The organization of the proteins of vesicular stomatitis virions: Labeling with pyridoxal phosphate

Eger, Richard; Compans, Richard W.; Rifkin, Daniel B.

doi:10.1016/0042-6822(75)90233-0

Cited by 25 publications

(11 citation statements)

References 18 publications

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“…The increase seen in the smaller G-tail region was somewhat greater than expected, but this may be accounted for by small losses in the region between M and the G-tail. A small amount of M protein also is consistently labelled by isethionyl [~4C]acetimidate, in agreement with the observations of others when using external labels such as pyridoxal phosphate or lactoperoxidase-catalysed iodination (Eger et al, 1975;Moore et al, 1974).…”

Section: G Protein Spans the Virion Envelopesupporting

confidence: 77%

Structural Study of Vesicular Stomatitis Virus G Protein in the Virion Envelope

Taube

Braun

1982

Journal of General Virology

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SUMMARYSome structural properties of the vesicular stomatitis virus (VSV) G protein were examined in virions and isolated envelope fragments. We have shown that in the virion a portion of the G protein extends through the lipid envelope and that this part of the molecule can be cleaved by ehymotrypsin. Envelope fragments isolated from VSV without the use of detergents maintained the structural characteristics of the G protein found in intact virions. In addition, we provide evidence that at least some of the isolated envelope fragments have both sides of the bilayer exposed to added reagents, suggesting that this preparation would be useful for in vitro reassociation experiments.

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Section: G Protein Spans the Virion Envelopesupporting

confidence: 77%

Structural Study of Vesicular Stomatitis Virus G Protein in the Virion Envelope

Taube

Braun

1982

Journal of General Virology

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“…Where the M protein is located is not as clear. No large region of the M protein is apparently exposed on the outer surface of the virion, but the existing experiments do not eliminate the possibility of a small extracytoplasmic segment (2). It is also not known whether the M protein binds directly to the lipid membrane; the NH2-terminal region of the M protein is hydrophobic and could bind directly to the phospholipid membrane (D. Sabatini, personal communication), nor is it clear whether there is a direct interaction between parts of the M and G polypeptides.…”

Section: Resultsmentioning

confidence: 92%

“…This complex process is not well understood, but must reflect the structural organization of the viral proteins in the infected cell and in the virion. The transmembrane (5,6,13,16,20) viral glycoprotein (G protein) is imbedded in the plasma membrane; it becomes, by far, the major protein exposed on the surfaces of infected cells and on the surface of the virion (2,3,7,21). The M protein is apparently localized in the inner surface of the virus membrane and may serve as a "bridge" between the C; protein and the viral nucleocapsid, which consists of one molecule of viral RNA and the other three virus-encoded proteins, N, NS, and L (11,12,17,21,22).The VSV budding process is not totally spe-…”

mentioning

confidence: 99%

Heterogeneity of vesicular stomatitis virus particles: implications for virion assembly

Lodish¹,

Porter²

1980

J Virol

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Vesicular stomatitis virus (VSV) particles formed at early times after infection contain only one-third the amount of viral glycoprotein (G protein), relative to the major internal structural proteins M and N, as is found in particles released later. These "early" particles also have a lower density in equilibrium sucrose gradients than do those formed later; however, the sedimentation velocity and specific infectivity of these two classes of particles are the same. VSV-infected cells also release virus-like particles which sediment considerably faster than authentic virions and contain a higher-than-normal proportion of the VSV G protein relative to internal VSV proteins. These particles have a reduced specific infectivity but a normal density in sucrose gradients. All classes of VSV virions contain a constant proportion of M and N polypeptides. The ratio of G protein to M or N protein, in contrast, can vary over a sixfold range; this implies that an interaction between a precise number of surface G proteins with either of the underlying M and N proteins is not a prerequisite for budding of infectious viral particles from the cell surface.A vesicular stomatitis virus (VSV) particle, like those of most lipid-containing animal viruses, is formed by budding from the plasma membrane of an infected cell (reviewed in references 3, 11, 12, 18, and 21). This complex process is not well understood, but must reflect the structural organization of the viral proteins in the infected cell and in the virion. The transmembrane (5,6,13,16,20) viral glycoprotein (G protein) is imbedded in the plasma membrane; it becomes, by far, the major protein exposed on the surfaces of infected cells and on the surface of the virion (2,3,7,21). The M protein is apparently localized in the inner surface of the virus membrane and may serve as a "bridge" between the C; protein and the viral nucleocapsid, which consists of one molecule of viral RNA and the other three virus-encoded proteins, N, NS, and L (11,12,17,21,22).The VSV budding process is not totally spe-

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“…We conclude that some penetration of the lipids by envelope proteins is necessary to extend the bilayer. From this study, we feel that no speculation as to the degree of protein penetration is yet possible, although the M and G proteins of VSV and rabies virus penetrate but do not traverse the membrane (11,33); thus, our calculations in no way conflict with the proposed models of rhabdovirus (9, 32; Brown and Crick, in press). We have previously suggested that an important factor in rhabdovirus assembly is the time sequence of coiling of the nucleocapsid, which could be under the control of a morphopoetic factor.…”

Section: Resultsmentioning

confidence: 71%

Lipids of rabies virus and BHK-21 cell membranes

Blough¹,

Tiffany²,

Aaslestad³

1977

J Virol

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MATERIALS AND METHODS Virus strain and propagation. The Flury highegg-passage (HEP) strain of rabies virus was propagated in BHK-21 cells and concentrated by previously published methods (28), except that the maintenance medium used for virus propagation contained 0.2% (vol/vol) "fatty acid poor" bovine serum albumin (Miles Laboratories, Inc., Elkhart, Ind.) as the only protein supplement to permit unrestricted lipid synthesis (7). With this technique, as with influenza virus, there was no loss of viral infectivity or hemagglutinating activity. Virus was quantified by hemagglutination (18), and protein was measured by the Lowry method (19). 32PO43-labeled rabies virus was prepared from equilibrium-labeled BHK-21 cells to insure the complete labeling of viral phospholipids (24). BHK-21 cells were grown to con-950

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The organization of the proteins of vesicular stomatitis virions: Labeling with pyridoxal phosphate

Cited by 25 publications

References 18 publications

Structural Study of Vesicular Stomatitis Virus G Protein in the Virion Envelope

Structural Study of Vesicular Stomatitis Virus G Protein in the Virion Envelope

Heterogeneity of vesicular stomatitis virus particles: implications for virion assembly

Lipids of rabies virus and BHK-21 cell membranes

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