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Role of adenovirus structural proteins in the cessation of host-cell biosynthetic functions

Levine, A. J. and Ginsberg, H. S. (1968) Role of adenovirus structural proteins in the cessation of host-cell biosynthetic functions. Journal of virology, 2 (5). pp. 430-439. ISSN 0022-538X. PMCID PMC375631.

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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.

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Additional Information:© 1968 American Society for Microbiology. Received for publication 6 December 1967. 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. It is a pleasure to thank J. J. Furth for his many helpful discussions, his frequent aid in the assay of the polymerases, and for the gift of E. coli DNA-dependent RNA polymerase. The data in Table 1 were obtained in collaboration with L. Bello. This investigation was supported by Public Health Service Grant AI-03620 and Training Grant AI-203, from the National Institute of Allergy and Infectious Diseases, and was also under the sponsorship of the Commission on Acute Respiratory Diseases of the Armed Forces Epidemiological Board, and was supported in part by the U.S. Army Medical Research & Development Command, Department of the Army, under research contract DA-49-193-MD-2131.
Funding AgencyGrant Number
NIH Predoctoral FellowshipAI-203
Armed Forces Epidemiological BoardUNSPECIFIED
Army Medical Research & Development CommandDA-49-193-MD-2131
Issue or Number:5
PubMed Central ID:PMC375631
Record Number:CaltechAUTHORS:20190308-121709230
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Official Citation:Role of Adenovirus Structural Proteins in the Cessation of Host-Cell Biosynthetic Functions A. J. Levine, H. S. Ginsberg Journal of Virology May 1968, 2 (5) 430-439
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:93654
Deposited By: George Porter
Deposited On:08 Mar 2019 22:08
Last Modified:03 Oct 2019 20:56

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