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J Virol. 1968 May; 2(5): 430-439
Copyright © 1968 American Society for Microbiology. All Rights Reserved.

Role of Adenovirus Structural Proteins in the Cessation of Host-Cell Biosynthetic Functions ¹

Department of Microbiology, School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104

ABSTRACT

Two of the adenovirus capsid proteins, the fiber and the hexon, complexed with either KB cell or type 5 adenovirus deoxyribonucleic acid (DNA). Maximal binding occurred at 0.01 M NaCl; increasing the ionic strength of the reaction mixture to 0.2 M NaCl resulted in a decrease in the association of either antigen to DNA. Variations of pH between 6.3 and 8.4 did not affect the binding of fiber antigen to DNA. Below pH 7.5, however, there was a small decrease in the ability of the hexon to bind nucleic acid. The association between the adenovirus structural proteins and DNA was reversible and was independent of whether the DNA was native or denatured. The fiber or hexon protein inhibited the DNA-dependent ribonucleic acid (RNA) polymerase and the DNA polymerase from KB cells. On a weight basis, the fiber protein inhibited enzymatic activity to a greater extent than the hexon. Increasing the template DNA concentration decreased this inhibition. The inhibition of the DNA-dependent RNA polymerase activity by either antigen could be reversed by increasing the ionic strength of the reaction mixture. After infection of KB cells with type 5 adenovirus, the levels of DNA and RNA polymerases remained unchanged for 15 to 20 hr. Thereafter, the specific activity of both enzymes decreased. By 30 hr postinfection, the polymerase activities were only about 30% of the enzyme activities in uninfected cells.

² Present address: California Institute of Technology, Division of Biology, Pasadena, Calif. 91109.

¹ A preliminary report of this investigation was presented at the Annual Meeting of the American Society for Microbiology, Los Angeles, Calif., 1966. Presented to the Faculty of the Graduate School of Arts and Sciences of the University of Pennsylvania in partial fulfillment of the requirements for the PhD. degree by A. J. Levine.