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Volume 72,
Issue 1,
1991
Volume 72, Issue 1, 1991
- Animal
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Direct Isolation in Eggs of Influenza A (H1N1) and B Viruses with Haemagglutinins of Different Antigenic and Amino Acid Composition
More LessInfluenza A (H1N1) and influenza B viruses from clinical samples were isolated in the amniotic cavity of embryonated hens’ eggs by classical techniques and propagated in the allantoic cavity. Virus progeny from different eggs which had been inoculated with virus material from the same clinical sample possessed antigenically distinguishable haemagglutinins (HAs). Virus progeny of some eggs possessed HAs which were serologically identical to those of virus isolated in parallel in mammalian (MDCK) cells. These egg-grown viruses possessing HAs with the antigenic phenotype of mammalian cell-grown viruses appeared to be antigenically related to epidemic influenza virus because post-infection human sera reacted to high titre with the virus HA. Specific nucleotide changes were detected in the HAs of the viruses isolated directly in eggs at positions 163 and 189 for influenza A (H1Na) viruses or positions 141 and 196 to 198 for influenza B viruses. Egg-isolated viruses which possessed the antigenic phenotype of mammalian cell-grown viruses retained glycosylation sites at positions 163 and 196. The viruses isolated directly in embryonated hens’ eggs which possessed the HA antigenic phenotype and glycosylation sites of MDCK cell-grown virus can, unlike the latter viruses themselves, be used as candidate influenza vaccine viruses.
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The Specific Inhibition of Influenza A Virus Maturation by Amantadine: An Electron Microscopic Examination
More LessAmantadine specifically inhibits the release of virus particles from cells infected with the Rostock (H7N1) strain of influenza A virus, apparently as a consequence of a membrane protein M2-mediated conversion of haemagglutinin (HA) to its low pH conformation. Electron microscopic observations, together with immunogold labelling, showed that amantadine action does not alter the distribution of HA on the cell surface nor does it prevent the formation of budding virus particles. It was not possible, however, to discern whether low pH HA inhibited the final stage in virus maturation, i.e. pinching off, or simply prevented release of fully formed particles.
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Localization and Phosphorylation of Semliki Forest Virus Non-structural Protein nsP3 Expressed in COS Cells from a Cloned cDNA
More LessThe nsP3 protein of Semliki Forest virus is a phosphoprotein, which is processed from a large nonstructural polyprotein. The nsP3 gene was isolated from the large coding region by the polymerase chain reaction technique and cloned into a eukaryotic expression vector. Using the constructed pSVNS3 expression vector it was shown that nsP3 could be phosphorylated in the absence of other virus-specific proteins. This suggests that the formation of a complex with the other non-structural proteins is not required for the phosphorylation of nsP3. About half of the synthesized nsP3, in pSVN3-transfected COS cells, could be fractionated into the mitochondrial pellet fraction indicating that nsP3 is associated with large intracellular structures. Immunofluorescence microscopy of pSVNS3-transfected COS cells showed that nsP3 was found in the cytoplasm localized to vesicle-like structures. These results suggest that nsP3 contains information for specific interaction with large intracellular vesicular structures.
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Different Forms of the Bovine PrP Gene have Five or Six Copies of a Short, G-C-rich Element within the Protein-coding Exon
More LessCurrent models of the virus-like agents of scrapie and bovine spongiform encephalopathy (BSE) have to take into account that structural changes in a host-encoded protein (PrP protein) exhibit an effect on the time course of these diseases and the survival time of any man or animal exposed to these pathogens. We report here the sequence of different forms of the bovine PrP gene which contain either five or six copies of a short, G-C-rich element which encodes the octapeptide Pro-His-Gly-Gly-Gly-Trp-Gly-Gln or its longer variants Pro-Gln/His-Gly-Gly-Gly-Gly-Trp-Gly-Gln. Out of 12 cattle, we found eight animals homozygous for genes with six copies of the Gly-rich peptide (6:6), while four were heterozygous (6:5). Two confirmed cases of BSE occurred in (6:6) homozygous animals.
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- Plant
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Tomato Aspermy Virus has an Evolutionary Relationship with Other Tripartite RNA Plant Viruses
More LessThe entire RNA 3 (2214 nucleotides) of a chrysanthemum isolate of tomato aspermy virus (C-TAV) has been cloned and its sequence determined. C-TAV possesses two open reading frames which encode a 3a protein (277 amino acids) and a coat protein (229 amino acids). Computer-assisted comparisons were made between C-TAV RNA 3 and its predicted protein sequences and those of two other tripartite RNA viruses, cucumber mosaic virus (CMV) and brome mosaic virus (BMV). Results from this study suggest that a close evolutionary relationship exists between C-TAV, Q-CMV and BMV. Divergence of nucleotide and amino acid sequences between these viruses is not reflected at the level of the predicted secondary structure of the encoded proteins, where conservation is strong.
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The Genome Organization of Potato Virus M RNA
More LessThe 8534 nucleotide sequence of the genome of the carlavirus, potato virus M (PVM), has been determined. The sequence contains six large open reading frames (ORFs) and non-coding regions consisting of 75 nucleotides at the 5′ end, 70 nucleotides followed by a poly(A) tail at the 3′ end and 38 and 21 nucleotides between three large blocks of coding sequences. The ORF beginning at the first initiation codon at nucleotide 76 encodes a polypeptide of 223K which, according to its primary sequence analysis, seems to be a virus RNA replicase. The next coding block consists of three ORFs encoding polypeptides of 25K, 12K and 7K. The third block consists of two ORFs encoding polypeptides of 34K (PVM coat protein) and 11K. The 11K polypeptide contains a pattern resembling the consensus for a metal-binding nucleic acid-binding ‘finger’. The nucleotide sequence EMBL accession number is X53062.
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Nucleotide Sequence of the 3′-terminal Half of Beet Yellows Closterovirus RNA genome: Unique Arrangement of Eight Virus Genes
More LessThe sequence of 6746 nucleotides representing the 3′-proximal half of the beet yellows closterovirus (BYV) genome was determined. In the direction 5′ to 3′, the sequence was composed of eight open reading frames (ORFs) potentially encoding proteins of 6.4K (ORF2), 65K (ORF3), 64K (ORF4), 24K (ORF5), 22K (ORF6), 20K (ORF7) and 21K (ORF8). An incomplete ORF, ORF1, encoded the C-terminal part of a putative RNA-dependent RNA polymerase, most closely related to polymerases of tricornaviruses; the putative product of ORF3, 65K, was found to be a homologue of the hsp70 family of cell heat-shock proteins. ORF2 potentially encoded a small hydrophobic 6.4K protein, apparently homologous to small hydrophobic proteins of potex- and carlaviruses. ORF6 encoded the viral coat protein, as indicated by its deduced M r and amino acid composition. The products of ORFs 4, 5, 7 and 8 showed no significant similarities with protein sequences in the database and there are therefore no justifiable speculations concerning their possible functions. BYV RNA contains a 3′-terminal non-coding region of 181 nucleotides, with two stem-loop structures potentially folded within the 86 nucleotide sequence at the extreme 3′ end. Analysis of the primary and secondary structure of this region together with the absence of aminoacylation and adenylylation in vitro showed that the BYV genome is devoid of a tRNA-like structure at its 3′ end.
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Comparison and Differentiation of Potyvirus Isolates and Identification of Strain-, Virus-, Subgroup-specific and Potyvirus Group-common Epitopes Using Monoclonal Antibodies
More LessA panel of monoclonal antibodies (MAbs) generated against an admixture of 12 potyvirus isolates was used to compare and differentiate diverse potyviruses. Both native and denatured virions of strains of bean yellow mosaic (BYMV), potato virus Y, tobacco etch, pea seed-borne mosaic, iris severe mosaic, iris mild mosaic and asparagus virus-1 potyviruses were used as immunogen and as antigen for screening of the hybridoma cell lines. Thirty cell lines secreting potyvirus-specific antibodies reactive in indirect antigen-coated plate (ACP-) ELISA were selected for detailed analysis. All 30 MAbs reacted with at least one strain of BYMV; 11 MAbs reacted with between one and eight of the nine BYMV strains and an additional three MAbs reacted only with isolates within the BYMV subgroup (BYMV, pea mosaic virus and clover yellow vein virus). The remaining 16 MAbs reacted with a BYMV isolate and with at least one of the other 43 potyvirus isolates tested. MAb PTY 1 reacted with all 55 potyvirus isolates tested (representing at least 33 different and distinct aphid-transmissible potyviruses). The potyvirus cross-reactive MAbs generally gave higher reactivity values in ACP-ELISA with dissociated virus than with polyclonal antibody-trapped intact virions in triple antibody sandwich ELISA (i.e. were cryptotope-specific). The BYMV strain- and virus-specific MAbs reacted strongly with both types of antigens (i.e. were metatope-specific). At least 25 distinct epitopes (12 cryptotopes and 13 metatopes) could be identified from the MAb-antigen reactivity patterns. The distribution of these epitopes between virus isolates can be used to detect and differentiate potyviruses in infected plant extracts and to examine virus architectures. Some of these epitopes are shared by potyvirus isolates not previously shown to be serologically related. The broad spectrum-reacting MAb PTY 1 recognizes a cryptotope conserved on all of the aphid-transmissible potyviruses examined and should be a valuable tool for the detection and assay of these potyviruses.
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VPg-mediated Aggregation of Potyviral RNA
More LessRNA prepared from the potyvirus tobacco vein mottling virus contained aggregates of the 9.5 kb genomic RNA with electrophoretic mobilities corresponding to 20 and 41 kb species. Similar aggregates were present in preparations of the RNAs of two other potyviruses. Aggregation occurred during or after purification of the RNA by sucrose gradient centrifugation and alcohol precipitation and was dependent upon the presence of a protein apparently bound covalently to a region at or near the 5′ terminus of the viral RNA. This protein is probably the VPg. The RNAs of tobacco mosaic virus and cowpea mosaic virus did not form aggregates when isolated from purified virus by similar procedures.
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The Tobacco Mosaic Virus 30K Movement Protein in Transgenic Tobacco Plants is Localized to Plasmodesmata
More LessTransgenic tobacco plants expressing a gene encoding the tobacco mosaic virus (TMV) movement protein (30K) were studied using immunocytochemical techniques. The movement protein was shown to be localized within or on most of the plasmodesmata observed in the transformed plant. These results are consistent with the idea that the movement protein interacts with the plasmodesmata to facilitate the cell-to-cell spread of TMV.
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Nucleotide Sequence of RNA 2 of a Czechoslovakian Isolate of Red Clover Necrotic Mosaic Virus
More LessThe complete nucleotide sequence (1448 nucleotides) of RNA 2 of a Czechoslovakian isolate TpM-34 of red clover necrotic mosaic virus (RCNMV-TpM-34) has been determined. The sequence contained one major open reading frame (ORF) with the potential to encode a protein of 326 amino acids (Mr 35755), designated P2. The nucleotide sequence of RNA 2 of RCNMV-TpM-34 and the previously published sequence of RNA 2 of an Australian isolate of the virus (RCNMV-Aus) were 83% identical and there was 80% amino acid sequence identity between the P2 proteins of these isolates. However the N-terminal two-thirds of the P2 proteins shared a higher degree of similarity than the C-terminal regions which were predicted to have a more flexible structure. An ORF in the 3′ portion of RNA 2 of RCNMV-Aus, which could encode a protein of M r 5000, was not present in RNA 2 of RCNMV-TpM-34. RNAs 1 and 2 of RCNMV-TpM-34 and RCNMV-Aus are bilaterally compatible.
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