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J Virol. 1972 June; 9(6): 923-929
Copyright © 1972 American Society for Microbiology. All Rights Reserved.

Structure and Function of the Polypeptides in Simian Virus 40 I. Existence of Subviral Deoxynucleoprotein Complexes

Eng-Shang Huang, Mary K. Estes and Joseph S. Pagano

1 Department of Bacteriology and Immunology and Department of Medicine, School of Medicine, University of North Carolina, Chapel Hill, North Carolina 27514

ABSTRACT

Velocity sedimentation analysis of simian virus 40 degraded in alkaline buffers, pH 10.5, yields two components: soluble protein containing the largest polypeptides, VP1 and VP2, of the virion, and a deoxynucleoprotein complex (DNP-I) containing the viral deoxyribonucleic acid (DNA) and the small polypeptides, VP4, 5, and 6, and all or part of VP3. Dissociation of DNP-I by equilibrium centrifugation in CsCl yields a complex (DNP-II) of the viral DNA and residual, tightly bound polypeptide; VP4, 5, and 6, but not VP3, are recovered after separation from DNP-II. Treatment of the virus with ß-mercaptoethanol and iodination experiments suggest that VP1 and VP2 might exist as compact structures cross-linked with disulfide bonds, perhaps forming the capsid. VP4, 5, and 6 form a relatively stable complex with the viral DNA and are supposed to be the internal proteins. The location of VP3 is not well defined; at least a portion of it is tightly bound to the viral DNA.

J Virol. 1972 June; 9(6): 923-929
Copyright © 1972 American Society for Microbiology. All Rights Reserved.



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