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 Kiley, M. P. Articles by Johnson, K. M. Search for Related Content PubMed PubMed Citation Articles by Kiley, M. P. Articles by Johnson, K. M. Agricola Articles by Kiley, M. P. Articles by Johnson, K. M.

Ebola Virus: Identification of Virion Structural Proteins

Special Pathogens Branch, Virology Division, Bureau of Laboratories, Center for Disease Control, Public Health Service, U.S. Health, Education, and Welfare, Atlanta, Georgia 30333, U.S.A.

Polyacrylamide gel electrophoresis of purified Ebola virus revealed the presence of four major virion structural proteins which we have designated VP1, VP2, VP3 and VP4. Vesicular stomatitis virus (VSV) proteins were used as mol. wt. markers, and the virion proteins were found to have mol. wt. of 125000 (VP1), 104000 (VP2), 40000 (VP3) and 26000 (VP4). VP1 was labelled with glucosamine and is probably a glycoprotein. The density of the Ebola virion was approx. 1.14 g/ml in potassium tartrate. Virus nucleocapsids with a density of 1.32 g/ml in caesium chloride were released when virions were treated with detergents. Proteins VP2 and VP3 were consistently associated with released nucleocapsids and are probably the major structural nucleocapsid proteins analogous to the N protein of VSV. Protein VP4 was reduced or absent in released nucleocapsids and is probably analogous to the membrane (M) protein of VSV and similar viruses. The glycoprotein (VP1) is larger than the glycoprotein of any known negative-strand RNA virus and is not labelled well with ³⁵S-methionine. VP1 is solubilized by detergent treatment, suggesting that it is a component of the virion spikes and analogous to the G protein of VSV. Our results, in conjunction with analysis of Ebola virion RNA (Regnery et al. 1980), strongly suggest that the virus is a negative-strand RNA virus and, along with Marburg virus, may constitute a new taxon within this group.

Received 5 October 1979; accepted 6 March 1980.

This article has been cited by other articles:

				A. Bukreyev, P. E. Rollin, M. K. Tate, L. Yang, S. R. Zaki, W.-J. Shieh, B. R. Murphy, P. L. Collins, and A. Sanchez Successful Topical Respiratory Tract Immunization of Primates against Ebola Virus J. Virol., June 15, 2007; 81(12): 6379 - 6388. [Abstract] [Full Text] [PDF]

				M. Niikura, T. Ikegami, M. Saijo, T. Kurata, I. Kurane, and S. Morikawa Analysis of Linear B-Cell Epitopes of the Nucleoprotein of Ebola Virus That Distinguish Ebola Virus Subtypes Clin. Vaccine Immunol., January 1, 2003; 10(1): 83 - 87. [Abstract] [Full Text] [PDF]

				A. Sanchez, Z.-Y. Yang, L. Xu, G. J. Nabel, T. Crews, and C. J. Peters Biochemical Analysis of the Secreted and Virion Glycoproteins of Ebola Virus J. Virol., August 1, 1998; 72(8): 6442 - 6447. [Abstract] [Full Text] [PDF]

				A. Takada, C. Robison, H. Goto, A. Sanchez, K. G. Murti, M. A. Whitt, and Y. Kawaoka A system for functional analysis of Ebola virus glycoprotein PNAS, December 23, 1997; 94(26): 14764 - 14769. [Abstract] [Full Text] [PDF]