- Volume 72, Issue 12, 1991
Volume 72, Issue 12, 1991
- Animal
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Copurification of Sp33–37 and Scrapie Agent from Hamster Brain Prior to Detectable Histopathology and Clinical Disease
More LessStudies were conducted to determine whether accumulation of the scrapie agent protein Sp33–37 in brain correlated with the appearance of the scrapie agent or with pathology. The concentrations of the scrapie agent and Sp33–37 were measured in purified fraction P5 isolated from hamster brains at weekly intervals after inoculation. The scrapie agent concentration in fraction P5 was approximately 10−1 LD50/g brain 1 day post-inoculation and increased to 109.4LD50/g at day 77. Sp33–37 was first detected in P5 at day 21, when the agent titre was 103.9 LD50/g. Sp33–37 concentration increased in concert with the scrapie agent concentration, although the apparent rate of increase was somewhat lower for the protein than for the agent. The histopathological evidence of disease, consisting of mild vacuolation and gliosis, was first seen at 35 days, but was not conspicuous until 49 to 56 days post-inoculation. Vacuolation and gliosis increased until termination of the experiment at day 77. Amyloid plaques were first detected at 56 days and were widespread at day 77. Clinical disease was first seen in these animals at day 66, with an average onset at day 71. Control animals inoculated with buffer alone showed some mild gliosis, but were otherwise normal. The fact that Sp33–37 purified with the scrapie agent isolated from brain 14 days prior to detectable (light microscopic) pathology supports the theory that Sp33–37 is the major structural component of the scrapie agent and not solely a product of the pathology.
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Monoclonal Antibodies to Three Structural Proteins of Avian Infectious Bronchitis Virus: Characterization of Epitopes and Antigenic Differentiation of Australian Strains
More LessTen monoclonal antibodies (MAbs) directed against three structural proteins of infectious bronchitis viruses (IBV), the peplomer (S), membrane (M) and nucleocapsid (N) proteins, were characterized and used to determine the antigenic relationship between Australian IBV strains. One MAb (MAb 5) was directed against an epitope on the S1 subunit of the peplomer, another (MAb 2) against an epitope on the M glycoprotein and eight MAbs (MAbs 1, 7, 9, 16, 24, 26, 27 and 51) were directed against seven non-overlapping epitopes on the N protein. None of the MAbs neutralized infectivity or inhibited haemagglutination of the virus. Conservation of the nine epitopes detected by these MAbs was determined in 13 serotypes of Australian IBV strains. Only epitope 5 on the S1 subunit of the peplomer was conserved in all strains. Epitope 2 on the M protein showed a high degree of conservation although this epitope was absent from four strains. None of the eight epitopes on the N proteins was conserved in all IBV strains but four epitopes (1, 16, 24 and 27) showed a high degree of conservation. Epitope 9 on the N protein was present only in IBV strains of one serotype whereas epitope 7 on the N protein distinguished vaccine viruses of serotype B from other IBV strains. The presence or absence of nine epitopes on three structural proteins differentiated IBV strains into five antigenic groups.
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Bovine Immunodeficiency Virus: Immunochemical Characterization and Serological Survey
Bovine immunodeficiency virus (BIV) was purified by isodensity centrifugation; viral activities were monitored in gradient fractions using the reverse transcriptase assay and a p26-specific monoclonal antibody ELISA. In the coincident peak fractions (density about 1.17 g/ml) proteins with M r values of 26K, 17K, 53K, 14K and 100K (with decreasing intensity) were detected by Western blotting using serum of a calf after experimental BIV infection. When 957 randomly collected cattle sera from The Netherlands were tested by indirect immunofluorescence and confirmed using Western blot and/or radioimmunoprecipitation, 1.4% appeared seropositive. Thus BIV infection is not uncommon in one European cattle population.
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Molecular and Antigenic Analyses of Serotypes 8 and 10 of Bovine Rotaviruses in Thailand
Antigenic and genomic properties of non-serotype 6 bovine rotaviruses isolated in Thailand and Japan were studied by cross-neutralization tests, nucleotide sequence determination of the VP7 gene, and RNA-RNA hybridization. Two Thai strains (61A and A44) were serologically related to a Japanese isolate KK3 which has been assigned to serotype 10. In contrast, strain A5 was found to be antigenically similar to human strain 69M with serotype 8 specificity, although strain A5 showed a one-way cross-reaction with serotype 6 strain NCDV. VP7 sequence analysis confirmed these results. High degrees of similarity in nucleotide and amino acid sequences (92.5 to 98.2% and 96.3 to 97.9%, respectively) were found among the VP7 genes of the four serotype 10 bovine strains (61A, A44, KK3 and B223). The VP7 amino acid sequence of strain A5 was similar to those of serotype 8 human strains (91.7% and 94.8% for strains B37 and 69M, respectively). In RNA-RNA hybridization experiments, a high level of overall relatedness was found among the three serotype 10 bovine strains (61A, A44 and KK3), and strains A5 and NCDV were also moderately related to the three serotype 10 viruses. All the bovine rotaviruses tested in this study, regardless of their serotype specificity, exhibited a moderate genetic-relatedness to strain 69M of serotype 8, and, to a lesser extent, to serotype 2 human rotavirus strains.
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Infection of a polarized epithelial cell line with wild-type reovirus leads to virus persistence and altered cellular function
The mechanisms and consequences of persistence of non-transforming viruses are poorly understood. Reovirus infections are usually regarded as cytocidal and infection is associated with inhibition of cellular protein and DNA synthesis. Reovirus infection of the polarized epithelial MDCK cell line is not associated with inhibition of protein synthesis, and cells become persistently infected and continue to grow without c.p.e. after infection. After several passages, virus persistence is associated with profound morphological and functional changes. The cells lose their usual cobblestone appearance and acquire a fibroblastic, undifferentiated morphology. This is associated with an inability to form tight junctions. In addition, expression of epidermal growth factor receptors and one adhesion protein is altered in the persistently infected cells. These results demonstrate that reovirus persistence will occur readily, and that infection of differentiated cells with a non-transforming virus can lead to loss of differentiation and abnormal protein expression.
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Proliferative Responses of T cells Primed Against Human Rhinovirus to other Rhinovirus Serotypes
More LessLymphocytes from mice immunized with human rhinovirus (HRV) serotypes 1A or 15 proliferated in vitro in response to HRV and the activated cells were shown to be helper T (Th) cells. Lymphocytes from mice primed with HRV-1A responded to seven of eight heterologous virus serotypes, the responses to other minor cell receptor group viruses being greater than to those belonging to the major cell receptor group. A similar bias was seen with cells from mice primed with HRV-15 in that they responded preferentially to other major receptor group viruses. This pattern of cross-serotype recognition was shown to be similar in three inbred mouse strains and was not dependent upon the major histocompatibility complex haplotype. These results have revealed that there are determinants within the viral proteins of a number of serotypes of HRV that are recognized by Th cells primed against a single HRV serotype. Thus, at the level of Th cell recognition of HRV, a cross-serotype reactivity is seen which is not reflected in the B cell antibody response to virus, which is generally highly serotype-specific.
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Further Characterization of Conditional Lethal Amber Nonsense Mutants of Vesicular Stomatitis Virus: Nucleotide Sequence Analysis
More LessConditional lethal amber nonsense mutants of vesicular stomatitis virus, Indiana serotype, classified in complementation group I (the L gene), synthesize truncated versions of the L protein. This paper reports further characterization of mutants AmbL1, AmbL2 and AmbL3 by nucleic acid sequence analysis, which was achieved by sequencing L mRNA directly using appropriate synthetic oligonucleotides. In each case a single point mutation altered a glutamine-specifying codon to an amber stop codon. The L mRNA from wild-type and revertant viruses was sequenced for comparison. Of the revertants sequenced, each had reverted by back mutation within the same codon as the original mutation. A revertant of AmbL2 reverted by a second site mutation, also within the same codon as the original mutation. These mutants may be useful for assigning functions to different parts of the L polypeptide chain.
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The Nucleotide Sequence and Deduced Amino Acid Composition of the Haemagglutinin and Fusion Proteins of the Morbillivirus Phocid Distemper Virus
More LessThe amino acid composition of the two surface proteins of the recently isolated morbillivirus phocid distemper virus (PDV) were deduced from the nucleotide sequence. The fusion (F) protein of PDV exhibited characteristics similar to those of other morbillivirus F proteins. The overall amino acid similarity with its closest homologue, canine distemper virus (CDV), was 72%. From the context of the starting codons and the requirement for a hydrophobic signal peptide, it is likely that translation of the PDV F mRNA starts at the third AUG, corresponding to codon 95 in the long open reading frame of the PDV F gene. After removal of the signal peptide, F0 starts at amino acid 105. From this position the F protein of PDV and CDV exhibit 84% amino acid similarity. The PDV haemagglutinin (H) protein showed 74% amino acid similarity with CDV H protein and highly conserved features responsible for the tertiary structure. Despite these similarities, the two H proteins show marked antigenic differences when probed with monoclonal antibodies. Earlier studies have indicated that rinderpest virus (RPV) is the prototype virus of the morbillivirus genus, from which first CDV/PDV and later measles virus (MV) evolved. From the close relationship shown in this study, it is likely that the divergence of CDV and PDV occurred after MV evolved from RPV.
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A Baculovirus Dual Expression Vector Derived from the Autographa Californica Nuclear Polyhedrosis Virus Polyhedrin and p10 Promoters: Co-expression of Two Influenza Virus Genes in Insect Cells
More LessA baculovirus transfer vector, pAcUW3, was developed to facilitate the insertion of two influenza virus genes, those encoding the haemagglutinin (HA) and neuraminidase (NA) membrane glycoproteins, into the Autographa californica nuclear polyhedrosis virus genome in a single cotransfection experiment. The NA gene was inserted in place of the polyhedrin coding sequences under the control of the polyhedrin promoter, whereas the HA gene was placed under the control of a copy of the p10 promoter at a site upstream of and in opposite orientation to the polyhedrin promoter. After infection of Spodoptera frugiperda cells with the recombinant virus, AcUW3HANA, both HA and NA were expressed in the very late phase of infection and were shown to be functional in appropriate assays. Immunofluorescence assays demonstrated their localization at the surface of infected insect cells. The expression of both foreign genes in the recombinant virus was found to be stable for at least 12 passages in cell culture.
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The DNA-binding Domain of Nuclear Factor I is Sufficient to Cooperate with the Adenovirus Type 2 DNA-binding Protein in Viral DNA Replication
More LessRecombinant baculoviruses have been constructed which express the full-length nuclear factor I (NFI) protein or a derivative of NFI that contains only the DNA-binding domain of the protein in infected insect cells. Both proteins were purified from insect cells infected with the respective baculoviruses and tested for their ability to cooperate with the adenovirus type 2 (Ad2) DNA-binding protein during virus replication. DNase I protection experiments demonstrated that the viral DNA-binding protein increased the affinity of both the full-length NFI and the DNA-binding domain of NFI for their recognition site in the Ad2 origin of DNA replication. As a consequence, the NFI-dependent increase in the efficiency of DNA replication observed upon addition of viral DNA-binding protein was the same when the full-length or DNA-binding domain derivative of NFI was added. Thus it appears that all of the activities associated with the ability of NFI to stimulate Ad2 DNA replication are located within the DNA-binding domain of the protein.
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Baculovirus Expression of the Human Papillomavirus Type 16 Capsid Proteins: Detection of L1–L2 Protein Complexes
More LessThe human papillomavirus (HPV) type 16 major capsid proteins L1 and L2 have been produced in a baculovirus expression system. Both proteins are expressed at a high level and can be readily solubilized. The L1 capsid protein migrates close to its expected M r of 60K. On the other hand L2 exhibits a much higher M r migrating at 73K, which is considerably greater than its predicted M r of 50K. The identity of both proteins has been confirmed also by Western blot analysis. Both proteins are produced in drastically reduced amounts in the presence of tunicamycin. In addition both L1 and L2 show interesting patterns of phosphorylation. L1 is phosphorylated only weakly and this appears to be quite labile, whereas L2 is very heavily phosphorylated and this, in contrast, appears to be very stable. We have also made use of a dual expression vector for co-expressing the L1 and L2 proteins within the same baculovirus-infected cell. The results obtained from this system demonstrate the presence of protein complexes forming between the two capsid proteins. These studies indicate that at least the initial events in capsid assembly of HPVs can occur in the absence of viral DNA.
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Unique Topography of DNA-protein Interactions in the Non-coding Region of Epidermodysplasia Verruciformis-associated Human Papillomaviruses
More LessThe non-coding region (NCR) of the epidermodysplasia verruciformis (EV)-associated human papillomavirus 8 (HPV-8) has been investigated for sequence-specific DNA-protein interactions with nuclear proteins from epithelial HeLa cells. Using DNase I protection analysis 18 footprints could be found within the HPV-8 NCR, covering altogether over 60% of both DNA strands. Several footprints coincided with the known binding sites of transcription factors (NF1, AP1, octamer and PEA3 consensus sequences); the other displayed no obvious similarities in this regard. The overall distribution of sequences involved in DNA-protein interactions differed clearly from the binding patterns reported for other HPVs. Parts of the two binding sites for the viral trans-activator protein E2 were shown to interact with non-E2 factors. The EV-specific NCR motifs M33, M29 and A/T box were all involved in protein binding. By comparing the footprints within the respective motifs of the closely related types HPV-8 and -19, quantitative and qualitative differences were detected for M33 and the A/T box.
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Firefly Luciferase as a Marker for Herpesvirus (pseudorabies virus) Replication in Vitro and in Vivo
More LessInsertion of reporter genes into complex viral genomes and monitoring virus replication by detecting the corresponding protein products is increasingly used in pathogenesis studies. We present here the isolation and characterization of a recombinant neurotropic alpha-herpesvirus, pseudorabies virus (PrV), which stably carries the gene encoding firefly luciferase. To express the enzyme the complete open reading frame for luciferase was fused to the promoter and first seven codons of the non-essential glycoprotein gX gene of PrV. A recombinant PrV carrying the luciferase gene inserted into the gX gene and exhibiting strong luciferase activity after infection of cultured cells was further characterized. Kinetic analyses showed that luciferase activity was detectable as early as 90 min after infection. Luciferase expression could be monitored in cell extracts in a luminometer. For facilitating plaque isolation of luciferase recombinant viruses it was also visualized in situ on sensitive film. Kinetic experiments in mice proved the suitability of luciferase as an excellent marker for following herpesvirus spread in the animal. By way of luciferase detection we show that PrV invasion of the central nervous system after intranasal infection of mice occurred independently of replication in non-neural tissues such as lung or thymus. Furthermore, comparison of isogenic luciferase recombinant PrV strains carrying intact or deleted glycoprotein gI genes showed differences in the organotropism between these two viruses.
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Evidence that Human Cytomegalovirus Assembly Protein Shares Antigenic Sites with an Uninfected Cell Membrane Protein
More LessImmunological abnormalities of an autoimmune nature often develop during acute primary human cytomegalovirus (HCMV) infection. IgM antibodies reacting with the membrane of uninfected human embryonic fibroblasts can be detected in most patients undergoing a primary HCMV infection. In this work, we have found that there is a common antigenic epitope shared by a cell membrane component of M r 60K (mp60), which is recognized by IgM in sera from patients with primary HCMV infection, and a linear determinant in the C-terminal half of the HCMV assembly protein of M r 38K (vp38), which is known to be one of the most IgM-reactive antigens of HCMV. While vp38 seems to contain other specific IgM-reactive regions, IgM reactivity to mp60 is due exclusively to this shared epitope. Furthermore, mp60 is found abundantly on the surface of human red blood cells, a possible explanation for the pathogenesis of the haemolytic anaemia that may appear during primary HCMV infection.
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Characterization of a Major Antigenic Region on gp55 of Human Cytomegalovirus
More LessA major antigenic region localized to the C-terminal part of the 55K glycoprotein of human cytomegalovirus (HCMV) was mapped using synthetic peptides. Analysis of the region with six sera from healthy anti-HCMV seropositive blood donors showed that the length of the reactive sequence varied between four and eight amino acids (aa). The shortest sequence recognized was VTSG (aa 798 to 801 of the 130K precursor protein), but most sera required the three or four residues C-terminal to this to react, giving a major site of VTSGSTKD (aa 798 to 805). Using peptides immobilized on polyethylene pins, the importance of both interior (between aa essential for the binding of an antibody) and extension spacer residues was evident. Free peptides containing the reactive sequence were prepared for use in a conventional ELISA and optimal pH conditions for coating were determined. The best results were achieved at pH 2 to 3, which is in agreement with the advantageous net charge of these peptides at this low pH. Anti-HCMV positive sera showed a sensitivity of approximately 50% for both peptides on polyethylene pins and peptides coated onto plates.
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B Cell Phenotype-dependent Expression of the Epstein-Barr Virus Nuclear Antigens EBNA-2 to EBNA-6: Studies with Somatic Cell Hybrids
The expression of the transformation-associated Epstein-Barr virus (EBV)-encoded nuclear antigens (EBNAs) 1 to 6 and membrane protein LMP-1 was studied in a series of somatic cell hybrids derived from the fusion of the EBV-transformed lymphoblastoid cell line (LCL) KR-4, and the EBV-carrying Burkitt’s lymphoma lines Daudi, P3HR-1 and Raji, with non-B cell lines of fibroblast, erythroid, myeloid and epithelial origin. Expression of EBNAs 2 to 6 was down-regulated in the hybrids in parallel with extinction of the B cell markers CD19, CD20, CD21, CD23, HLA class II, and surface or cytoplasmic immunoglobulin. LMP-1 was expressed independently of EBNA-2 in hybrids derived by the fusion of the LMP-1-positive KR-4 and P3HR-1 cell lines with epithelial and myeloid cells, respectively. LMP-1 was down-regulated in hybrids derived by the fusion of P3HR-1 with an erythroid cell line and in the hybrid between Raji and a mouse fibrosarcoma line. EBNA-1 was the only EBV antigen that was regularly expressed in the hybrids regardless of the dominating cellular phenotype. The autonomous expression of EBNA-1 suggests that its regulatory pathway is independent of phenotype-associated cellular or viral factors. In contrast, the expression of EBNAs 2 to 6 appears to require a B cell environment. EBNA-2 was shown to contribute to the regulation of LMP expression in B cells. We show that in LCL-carcinoma hybrids the dominating epithelial phenotype is permissive for LMP expression in the absence of EBNA-2.
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Epstein-Barr Virus Infection in Oral Hairy Leukoplakia: Virus Replication in the Absence of a Detectable Latent Phase
Epstein-Barr virus (EBV) infects both B lymphocytes and oropharyngeal epithelium, and it has been argued that the true reservoir of virus persistence in vivo is the self-renewing basal epithelial compartment. The identification of oral hairy leukoplakia (HL) of AIDS patients as a clinically apparent focus of EBV replication in lingual epithelium therefore provides a means of studying the EBV-epithelial cell interaction in situ. Replicative EBV DNA and productive cycle antigens are restricted to the upper, more differentiated epithelial layers in HL, and here we have applied highly sensitive in situ hybridization and immunohistological methods to examine the lower basal/suprabasal layers for evidence of latent EBV infection. We could not detect EBV DNA in these layers using an in situ DNA hybridization protocol which, on reference B cell lines, detected 1 viral genome/cell. Likewise, using sensitive in situ RNA hybridization for both the small non-polyadenylated EBER RNAs (abundant transcripts seen in all known forms of EBV latency) and the latent membrane protein (LMP) mRNA (the most abundant viral mRNA in B lymphoblastoid cell lines), the basal/suprabasal cells in HL were consistently negative; immunohistological staining with specific monoclonal antibodies also gave no evidence of latently infected LMP-positive cells. When the biopsy extracts were analysed by immunoblotting with selected human antisera, in addition to abundant productive cycle antigens, a band of constant size (66K) was observed which also reacted with immunopurified antibodies monospecific for one of the latency-associated nuclear antigens, EBNA 1; the cellular origin of this EBNA 1 could not be ascertained, but it is possible that in HL the protein is expressed during the productive cycle. The absence of demonstrable EBV latency in the basal/suprabasal cells of HL suggests that this is purely a virus replicative lesion which is sustained by continual re-infection of the maturing epithelium, not by the maturation of latently infected cells from the basal compartment.
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Cloning and Characterization of cDNA Clones Corresponding to Transcripts from the BamHI G Region of the Epstein-Barr Virus Genome and Expression of BGLF2
More LessA cDNA library was constructed from poly(A)+ RNA isolated from the iododeoxyuridine-treated P3HR1 cell line. Five cDNA clones, which hybridized with the BamHI G fragment of Epstein-Barr virus (EBV) DNA, were subcloned and sequenced. Clones G2, G3 and G4 corresponded to the BGLF2 open reading frame (ORF) of EBV (B95-8, nucleotides 126 837 to 125 866); G3 was found to contain the entire BGLF2 ORF. The predicted M r of the putative protein product of the EBV B95-8 BGLF2 ORF is 36K. Complete nucleotide sequencing of G3 revealed that there were two nucleotide changes from the reported sequence of the EBV B95-8 BGLF2 gene, but these did not alter the predicted amino acid sequence of the products. Clone G3 and a cDNA derived from it by N-terminal deletion were expressed in Escherichia coli, producing fusion proteins. Rabbit antisera against these proteins were shown to react with viral capsid antigen-expressing HR1 cells in an indirect immunofluorescence assay. In vitro transcription/translation products and fusion proteins expressed in E. coli were used to determine the presence of antibodies in sera from EBV-infected individuals. The results of immunoprecipitation and immunoblotting studies showed that the majority of EBV-seropositive individuals mount a serum antibody response to the BGLF2 ORF-encoded protein.
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Comparative Sequence Analysis of the Long Repeat Regions and Adjoining Parts of the Long Unique Regions in the Genomes of Herpes Simplex Viruses Types 1 and 2
More LessWe report the determination of the DNA sequence of the long repeat (R l ) region and adjacent parts of the long unique (U l ) region in the genome of herpes simplex virus type 2 (HSV-2) strain HG52. The DNA sequences and genetic content of the extremities of HSV-2 U l were found to be closely similar to those determined previously for HSV-1. The 5658 bp sequenced at the left end of HSV-2 U l contained coding regions for genes UL1 to UL4 plus part of UL5. The 4355 bp sequenced at the right end of U l contained coding regions for part of gene UL53, and the whole of genes UL54 to UL56. Comparison of the HSV-1 and HSV-2 UL56 sequences led to a correction in the published HSV-1 UL56 reading frame. The HSV-2 R l region, including one copy of the a sequence, was determined to be 9263 bp, with a base composition of 75.4% G+C and with many repetitive sequence elements. In HSV-2 R l , sequences were identified corresponding to HSV-1 genes encoding the immediate early IE110 (ICP0) transcriptional regulator and the ICP34.5 neurovirulence factor; the former HSV-2 gene was proposed to contain two introns, and the latter one intron. Downstream of the HSV-2 immediate early gene, the R l sequence encoding the latency-associated transcripts (LATs) was found to be dissimilar to that in HSV-1; the probable LAT promoter regions, however, showed similarities to HSV-1. Properties of the LAT sequences in both HSV-1 and HSV-2 were consistent with LATs being generated as an intron excised from a longer transcript.
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The Most Abundant Protein in Bovine Herpes 1 Virions is a Homologue of Herpes Simplex Virus Type 1 UL47
More LessThe bovine herpesvirus type 1 (BHV-1) protein VP8 is present, in large amounts, in the tegument of virions. As a preliminary step towards determining the function of VP8 and the biological relevance for its abundant presence, we describe the mapping of the location of its gene and determination of its nucleotide sequence. The gene for VP8 was located between 0.088 and 0.108 map units on the BHV-1 genome and contained a 2226 bp reading frame encoding a 742 amino acid protein. The protein, produced in vitro by transcribing and translating the reading frame, was precipitated by monoclonal antibodies and polyclonal serum directed against VP8. The primary structure of VP8 showed considerable homology with the product of the UL47 reading frame of herpes simplex virus type 1.
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