H.,
WagenaarF.,
GielkensA. L. J.1979; Isolation and characterization of trypsin-resistant O, variants of foot-and-mouth disease virus. Journal of General Virology 43:383–393
BrownF.,
CartwrightB.,
StewartD. L.1963; The effect of various inactivating agents on the viral and ribonucleic acid infectivities of foot-and-mouth disease virus and on its attachment of susceptible cells. Journal of General Microbiology 31:179–186
CrowtherJ. R.1977; Examination of differences between foot-and-mouth disease strains using a radio immuno assay technique. International Symposium on Foot-and-Mouth Disease Virus, Lyon 1976. Developments in Biological Standardization 35:185–193
KitamuraN.,
SemlerB. L.,
RothbergP. G.,
LarsenG. R.,
AdlerC. J.,
DornerA. J.,
EminiE. A.,
HanecakR.,
LeeJ.J.,
Van Der WerfS.,
AndersonC. W.,
WimmerE.1981; Primary structure, gene organization and polypeptide expression of poliovirus RNA. Nature, London 291:547–553
KleidD. G.,
YansuraD.,
SmallB.,
DowbenkoB.,
MooreD. M.,
GrubmanM. J.,
McKercherP. D.,
MorganO. O.,
RobertsonB. H.,
BachrachH. L.1981; The cloned foot-and-mouth disease viral protein VP3 expressed in E. coli elicits protective immunogenic responses in cattle and swine. Sciences 214:1125–1129
KurzC.,
ForssS.,
KüpperH.,
StrohmaierK.,
SchallerH.1981; Nucleotide sequence and corresponding amino acid sequence of the gene for the major antigen of foot-and-mouth disease virus. Nucleic Acids Research 9:1919–1931
O’farrellP. Z.,
GoodmanH. M.,
O’farrellP. H.1977; High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell 12:1133–1142
RobsonK. J. H.,
CrowtherJ. R.,
KingA. M. Q.,
BrownF.1979; Comparative biochemical and serological analysis of five isolates of a single serotype of foot-and-mouth disease virus. Journal of General Virology 37:271–276
RowlandsD. J.,
SangarD. V.,
BrownF.1971; Relationship of the antigenic structure of foot-and-mouth disease virus to the process of infection. Journal of Virology 13:85–93
SangarD. V.,
BlackD. N.,
RowlandsD. J.,
BrownF.1977; Biochemical mapping of the foot-and-mouth disease virus genome. Journal of General Virology 35:281–297
StrohmaierK.,
FranzeR.,
AdamK.-H.1982; Location and characterization of the antigenic portion of the FMDV immunizing protein. Journal of General Virology 59:295–306
WilsonJ. A.,
SkehelJ. J.,
WileyD. C.1980; Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 á resolution. Nature, London 289:366–373
The Positively Charged Structural Virus Protein (VP1) of Foot-and-Mouth Disease Virus (Type O1) Contains a Highly Basic Part which may be Involved in Early Virus-Cell Interaction