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Pseudotypes of vesicular stomatitis virus with the mixed coat of reticuloendotheliosis virus and vesicular stomatitis virus.

Vesicular stomatitis virus (VSV) forms pseudotypes with envelope components of reticuloendotheliosis virus (REV). The VSV pseudotype possesses the limited host range and antigenic properties of REV. Approximately 70% of the VSV, Indiana serotype, and 45% of VSV, New Jersey serotype, produced from the REV strain T-transformed chicken bone marrow cells contain mixed envelope components of both VSV and REV. VSV pseudotypes with mixed envelope antigens can be neutralized with excess amounts of either anti-VSV antiserum or anti-REV antiserum.

Antigens, Viral↗

Oligosaccharide moieties of the glycoprotein of vesicular stomatitis virus.

Vesicular stomatitis virus contains a single structural glycoprotein whose carbohydrate sequences are probably specified by the host cell. The glycopeptides derived by Pronase digestion of the glycoprotein of vesicular stomatitis virus grown in HeLa cells have an average molecular weight of 1,800. There are multiple oligosaccharide chains on the vesicular stomatitis virus glycoprotein with protein-carbohydrate linkages that are cleaved only by strong alkali under reducing conditions, suggesting that they contain asparagine and N-acetylglucosamine. The oligosaccharide moieties, in addition, appear to be heterogeneous in sequence on the basis of their mobilities during electrophoresis and their sensitivities to cleavage by an endoglycosidase. The carbohydrate-peptide linkage region of the major class of oligosaccharides of the vesicular stomatitis virus glycoprotein has the proposed sequence: (see article).

Acetylglucosamine↗

Photolabeling identifies a putative fusion domain in the envelope glycoprotein of rabies and vesicular stomatitis viruses.

Vesicular stomatitis and rabies viruses enter cells through receptor-mediated endocytosis, followed by fusion of the viral with the endosomal membrane. The latter step is catalyzed by the viral envelope glycoprotein, which, in the low pH environment of the endosome, undergoes a conformational transition to a fusion-competent state. To investigate whether fusion competence involves the low pH exposure of a hydrophobic fusion region(s), we have applied hydrophobic photolabeling using the recently developed phospholipid analogue 1-O-hexadecanoyl-2-O-[9-[[[2-[125I]iodo-4-(trifluoromethyl-3H- diazirin-3-yl)benzyl]oxy]carbonyl] nonanoyl]-sn-glycero-3-phosphocholine ([125I]TID-PC/16) (Weber, T., and Brunner, J. (1995) J. Am. Chem. Soc. 117, 3084-3095). Rosettes of rabies virus glycoprotein, whole rabies virus, or vesicular stomatitis virus were incubated with large unilamellar vesicles containing [125I]TID-PC/16. Following reagent activation, the labeled glycoprotein was isolated and analyzed. In all cases, labeling of the glycoprotein strongly increased as the pH was lowered from 7.0 to 6.0, suggesting the exposure at acidic pH of a domain capable of interacting with membranes. To identify the labeled region(s), CNBr fragments were generated and analyzed by SDS-polyacrylamide followed by autoradiography. In rabies glycoprotein, the labeled segment was found to be contained within fragment RCr5 (residues 103-179). Glycoprotein from vesicular stomatitis virus was labeled within fragment VCr1 (residues 59-221). These results demonstrate that rhabdovirus glycoprotein contains a domain that at low pH is capable of interacting with a target membrane in a hydrophobic manner. This domain may play a role similar to that of the fusion peptide found in many other viral fusion proteins.

Amino Acid Sequence↗

Isolation of the envelope of vesicular stomatitis virus.

Vesicular stomatitis virus was disrupted by a combination of freezing and thawing, osmotic shock, and sonic treatment. Subviral components were separated by isopycnic centrifugation. The low-density, lipid-rich fractions were pooled and shown to contain primarily viral glycoprotein. Further purification of this material resulted in the isolation of a preparation of vesicles which contained only the G protein and the same phospholipids as in the intact virions and exhibited spikelike structures similar to those on intact vesicular stomatitis virions. We conclude that we have isolated fragments of native vesicular stomatitis virus envelopes.

Centrifugation, Isopycnic↗

Induction of apoptotic DNA fragmentation by the infection of vesicular stomatitis virus.

Vesicular stomatitis virus (VSV) induced apoptosis of infected HeLa cells. Fragmentation of chromosomal DNA into nucleosomal oligomers as well as a characteristic nuclear fragmentation were observed in the infected cells. The kinetics of the apoptotic response was determined in relation to viral multiplication and cytopathic effect. Comparison of these kinetics revealed that the production of progeny virus occurs at almost similar kinetics to that of the DNA fragmentation, so that viral multiplication is not interrupted by the apoptotic cell damage.

Animals↗

Model for vesicular stomatitis virus.

Vesicular stomatitis virus contains single-stranded ribonucleic acid of molecular weight 3.6 x 10(6) and three major proteins with molecular weights of 75 x 10(3), 57 x 10(3), and 32.5 x 10(3). The proteins have been shown to be subunits of the surface projections, ribonucleoprotein, and matrix protein, respectively. From these values and from estimates of the proportions of the individual proteins, it has been calculated that the virus has approximately 500 surface projections, 1,100 protein units on the ribonucleoprotein strand, and 1,600 matrix protein units. Possible models of the virus are proposed in which the proteins are interrelated.

Amino Acids↗

Extreme heterogeneity in populations of vesicular stomatitis virus.

Vesicular stomatitis virus (VSV) sequence evolution and population heterogeneity were examined by T1 oligonucleotide mapping. Individual clones isolated from clonal pools of wild-type Indiana serotype VSV displayed identical T1 maps. This was observed even after one passage at high concentrations of the potent viral mutagen 5-fluorouracil. Under low-multiplicity passage conditions, the consensus T1 fingerprint of this virus remained unchanged after 523 passages. Interestingly, however, individual clones from this population (passage 523) differed significantly from each other and from consensus sequence. When virus population equilibria were disrupted by high-multiplicity passage (in which defective interfering particle interference is maximized) or passage in the presence of mutagenic levels of 5-fluorouracil, rapid consensus sequence evolution occurred and extreme population heterogeneity was observed (with some members of these population differing from others at hundreds of genome positions). A limited sampling of clones at one stage during high-multiplicity passages suggested the presence of at least several distinct master sequences, the related subpopulations of which exhibit at least transient competitive fitness within the total virus population (M. Eigen and C.K. Biebricher, p. 211-245, in E. Domingo, J.J. Holland, P. Ahlquist, ed., RNA Genetics, vol. 3, 1988). These studies further demonstrate the important role of selective pressure in determining the genetic composition of RNA virus populations. This is true under equilibrium conditions in which little consensus sequence evolution is observed owing to stabilizing selection as well as under conditions in which selective pressure is driving rapid RNA virus genome evolution.

Animals↗

Localization of membrane proteins by the use of a photoreactive fatty acid incorporated in vivo into vesicular stomatitis virus.

Vesicular stomatitis virus grown in the presence of omega-[9-3H]diazirinophenoxy nonanoate resulted in the biosynthetic incorporation of this photoreactive fatty acid into viral phospholipids as well as into the membrane anchoring domain of the viral G glycoprotein. Photolysis of the isolated virus at 360 nm resulted in extensive labeling of the G protein but none of the other proteins by the viral phospholipids. In addition, a new product was obtained and was identified as a G-G dimer by its molecular weight and its reaction with anti-G antibody. These results demonstrate the use of photoreactive fatty acid to identify integral membrane proteins and to make photoaffinity probes of fatty acylated membrane proteins.

Animals↗

Activation of mouse lymphocytes by vesicular stomatitis virus.

Vesicular stomatitis virus (VSV) is a mitogen for mouse spleen cells, and infectious virus is not required for mitogenesis. At concentrations between 10 and 100 microgram per culture, VSV stimulated DNA synthesis and blast transformation. Maximal activation by VSV occurred 48 h after culture initiation. Spleen cells depleted of T-lymphocytes by treatment with anti-Thy 1.2 and complement and those obtained from congenitally athymic BALB/c nu/nu mice were activated by VSV, suggesting that VSV is a B-cell mitogen. Activation of spleen cells was independent of the host in which the virus was grown, since VSV grown in BHK-21, HKCC, or MDBK cells was mitogenic. The mitogenesis was specific for VSV, since MDBK cell-grown WSN influenza virus was not a mitogen in this in vitro activation system, VSV-specific antibody prevented VSV mitogenesis, and VSV was mitogenic for spleen cells from C3H/HeJ mice which were resistant to mitogenesis by endotoxin.

Animals↗

Grasshoppers (Orthoptera: Acrididae) could serve as reservoirs and vectors of vesicular stomatitis virus.

Vesicular stomatitis (VS) is an economically devastating disease of livestock in the Americas. Despite strong circumstantial evidence for the role of arthropods in epizootics, no hematophagous vector explains the field evidence. Based on the spatiotemporal association of grasshopper outbreaks and VS epizootics, we investigated the potential role of these insects as vectors and reservoirs of the disease. The critical steps in the grasshopper-bovine transmission cycle were demonstrated, including 1) 62% of grasshoppers [Melanoplus sanguinipes (F.)] fed vesicular stomatitis virus (VSV) from cell culture became infected, with titers reaching 40,000 times the inoculative dose; 2) 40% of grasshoppers that cannibalized VSV-infected grasshopper cadavers became infected, amplifying virus up to 1,000-fold; 3) one of three cattle consuming VSV-infected grasshopper cadavers contracted typical VS and shed virus in saliva; and 4) 15% of grasshoppers became infected when fed saliva from this infected cow. The ecological conditions and biological processes necessary for these transmissions to occur are present throughout much of the Americas. Field studies will be required to show these findings are relevant to the natural epidemiology of VSV.

Animals↗

Ultrastructural changes in bovine lingual epithelium infected with vesicular stomatitis virus.

Vesicular stomatitis virus was inoculated into the dorsal lingual epithelium of three cows. The reaction that developed in 72 h was characterized by severe acute diffuse glossitis with intercellular edema and necrosis of keratinocytes. Virions budded from the plasma membrane and were in the intercellular spaces. Reduplication of desmosomes was a prominent alteration, and normal desmosomes were within the cytoplasm. Intracytoplasmic desmosomes appeared to be formed by endocytosis after breaks occurred in the plasma membrane of one cell; endocytosis of loops of plasma membrane containing desmosomes; and formation of desmosomes on invagination of the plasma membrane.

Animals↗

Encapsulation of lymphocyte DNA by vesicular stomatitis virus.

Vesicular stomatitis virus, grown on the WIL(2)-3A line of continuously growing human lymphocytes, contains DNA in addition to the viral RNA. By contrast, virus grown on BHK 21-C13 fibroblasts has no detectable DNA. The virus-associated DNA is found in both the B and T particles of the virus and is resistant to deoxyribonuclease. The DNA is intimately associated with the virus and appears to be incorporated into the viral ribonucleoprotein core structure produced by treatment of the virus with Nonidet P40 follow edby CsCl isopycnic banding. The virus-associated DNA has an isopycnic density of 1.699 g x cm(-) (-3) in CsCl, identical to that of human DNA. The average molecular weight of the DNA molecules associated with the virus is 9.0 x 10(5), as determined by velocity sedimentation in sucrose density gradients and studies of its contour length in the electron microscope. DNA.DNA reassociation kinetics of this DNA demonstrate that the DNA is of host origin and rules out the possibility that it originates from contaminating microorganisms or mitochondria. The analytical complexity of the virus-associated DNA shows that 50% of the virus-associated DNA sequences are homologous to the repeated DNA sequences of human DNA and the remaining 50% are homologous to human unique sequences. On the average, there is one molecule of DNA for each four virion particles.

Animals↗

Elicitation of natural killer cells in beige mice by infection with vesicular stomatitis virus.

Vesicular stomatitis virus (VSV) infection of beige (bg/bg) mice induced levels of natural killer cytolytic activity comparable to that of uninfected normal bg/+ controls, but considerably less than natural killer activity in VSV-infected bg/+ mice. In contrast, VSV-infected bg/bg and bg/+ mice had essentially equivalent amounts of anti-VSV cytotoxic T-lymphocyte and antibody activity. VSV infection induced comparable levels of interferon in both bg/bg and bg/+ mice. Therefore, the decreased natural killer activity in bg/bg mice could not be attributed to an inability to produce interferon.

Animals↗

A small highly basic protein is encoded in overlapping frame within the P gene of vesicular stomatitis virus.

Vesicular stomatitis virus (VSV) has served for several decades as the prototype rhabdovirus and a model RNA virus. Extensive studies upheld the original view of VSV genetics with simply five genes (N, P, M, G, and L), each encoding a single unique protein. We now report the first unambiguous demonstration of the existence of an additional unique protein encoded in an overlapping frame within the virus P gene. Experiments using antipeptide sera specific for the predicted second open reading frame have demonstrated the synthesis of two N-terminally nested forms of the protein in virus-infected cells. The major form is 55 amino acids in length, whereas the minor form has 10 additional N-terminal amino acids. Ribosome initiation of synthesis of these proteins appears to occur at AUG codons, 68 and 41 bases, respectively, downstream of the P protein AUG initiation codon. The proteins are found in the cytoplasm of the infected cell but are undetectable in purified virions, consistent with their being nonstructural proteins. Both the major and minor forms of the protein are highly basic and arginine rich, reminiscent of the C and C' proteins encoded in overlapping frame close to the 5' terminus of the P mRNA of several paramyxoviruses. The potential to encode small, highly basic proteins within the P mRNA 5' terminus is highly conserved among the vesiculoviruses.

Amino Acid Sequence↗

Further studies of the RNA synthesis phenotype selected during persistent infection with vesicular stomatitis virus.

Vesicular stomatitis virus (VSV) isolated from two independently established lines of persistently infected mouse L cells expressed an altered phenotype of RNA synthesis at 37 degrees, the temperature at which the persistently infected cultures were maintained (T.K. Frey and J.S. Youngner, 1982, J. Virol. 44, 167-174). In comparison to the viruses used to initiate the two lines, wild-type (wt) VSV and ts-0-23 (ts-, RNA+ complementation group III), the VSV expressing this RNA phenotype synthesized much less mRNA but equal or greater amounts of 40 S genomic RNA (rt- phenotype). In the line initiated with wt-VSV, at 17 days after initiation, when 85% of the clones were ts-, 36% of the ts- clones were rt-. By 63 days the VSV-PI population was uniformly ts- and rt- and this phenotype prevailed for at least 2 years of persistence. In the line initiated with ts-0-23, the rt- phenotype was stable for at least 3 years of persistence. To study the relationship of the ts- and rt- phenotypes which were coselected during persistence, ts+ revertants of a ts- rt- VSV-PI clone were isolated. All of the ts+ revertants expressed a wt-VSV phenotype of RNA synthesis at 37 degrees (rt+), indicating that the two phenotypic markers may be pleiotropic manifestations of the same mutation. rt-VSV inhibited host cell RNA and protein synthesis more slowly than did wt-VSV. However, rt-VSV synthesized equivalent or greater amounts of all the virus proteins, compared to wt-VSV, despite the reduced amount of mRNA transcription. The attenuated shutoff of host cell macromolecular synthesis by rt- VSV and the concomitant efficient 40 S genome replication and virus protein synthesis may in part explain the selective advantage of the rt- mutation during persistence. The rt- phenotype was not unique to persistent infection; ts- rt- mutants also evolved during serial undiluted passages of wt-VSV in L cells and one ts- rt- mutant was identified in a group of spontaneous mutants isolated from a wt-VSV stock.

Animals↗

Complete transcription by the transcriptase of vesicular stomatitis virus.

Vesicular stomatitis virus (VSV) transcriptase completely transcribes the VSV genome into messenger-size ribonucleic acid (RNA) species. The replicating complexes of template and product RNA, generated in vitro by VSV transcriptase, exhibit a mass parity between product and template molecules. Purified product RNA, after annealing to small amounts of viral RNA, rendered 92% of the viral RNA ribonuclease-resistant. It is calculated that, under optimal conditions, 60 min is required before the VSV genome is completely transcribed.

Animals↗

Direct cell-to-cell transmission of vesicular stomatitis virus.

Vesicular stomatitis virus (VSV) infection of kidney-derived, LLC-PK1 epithelial cells resulted in the budding of new viral particles into the basolateral space of the cultures. In lateral regions where cells were in close apposition, the majority of assembling viral particles in the process of budding from the producing cell had their apex already engaged in clathrin-coated pits of the neighbouring cell surface. These observations suggest that the viral envelope-plasma membrane interaction triggers the focal formation of clathrin-coated pits; they also show how VSV infection could spread throughout a tissue with only minimal exposure to a host's extracellular environment.

Animals↗

Translation and identification of the mRNA species synthesized in vitro by the virion-associated RNA polymerase of vesicular stomatitis virus.

Vesicular stomatitis virus messenger RNA has been transcribed in vitro from the viral genome by the virion-associated RNA polymerase in quantities suitable for translation. Wheat germ cell-free extracts programmed with the isolated in vitro 12-18S RNA fraction synthesize polypeptides similar to the viral N, NS, and M proteins, as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and tryptic peptide mapping of the in vitro products and the viral marker polypeptides. In addition, the RNA synthesized in vitro also codes for a protein of molecular weight 63,000 which may be a nonglycosylated form of the viral glycoprotein G. The 12-18S RNA has been partially separated into individual messenger species and these have been identified by the proteins for which they code. There are four monocistronic messenger species in the in vitro 12-18S RNA and the coding capacity of three of these molecules agrees with the estimated molecular weight of the polypeptide assigned to it.

Animals↗