Protein–protein interaction of Moloney murine leukaemia virus was studied by an assay where one protein preparation was coupled covalently to Sepharose, and binding of radiolabelled proteins to the protein–Sepharose was examined. It was found that the virus proteins gp70, p30, p15E and p15 in solution could associate weakly to disrupted virus particles and to p30. However, when the disrupted virus particles and p30 were coupled to Sepharose in the presence of Triton X-100, stronger binding of the four proteins was observed. Only low or no binding of p12 and p10 was observed to these protein–Sepharoses. The results are discussed with respect to the assembly and structure of the virus particle.
BurnetteW. N.,
HollidayL. A.,
MitchellW. M.1976; Physical and chemical properties of Moloney murine leukemia virus p30 protein: a major core structural componant exhibiting high helicity and self-association. Journal of Molecular Biology 107:131–143
DavisN. L.,
RueckertR. R.1972; Properties of a ribonucleoprotein particle isolated from Nonidet P-40-treated Rous sarcoma virus. Journal of Virology 10:1010–1020
ForchhammerJ.,
KlarlundJ.1979; Changes in proteins from transformed cultures and tumors induced by sarcoma virus. In Carcinogenesis pp 51–60 Edited by
MargisonG. P.
Oxford and New York: Pergamon Press;
ForchhammerJ.,
TurnockG.1978; Glycoproteins from murine C-type virus are more acidic in virus derived from transformed cells than from nontransformed cells. Virology 88:177–182
HeleniusA.,
SimonsK.1977; Charge shift electrophoresis: simple method for distinguishing between amphiphilic and hydrophilic proteins in detergent solution. Proceedings of the National Academy of Sciences of the United States of America 74:529–532
HunterW. M.1967; The preparation of radioiodinated proteins of high activity, and their reaction with antibody in vitro. The radioimmunoassay. In Handbook of Experimental Immunology pp 608–654 Edited by
WeirD. M.
Oxford: Blackwell Scientific Publications;
LeisJ. P.,
McginnisJ.,
GreenR. W.1978; Rous sarcoma virus pl9 binds to specific double-stranded regions of viral RNA: effect of p19 on cleavage of viral RNA by RNase III. Virology 84:87–98
LowryO. H.,
RosebroughN. J.,
FarrA. L.,
RandallR. J.1951; Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193:265–275
MarcusS. L.,
SmithS. W.1978; Hydrophobic interaction of retroviral DNA polymerases with alkyl-agarose matrices. Biochemical and Biophysical Research Communications 80:220–228
MarcusS. L.,
SmithS. W.,
RacevskisJ.,
SarkarN. H.1979; Purification of murine oncornaviral phosphoproteins using alkyl-agarose derivatives. Journal of Biological Chemistry 254:4809–4813
MontelaroR. C.,
SullivanS. J.,
BolognesiD. P.1978; An analysis of type-C retrovirus polypeptides and their associations in the virion. Virology 84:19–31
PinterA.,
FleissnerE.1979; Structural studies of retroviruses: characterization of oligomeric complexes of murine and feline leukemia virus envelope and core components formed upon cross-linking. Journal of Virology 30:157–165
SchüleinM.,
BurnetteW. N.,
AugustJ. T.1978; Stoichiometry and specificity of binding of Rauscher oncovirus 10.000 dalton (p10) structural protein to nucleic acids. Journal of Virology 26:54–60
WitteO. N.,
WeissmanI. L.1974; Polypeptides of Moloney sarcoma-leukemia virions: their resolution and incorporation into extracellular virions. Virology 61:575–587
WongT. C.,
LewisR. B.,
BoseH. R.Jr,
KangC. Y.1980; Assembly of avian reticuloendotheliosis virus: association of the core precursor polypeptide with the intracellular ribonucleoprotein complex. Journal of Virology 34:484–489