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At least 1,207 records · Page 67Linked to original sources
PubMed1981

Characterization of an immunosuppressive parvovirus related to the minute virus of mice.

We have characterized an immunosuppressive parvovirus related to the minute virus of mice (MVM). The parvovirus, MVM(i), grew efficiently on the murine lymphoma cell line EL-4 and not on the A-9 strain of L-cells which is a host for the prototype MVM. MVM(i) was immunosuppressive for allogeneic mixed leukocyte cultures, inhibiting the generation of cytolytic T lymphocytes. MVM had no effect on mixed leukocyte cultures. MVM and MVM(i) particles were similar in buoyant density, sedimentation rate, appearance in the electron microscope, and polypeptide composition. We present restriction enzyme maps of the DNAs of MVM and MVM(i) which show that they are closely related. Out of 109 restriction endonuclease cleavage sites (representing together about 10% of the nucleotide sequence), 86 sites were shared by MVM and MVM(i), whereas 22 sites were absent from one of the two viruses. MVM(i) DNA had an apparent deletion of about 60 nucleotides relative to MVM, located near the 5' terminus of viral DNA.

Animals↗
PubMed1982

Complementation for replicative form DNA replication of a deletion mutant of H-1 by various parvoviruses.

A defective interfering genome of the parvovirus H-1, called dl1, has been isolated and characterized. The only alteration in dl1 that has been detected is a 300-base-pair deletion at map position 38. Replicative form DNA replication of dl1 requires the RF rep function of a helper virus and the parvoviruses H-1, H-3, MVM, or MVM(i), but not LuIII complement dl1 for replicative form DNA replication.

DNA Replication↗
PubMed1983

Parvovirus genome: nucleotide sequence of H-1 and mapping of its genes by hybrid-arrested translation.

The nucleotide sequence of the parvovirus H-1 has been determined by the chain-terminating method of Sanger. The sequence is 5,176 nucleotides long. Two large open reading frames (1 and 2) and two smaller open reading frames (3 and 4) of potential importance were identified in the plus-strand sequence. Promoter sequences are located at map positions 4 and 38 when map positions are expressed as percent of genome length from the 3' end of the virion minus strand. The locations for the genes for the parvovirus capsid proteins and a 76,000-dalton noncapsid protein (NCVP1) were mapped by hybrid-arrested translation. The gene for the capsid proteins VP1 and VP2' is located in the 5' half of the virus genome. The gene for NCVP1 is located in the 3' half of the viral DNA.

Amino Acids↗
PubMed1985

Nucleotide sequence of the coat protein gene of canine parvovirus.

The nucleotide sequence of the canine parvovirus (CPV2) from map units 33 to 95 has been determined. This includes the entire coat protein gene and noncoding sequences at the 3' end of the gene, exclusive of the terminal inverted repeat. The predicted capsid protein structures are discussed and compared with those of the rodent parvoviruses H-1 and MVM.

Animals↗
PubMed1986

Parvovirus H-1 expression: mapping of the abundant cytoplasmic transcripts and identification of promoter sites and overlapping transcription units.

The 5.2-kilobase (kb) genome of the autonomous parvovirus H-1 was transcribed in the rightward direction, yielding steady-state polyadenylated transcripts of 4.8, 3.2, and 2.9 kb. Detailed mapping of these transcripts demonstrated that the H-1 genome contained two overlapping transcription units: the larger unit extended from 4 map units (5' end) to 96 map units (3' end), and the smaller unit extended from 40 map units (5' end) to 96 map units (3' end). The 4.8- and 3.2-kb transcripts were derived from the larger transcription unit and differed by a 1,500-nucleotide segment (10 to 40 map units) which was present in the 4.8-kb transcript but was spliced from the 3.2-kb transcript. The 2.9-kb transcript, the most abundant of the three known H-1 transcripts, was derived from the smaller transcription unit. The sequence at each initiation site was consistent with the presence of a class II (RNA polymerase II) promoter, and cell-free transcription of parvovirus H-1 restriction fragments containing either promoter resulted in transcription of the correct DNA strand and produced 5' ends identical to those seen in vivo. All three transcripts contained a small but heterogeneous splice at 45 to 47 map units. Minor differences in splicing at this site may result in the synthesis of different viral proteins.

DNA Restriction Enzymes↗
PubMed1986

Organization of nonstructural genes of the autonomous parvovirus minute virus of mice.

Regions of open reading frame (ORF) from the genome of the autonomous parvovirus minute virus of mice (MVM) were cloned into a procaryotic expression vector, and bacterial fusion proteins containing MVM-specific amino acid sequences were isolated. Antibodies raised against these proteins were used to immunoprecipitate viral proteins synthesized in vitro in a rabbit reticulocyte lysate translation system programmed with mRNA isolated from cells infected with MVM and a number of different parvoviruses. These studies demonstrated that: the 83-kilodalton nonstructural protein NS-1 and the 25-kilodalton nonstructural protein NS-2 have a common amino-terminal sequence which is encoded by the single ORF located between nucleotides 225 and 534 in the viral genome; the ORF located between nucleotides 1110 and 1638 is only expressed in the NS-1 protein; and the sequence encoded in a small alternative ORF between nucleotides 2075 and 2291 is expressed exclusively in NS-2. These data confirm that NS-1 is the product of the 4.8-kilobase R1 viral transcript and demonstrate that NS-2 is synthesized from the 3.3-kilobase R2 transcript which arises from the left-hand promoter at map unit 4 on the viral genome. Antibodies against the MVM fusion proteins also cross-reacted with similar proteins encoded by the viruses H-1 and LuIII, but although antibodies against the carboxy-terminal half of NS-1 cross-reacted with a similar protein in CPV, we were unable to demonstrate an NS-2 protein encoded by this virus.

Amino Acid Sequence↗
PubMed1986

A precise map of splice junctions in the mRNAs of minute virus of mice, an autonomous parvovirus.

We have determined the exact splicing patterns of the mRNAs of the minute virus of mice by a combination of cDNA sequencing and S1 nuclease protection analysis. There are four virus-specific mRNA species, each coding for one of the four polypeptides identified by in vitro translation. The R1 mRNA comprises sequences from nucleotide approximately 200 to 2281 and from 2378 to approximately 4800 and codes for the NS1 protein. The R2 mRNA is derived from nucleotides approximately 200 to 515, 1991 to 2281, and 2378 to approximately 4800 and codes for the NS2 protein. Between nucleotides 1991 and 2281, the coding sequence for NS2 overlaps that of NS1, but in a different reading frame. R3 covers nucleotides approximately 2007 to 2281 and 2378 to approximately 4800 and codes for VP2. The fourth species, R3', differs from R3 by using an alternative splice donor and acceptor in the region around 47 map units (nucleotide 2400); it extends from nucleotide approximately 2007 to 2317 and from 2400 to approximately 4800 and almost certainly codes for VP1. The R2 transcript is unusual in that the intron that was removed from it (nucleotides 516 to 1990) starts with GC rather than the canonical GU. With the exception of the splice acceptor at position 2378, which is found only in rodent parvoviruses, the splice junctions are highly conserved among autonomous parvoviruses. These results show that minute virus of mice, like other small DNA viruses, uses multiple strategies to compress the coding information for several viral proteins into a short (5,104 nucleotide) genome.

Base Sequence↗
PubMed1987

Organization and nucleotide sequence of a densovirus genome imply a host-dependent evolution of the parvoviruses.

The genome structure of a densovirus from a silkworm was determined by sequencing more than 85% of the complete genome DNA. This is the first report of the genome organization of an insect parvovirus deduced from the DNA sequence. In the viral genome, two large open reading frames designated 1 and 2 and one smaller open reading frame designated 3 were identified. The first two open reading frames shared the same strand, while the third was found in the complementary sequence. Computer analysis suggested that open reading frame 2 may encode all four structural proteins. The genome organization and a part of the nucleotide sequence were conserved among the insect densovirus, rodent parvoviruses, and a human dependovirus. These viruses may have diverged from a common ancestor.

Amino Acid Sequence↗
PubMed1988

Detailed transcription map of Aleutian mink disease parvovirus.

We studied the transcription program of Aleutian mink disease parvovirus (ADV) by using a combination of cDNA cloning and sequencing, primer extension, and Northern (RNA) blot hybridization with splice-specific oligonucleotides. The 4.8-kilobase ADV genome was transcribed in the rightward direction, yielding plus-sense polyadenylated transcripts of 4.3 (R1 RNA), 2.8 (R2), 2.8 (R3), 1.1 (RX), and 0.85 (R2') kilobases. Each RNA transcript had potential translation initiation sites within open reading frames, suggesting protein translation, and a scheme encompassing ADV structural and nonstructural proteins is proposed. Each of the five RNA transcripts had a characteristic set of splices and originated from a promoter at nucleotide 152 (map unit 3 [R1, R2, R2', and RX]) or at nucleotide 1729 (map unit 36 [R3]). The transcripts terminated with a poly(A) tail at one of two positions: either at map unit 53 (R2' and RX) or at map unit 92 (R1, R2, and R3). Similarities with and differences from the transcription maps of other parvoviruses are discussed, and possible roles of the unique features found in ADV transcription are related to the special pathogenic features of this virus.

Aleutian Mink Disease Virus↗
PubMed1988

Genomic clones of bovine parvovirus: construction and effect of deletions and terminal sequence inversions on infectivity.

Genomic clones of the autonomous parvovirus bovine parvovirus (BPV) were constructed by blunt-end ligation of reannealed virion plus and minus DNA strands into the plasmid pUC8. These clones were stable during propagation in Escherichia coli JM107. All clones tested were found to be infectious by the criteria of plaque titer and progressive cytopathic effect after transfection into bovine fetal lung cells. Sequencing of the recombinant plasmids demonstrated that all of the BPV inserts had left-end (3')-terminal deletions of up to 34 bases. DNA isolated from progeny virions arising from transfected infectious clones was found to be indistinguishable from wild-type DNA by restriction enzyme analysis. Defective genomes could also be detected in the progeny DNA even though the infection was initiated with homogenous, cloned DNA. Full-length genomic clones with 3' flip and 3' flop conformations were constructed and were found to have equal infectivity. Analysis of low-molecular-weight DNA isolated from lysates of cells transfected with these clones demonstrated that rescue and replication of BPV DNA could be detected 3 to 8 days after transfection. Expression of capsid proteins from transfected genomes was demonstrated by hemagglutination, indirect immunofluorescence, and immunoprecipitation of [35S]methionine-labeled cell lysates. Use of appropriate antiserum for immunoprecipitation showed the synthesis of BPV capsid and noncapsid proteins after transfection. Independently, a series of genomic clones with increasingly larger 3'-terminal deletions was prepared from separately subcloned 3'-terminal fragments. Transfection of these clones into bovine fetal lung cells revealed that deletions of up to 34 bases at the 3' end lowered but did not abolish infectivity, while deletions of greater than 52 bases were lethal. End-label analysis showed that the 34-base deletion was repaired to wild-type length in the progeny virus.

Amino Acid Sequence↗
PubMed1988

The two transcription units of the autonomous parvovirus minute virus of mice are transcribed in a temporal order.

Using quantitative RNase protection assays, we have monitored the appearance of mRNAs generated during lytic infection of tightly synchronized murine cells by the autonomous parvovirus minute virus of mice. Our results demonstrate that transcripts from the P4 promoter can be detected prior to those from the P39 promoter, providing direct evidence for a temporal order of expression between the two parvovirus promoters.

Animals↗
PubMed1988

Functional mapping of the genome of the B19 (human) parvovirus by in vitro translation after negative hybrid selection.

We have analyzed the coding capacity of B19 parvovirus transcripts by in vitro translation using the negative hybrid selection technique. Five different antisense oligonucleotides (18-mers) corresponding to different portions of the B19 genome were hybridized to RNA samples extracted from human erythroid bone marrow cells infected with B19 parvovirus in vitro, and RNase H was added to cleave specific B19 RNA molecules at selected sites. B19-specific translation products of these RNA samples were determined by immunoprecipitation. We localized the B19 nonstructural protein to the left-side transcript and the two capsid proteins to overlapping transcripts from the right side of the genome.

Erythroblasts↗
PubMed1988

The gene encoding the nonstructural protein of B19 (human) parvovirus may be lethal in transfected cells.

The B19 parvovirus is a cause of bone marrow failure in humans. B19 is toxic to erythroid progenitor cells in vitro. Viral products possibly responsible for toxicity were explored by transfection of cloned B19 genome into HeLa cells. The nonstructural (NS) protein was detected in cells 30 h after transfection. Plasmids containing the B19 genome were transfected with selectable marker genes in stable transformation assays. Plasmids that contained the left side of the B19 genome, which encodes the NS protein of the virus, inhibited antibiotic-resistant colony formation. Transformation occurred when NS protein expression was blocked by mutation. Suppression of transformation by NS protein was not tissue specific, suggesting a role for NS protein in toxicity for nonpermissive cells without parvovirus replication or virion accumulation.

Capsid↗
PubMed1989

A GC-box motif upstream of the B19 parvovirus unique promoter is important for in vitro transcription.

Nucleotides upstream of the B19 parvovirus P6 promoter affect in vitro transcription in HeLa cell nuclear extracts. Comparison of the relative transcriptional strengths of equimolar mixes of plasmids containing the intact upstream sequence and plasmids containing deletions within these nucleotides identified several regions that affect transcription in vitro. A fragment containing two of five GC-box motifs which correspond to high-affinity SP1-binding sites was shown, by using a gel shift assay, to bind a HeLa cell factor (or factors). DNase I, methylation interference, and methylation protection footprinting demonstrated that the HeLa cell factor(s) bound to one of the two GC-box motifs within this fragment. Mutation of this GC box abolished factor binding and significantly reduces in vitro transcription from the P6 promoter. These results suggest that the B19 parvovirus promoter includes a complex regulatory region containing multiple sequences which affect promoter strength and that the GC-box motif is a major controlling sequence for in vitro transcription.

Base Composition↗
PubMed1989

Polarized entry of canine parvovirus in an epithelial cell line.

The binding and uptake of canine parvovirus (CPV) in polarized epithelial cells were investigated by growing the cells on a permeable support and inoculating with the virus either from the apical or basolateral surface. Binding of radiolabeled CPV occurred preferentially on the basolateral surface. In contrast, when a similar experiment was carried out on nonpolarized A72 cells, virus binding occurred regardless of the direction of virus input. Binding appeared to be specific for CPV and could not be competitively inhibited by either bovine or porcine parvovirus. Analysis of the binding data revealed a high-affinity receptor (10(5) per cell) for CPV on the basolateral surfaces of MDCK cells (Kd, 29 pM). In indirect immunofluorescence studies, virus entered only from the basolateral surfaces of MDCK cells. These results provide evidence for a functional CPV-specific receptor that is expressed only on the basolateral surfaces of polarized epithelial cells, a result that has interesting consequences for viral pathogenesis.

Animals↗
PubMed1991

Replication of Aleutian mink disease parvovirus in lymphoid tissues of adult mink: involvement of follicular dendritic cells and macrophages.

By using strand-specific in situ hybridization and immunohistochemistry, evidence for replication of the Aleutian mink disease parvovirus was observed in cells resembling macrophages and cells resembling follicular dendritic cells at 10 days after infection but only in macrophages at 60 days. Sequestration of the Aleutian mink disease parvovirus in larger numbers of macrophages and follicular dendritic cells was noted at both 10 and 60 days.

Aleutian Mink Disease Virus↗
PubMed1991

Identification of the region including the epitope for a monoclonal antibody which can neutralize human parvovirus B19.

In this study, we identified a region in the human parvovirus structural protein which involves the neutralization of the virus by a monoclonal antibody and site-specific synthetic peptides. A newly established monoclonal antibody reacted with both viral capsid proteins VP1 and VP2. The epitope was found in six strains of independently isolated human parvovirus B19. The monoclonal antibody could protect colony-forming unit erythroid in human bone marrow cell culture from injury by the virus. The monoclonal antibody reacted with only 1 of 12 peptides that were synthesized according to a predicted amino acid sequence based on nucleotide sequences of the coding region for the structural protein of B19 virus. The sequence recognized by the antibody was a site corresponding to amino acids 328 to 344 from the amino-terminal portion of VP2. This evidence suggests that the epitope of the viral capsid protein is located on the surface of the virus and may be recognized by virus-neutralizing antibodies.

Amino Acid Sequence↗
PubMed1992

Canine and feline host ranges of canine parvovirus and feline panleukopenia virus: distinct host cell tropisms of each virus in vitro and in vivo.

Canine parvovirus (CPV) emerged as an apparently new virus during the mid-1970s. The origin of CPV is unknown, but a variation from feline panleukopenia virus (FPV) or another closely related parvovirus is suspected. Here we examine the in vitro and in vivo canine and feline host ranges of CPV and FPV. Examination of three canine and six feline cell lines and mitogen-stimulated canine and feline peripheral blood lymphocytes revealed that CPV replicates in both canine and feline cells, whereas FPV replicates efficiently only in feline cells. The in vivo host ranges were unexpectedly complex and distinct from the in vitro host ranges. Inoculation of dogs with FPV revealed efficient replication in the thymus and, to some degree, in the bone marrow, as shown by virus isolation, viral DNA recovery, and Southern blotting and by strand-specific in situ hybridization. FPV replication could not be demonstrated in mesenteric lymph nodes or in the small intestine, which are important target tissues in CPV infection. Although CPV replicated well in all the feline cells tested in vitro, it did not replicate in any tissue of cats after intramuscular or intravenous inoculation. These results indicate that these viruses have complex and overlapping host ranges and that distinct tissue tropisms exist in the homologous and heterologous hosts.

Animals↗