Biochemical and biophysical studies on the nucleocapsid and on the RNA of rabies virus

Sokol, F.; Schlumberger, H. D.; Wiktor, Tadeusz J.; Koprowski, Hilary; Hummeler, Klaus

doi:10.1016/0042-6822(69)90184-6

Cited by 89 publications

(52 citation statements)

References 35 publications

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“…When released from virions, the nucleocapsids of rhabdoviruses form helices -20 nm in diameter (13,(14)(15)(16)(17). The effect of salt concentration on VSV nucleocapsids was examined and, as with paramyxoviruses, the VSV nucleocapsid was found to unwind reversibly at low salt concentration.…”

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confidence: 99%

“…Two other proteins (L and P) are associated with the nucleocapsid and thought to be involved in the viral RNA transcriptase activity (8)(9)(10)(11)(12). The nucleocapsids of rhabdoviruses-e.g., vesicular stomatitis (VSV) and rabies viruses-also consist of a single-stranded RNA complexed with a single major structural protein (N) and two associated proteins (NS and L) (13)(14)(15)(16)(17)(18). In the VSV virion, the nucleocapsid forms a coil t40 nm in diameter but, when separated from the viral membrane, it is often found in helices of considerably smaller diameter (13)(14)(15)(16)(17).…”

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confidence: 99%

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Conformation of the helical nucleocapsids of paramyxoviruses and vesicular stomatitis virus: reversible coiling and uncoiling induced by changes in salt concentration.

Heggeness¹,

Scheid²,

Choppin³

1980

Proc. Natl. Acad. Sci. U.S.A.

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The conformations of the helical nucleocapsids of the paramyxoviruses Sendai virus and simian virus 5, and of a rhabdovirus, vesicular stomatitis virus, have been found to vary extensively with changes in salt concentration. In 10 mM sodium phosphate buffer at pH 7.2, the nucleocapsids are loosely coiled or almost completely extended; with increasing concentrations of NaCl they become more tightly coiled and less flexible. Under isotonic conditions (150 mM) the Sendai virus nucleocapsid is moderately tightly coiled but still curved and apparently flexible, whereas at 400 mM or higher it is very tightly coiled, with the appearance of a rigid rod. These saltdependent changes in conformation were also found with nucleocapsids composed of proteolytically cleaved protein subunits. Because of the effect of salt concentration, and the fact that it may change during the preparation of negatively stained samples for electron microscopy, it was necessary to fix the nucleocapsids before negative staining to preserve their original conformation. The striking changes in nucleocapsid conformation in response to the ionic milieu indicate the plasticity of its helical structure and suggest that changes in the microenvironment of the nucleocapsid could influence its conformation during viral RNA transcription and replication or during virus assembly by budding, processes in which changes in the coiling of the nucleocapsid or its flexibility could be important. The nucleocapsids of paramyxoviruses, such as Sendai virus, simian virus 5 (SV5), and Newcastle disease virus, are single, left-handed, helical structures which, when tightly coiled, have a diameter of 15-18 nm and a length of ;1 ,m (1-5). They are composed of single-stranded RNA and -2600 viral structural protein subunits (NP) with a molecular weight of t60,000 (6, 7). Two other proteins (L and P) are associated with the nucleocapsid and thought to be involved in the viral RNA transcriptase activity (8-12). The nucleocapsids of rhabdoviruses-e.g., vesicular stomatitis (VSV) and rabies viruses-also consist of a single-stranded RNA complexed with a single major structural protein (N) and two associated proteins (NS and L) (13-18). In the VSV virion, the nucleocapsid forms a coil t40 nm in diameter but, when separated from the viral membrane, it is often found in helices of considerably smaller diameter (13-17).The conformation of paramyxovirus nucleocapsids has shown wide variations as observed in the electron microscope. They have been seen to have tightly stacked turns and the overall appearance of relatively stiff rods ;1 ,um in length and also as loosely coiled helices extended to varying degrees (1-7, 19, 20). Proteolytic cleavage of the NP protein has been implicated as one of the causes of such variation in nucleocapsid conformation (6, 21); however, in the course of an electron microscopic study of Sendai virus nucleocapsids, we often observed a wide variation in the degree of coiling of duplicate samples that could not be attributed to this mechanism. When ...

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confidence: 99%

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confidence: 99%

Conformation of the helical nucleocapsids of paramyxoviruses and vesicular stomatitis virus: reversible coiling and uncoiling induced by changes in salt concentration.

Heggeness¹,

Scheid²,

Choppin³

1980

Proc. Natl. Acad. Sci. U.S.A.

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“…Clonal isolates of ERA and HEP strains of rabies virus were propagated in monolayers of BHK/S13 cells grown in roller bottles according to a technique described elsewhere (3). Tissue-culture media infected with the ERA strain used in the test had an infectivity titer of 6 X 108 plaque-forming units (PFU)/ml.…”

Section: Materials and Methods Antigensmentioning

confidence: 99%

Antibody Response In Vitro to an Animal Virus: Production of Rabies Virus Neutralizing Antibodies by Mouse Cells in Culture

Koprowski

Mocarelli

Wiktor

1972

Proc. Natl. Acad. Sci. U.S.A.

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“…The virion is bullet-shaped and contains an unsegmented and nonpolyadenylated negative-stranded RNA genome (Sokol et al, 1969;Wagner, 1975). The transcription and replication mechanisms are thought to be similar to those of rabies virus and vesicular stomatitis virus (VSV) (Banerjee, 1987).…”

Section: Introductionmentioning

confidence: 99%

Complete Cloning and Molecular Organization of a Rabies-related Virus, Mokola Virus

Bourhy

Tordo

Lafon

et al. 1989

Journal of General Virology

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Biochemical and biophysical studies on the nucleocapsid and on the RNA of rabies virus

Cited by 89 publications

References 35 publications

Conformation of the helical nucleocapsids of paramyxoviruses and vesicular stomatitis virus: reversible coiling and uncoiling induced by changes in salt concentration.

Conformation of the helical nucleocapsids of paramyxoviruses and vesicular stomatitis virus: reversible coiling and uncoiling induced by changes in salt concentration.

Antibody Response In Vitro to an Animal Virus: Production of Rabies Virus Neutralizing Antibodies by Mouse Cells in Culture

Complete Cloning and Molecular Organization of a Rabies-related Virus, Mokola Virus

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