HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Neurath, A. R. Articles by Rubin, B. A. Search for Related Content PubMed PubMed Citation Articles by Neurath, A. R. Articles by Rubin, B. A. Agricola Articles by Neurath, A. R. Articles by Rubin, B. A.

Characterization of Subviral Components Resulting from Treatment of Rabies Virus with Tri(n-butyl) Phosphate

Department of Research and Development, Wyeth Laboratories, Philadelphia, Pennsylvania 19101, U.S.A.

The PM strain of rabies virus was grown in human diploid WI-38 cells and labelled with the following radioactive substances: [¹⁴C]- or [³H]-d-glucosamine, [¹⁴C]-uridine, [¹⁴C]-stearic acid, [³H]-choline and a mixture of [¹⁴C]-amino acids. It was then purified and treated with 0.1% tri(n-butyl)phosphate (TNBP) in the presence of 0.1% Tween 80. All the stearic acid and choline and about 82% and 40%, respectively, of the d-glucosamine and amino acid (but none of the uridine) label was released from the virus. It was concluded that TNBP dissociates the lipids, most of the glycoproteins, and small quantities of non-glycosylated proteins from the virus leaving behind particles containing all of the virus RNA. These particles sedimented in sucrose gradients at the same rate as did intact virus; they had a higher buoyant density in CsCl gradients (1.304 compared with 1.244 g./cm³.) and they resembled intact virus in overall size and shape but lacked most of the surface projections. By polyacrylamide gel electrophoresis the following polypeptide species were identified in intact particles (tentative molecular weights are given in parentheses): glycoproteins (GP1 (78,000) and GP2 (65,000); nucleocapsid proteins NP1 (58,000) and NP2 (47,000) and two additional proteins MP (35,000) and CP (22,000). Treatment with TNBP released nearly all GP1 and GP2 and small quantities of MP. Particles obtained by treatment of the virus with the proteolytic enzyme bromelain also lacked the surface projections (and the glycoproteins GP1 and GP2) but retained the lipids.

Received 2 August 1971; accepted 6 September 1971.

This article has been cited by other articles:

				T. J. Wiktor, S. A. Plotkin, and D. W. Grella Human Cell Culture Rabies Vaccine: Antibody Response in Man JAMA, May 21, 1973; 224(8): 1170 - 1171. [Abstract] [PDF]