The envelope of the bunyavirus La Crosse contains two glycoproteins, G1 (120000 mol. wt.) and G2 (38000 mol. wt.). When incubated with trypsin or plasmin, the G1 glycoprotein of virus grown in cell culture was cleaved, leaving two different sized polypeptides in the envelope (67000 and 95000 mol. wt.). Chymotrypsin cleaved G1 leaving polypeptides of 70000 and 100000 mol. wt. G2, however, was not altered by these enzymes. When used in antibody neutralization studies, these proteolytically modified viruses were neutralized approximately 1 to 2 log10 units in 60 min while control virus was neutralized by over 4 log10 units in 20 min. Because antibody to G1, but not G2, was involved in La Crosse virus neutralization, cleavage of G1 appeared to be directly responsible for these altered kinetics of neutralization. Antibody did bind to the polypeptides remaining associated with the envelope resulting in infectious virus-antibody complexes. This indicated that a critical site in terms of antibody neutralization was removed from G1 by proteolytic enzymes.
BonnerW. M.,
LaskeyR. A.1974; A film detection method for tritium-labeled proteins and nucleic acids in polyacrylamide gels. European Journal of Biochemistry 46:83–88
ChanasA. C.,
GouldE. A.,
CleggJ. C. S.,
VarmaM. G. R.1982; Monoclonal antibodies to Sindbis virus glycoprotein E1 can neutralize, enhance infectivity, and independently inhibit haemagglutination or haemolysis. Journal of General Virology 58:37–46
ClarkeD. H.,
CasalsJ.1958; Techniques for hemagglutination and hemagglutination-inhibition with arthropod-borne viruses. American Journal of Tropical Medicine and Hygiene 7:561–573
DalrympleJ. M.,
SchlesingerS.,
RussellP. K.1976; Antigenic characterization of two Sindbis envelope glycoproteins separated by isoelectric focusing. Virology 69:93–103
GentschJ. R.,
RozhonE. J.,
KlimasR. A.,
El SaidL. H.,
ShopeR. E.,
BishopD. H. L.1980; Evidence from recombinant bunyavirus studies that the M RNA gene products elicit neutralizing antibodies. Virology 102:190–204
HommaM.,
OhuchiM.1973; Trypsin action on the growth of Sendai virus in tissue culture cells. Ⅲ. Structural differences of Sendai viruses grown in eggs and tissue culture cells. Journal of Virology 12:1457–1465
HummelB. C. W.1959; A modified spectrophotometric determination of chymotrypsin, trypsin, and thrombin. Canadian Journal of Biochemistry and Physiology 37:1393–1399
ItoH.,
IwasaS.1980; Simple serological diagnosis of arboviruses: a simplified diluent system for Japanese encephalitis virus hemagglutination-inhibition tests using formalinized chick erythrocytes. Journal of Virological Methods 1:299–302
KelleyJ. M.,
EmersonS. U.,
WagnerR. R.1972; The glycoprotein of vesicular stomatitis virus is the antigen that gives rise to and reacts with neutralizing antibody. Journal of Virology 10:1231–1235
KingsfordL.,
EmersonS. U.,
KelleyJ. M.1980; Separation of cyanogen bromide-cleaved peptides of the vesicular stomatitis virus glycoprotein and analysis of their carbohydrate content. Journal of Virology 36:309–316
MontelaroR. C.,
RueckertR. R.1975; Radiolabeling of proteins and viruses in vitro by acetylation with radioactive acetic anhydride. Journal of Biological Chemistry 250:1413–1421
O’FarrellP. Z.,
GoldL. M.,
HuangW. M.1973; The identification of prereplicative bacteriophage T4 proteins. Journal of Biological Chemistry 248:5499–5501
QureshiA. A.,
TrentD. W.1973; Group B arbovirus structural and nonstructural antigens. I. Serological identification of Saint Louis encephalitis virus soluble antigens. Infection and Immunity 7:242–248
SkehelJ. J.,
WaterfieldM. D.1975; Studies on the primary structure of the influenza virus hemagglutinin. Proceedings of the National Academy of Sciences, U. S. A 72:93–97
Ter MeulenV.,
LӧfflerS.,
CarterM. J.,
StephensonJ. R.1981; Antigenic characterization of measles and SSPE virus haemagglutinin by monoclonal antibodies. Journal of General Virology 57:357–364
WebsterR. G.,
HinshawV. S.,
LaverW. G.1982; Selection and analysis of antigenic variants of the neuraminidase on N2 influenza vuses with monoclonal antibodies. Virology 117:93–104