- Volume 74, Issue 3, 1993
Volume 74, Issue 3, 1993
- Animal
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Ribonucleotide reductase-deficient mutants of pseudorabies virus are avirulent for pigs and induce partial protective immunity
More LessWe have mutagenized and mapped the gene encoding the large subunit of ribonucleotide reductase (RR1) in pseudorabies virus (PRV; synonyms Aujeszky's disease virus, suid herpesvirus type 1). PRV strains carrying an oligonucleotide that leads to termination of translation of the RR1 gene are avirulent for mice. We subsequently constructed a PRV strain carrying a deletion in the RR1 gene and also a PRV strain carrying both the deletion in the RR1 gene and a deletion in the glycoprotein g1 gene, which is a marker for PRV virulence. Both PRV strains were assayed for virulence and immunogenicity in pigs, the natural host for PRV. In contrast to a marker-rescued PRV strain, these RR1-deleted mutants were avirulent, were shed in very low titres in the oropharyngeal fluid by the animals, and induced low titres of neutralizing antibodies. However, protection against clinical signs after infection with virulent PRV was induced by both RR1-deleted mutants. The relative importance of viral RR and thymidine kinase enzymes for deoxynucleotide synthesis in viral replication is discussed. In addition, we discuss the potential use of RR as a target for anti-herpesviral drugs and the use of PRV strains, deleted for the RR1 gene, as vaccine strains.
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Epstein–Barr virus (EBV) nuclear antigen 6 induces expression of the EBV latent membrane protein and an activated phenotype in Raji cells
More LessEpstein–Barr virus (EBV) nuclear antigen (EBNA) 6 (also known as 3c) is a latent nuclear protein with an M r of about 160K which is invariably expressed in EBV-immortalized B cells. It includes a putative basic leucine zipper domain; as such it is a good candidate for a regulator of viral gene expression. More than 75% of the EBNA 6 coding sequence is deleted from viral genomes carried in the Burkitt's lymphoma (BL) tumour-derived cell line, Raji. Thus although Raji cells express normal levels of the remaining five EBNAs and low levels of latent membrane protein (LMP), EBNA 6 protein is completely absent. In this study we have established Raji clones stably expressing EBNA 6 after cotransfection of an EBNA 6 gene under the control of the simian virus 40 early promoter with a selectable marker. Analysis of these clones has revealed that EBNA 6 induces a significant increase in the expression of LMP. In addition the cells have undergone a number of morphological and phenotypic changes consistent with blast-activation of normal B lymphocytes. The Raji cells expressing EBNA 6 show ruffling of the cell membrane and the development of a polarity defined by multiple villous (‘spiky’) projections at one end of the cell. This morphological change is associated with a dramatic increase in the expression of the cytoskeletal protein, vimentin. The EBV-associated B cell activation marker CD23 (blast 2) is induced to high levels although other activation markers such as CD30 and CD39 are unaffected. All these changes appear to be independent of the precise levels of EBNA 6 protein expressed. EBNA 2 has been shown previously to trans-activate the LMP gene and in the control Raji cells, EBNA 6-positive Raji cells and in B lymphoblastoid cells similar levels of EBNA 2 are expressed. Our findings are therefore most consistent with a model in which EBNA 6 either augments or complements the action of EBNA 2 in the induction of LMP and the cascade of gene expression which leads to B cell activation and immortalization by EBV.
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Construction and properties of a turkey herpesvirus recombinant expressing the Marek's disease virus homologue of glycoprotein B of herpes simplex virus
More LessA herpesvirus of turkeys (HVT) recombinant containing a 3.9 kbp fragment of Marek's disease virus (MDV) DNA encoding MDV glycoprotein B (gB), stably integrated into the thymidine kinase (TK) gene of HVT, has been constructed. The replication of the recombinant in chick embryo fibroblasts (CEF) was comparable to that of wild-type HVT. The recombinant expressed authentic MDV gB and its processed forms (110K, 65K and 48K) in CEF as shown by immunoblotting using an MDV-specific anti-peptide serum. Northern blot analysis showed that MDV gB mRNA was transcribed from MDV promoter sequences flanking the MDV gB open reading frame and also from the HVT TK promoter. However, the level of replication of the recombinant in vivo appeared to be lower than wild-type HVT as shown by the titres of HVT antibodies, determined by ELISA. Pathogenicity tests showed that the recombinant was safe and did not cause microscopic or gross Marek's disease lesions or other abnormalities. The results suggest that HVT has potential as a vector for recombinant vaccines.
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- Articles
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Biological Characterization of Structural Components of Adenovirus type 12
E. Norrby and J. AnkerstSUMMARYTwo products with a large mass and five different soluble components of adenovirus type 12 have been identified. The former were virus particles and empty capsids, which both carried group-specific complement-fixing (CF) antigen and were active as complete haemagglutinins (HAs). Their buoyant densities in CsCl were 1·330 to 1·340 and 1·295 to 1·305, respectively. The soluble components were identified as hexons, pentons, isolated fibres, dimers of fibres and isolated vertex capsomeres. Hexons were trypsin-resistant, ther-mostable and carried group-specific CF antigen; ultrastructurally they resembled hexons of other human adenoviruses. Pentons were active as an incomplete HA, causing agglutination in the presence of heterologous antisera against representative members of all three subgroups of adenoviruses. Furthermore, they were trypsin-sensitive and thermolabile. Isolated fibres represented another incomplete HA, exhibiting agglutinating activity only in the presence of antisera against members of subgroup III, e.g. type 2. This component was also identified as the dominating type-specific CF antigen. The length of fibres was estimated as 28 to 32 nm. by electron microscopy. The dimers of fibres represented a complete HA, the activity of which became apparent only after other material was removed. Both isolated fibres and their dimers were trypsin-resistant and thermostable. The assumed pentons and fibre dimers occurred in too low concentration to allow ultrastructural identi-fication. Isolated vertex capsomeres were demonstrated by a haemaggluti- nation enhancement antibody consumption test. They were completely destroyed by trypsin treatment and exhibited a moderate thermostability. Electron microscopy confirmed the presence of capsomere-like structures. These structures occasionally displayed a five-sided contour, thereby differing from hexons.
The sequence of elution of different components from an anion exchanger was: isolated vertex capsomeres, hexons + pentons, fibres and dimers of fibres. In zonal centrifugation experiments the components sedimented at decreasing rates in the following order: hexons, pentons+isolated vertex capsomeres, dimers of fibres and isolated fibres. Probably on account of the morphological characteristics of the various components they presented a different pattern of elution in exclusion chromatography. Dimers of fibres, pentons and even isolated fibres were eluted before hexons. The position of the peak activity of type 12 fibres in the elution diagram was similar to that of types 1, 2 and 5 fibres.
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- Animal
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Anti-glycoprotein B monoclonal antibody protects T cell-depleted mice against herpes simplex virus infection by inhibition of virus replication at the inoculated mucous membranes
More LessA monoclonal antibody (MAb 2c) specific for glycoprotein B of herpes simplex virus (HSV) mediated clearance of the virus from the infected mucous membranes. Young adult C57BL/6J mice were inoculated intravaginally with HSV type 1 and injected intraperitoneally either 24 and 72 h or 65 and 265 h post-inoculation with a polyclonal immune serum or the MAb 2c, both adjusted to the same neutralizing capacity. Immunization with the polyclonal immune serum did not alter the duration of virus shedding from the genital mucous membranes although a lethal outcome of infection was clearly prevented. Immunization with the MAb, however, resulted in a rapid clearance of the virus from the genital tract thus completely inhibiting genital inflammation and lethality. The same effects were achieved in mice depleted in vivo of CD4+ T cells although peripheral virus replication continued longer in these mice. In mice depleted of both CD4+ and CD8+ T cells the polyclonal immune serum was no longer able to protect against lethality, and virus replication in the mucous membranes persisted until the mice died. In contrast, after treatment with the MAb peripheral infection was quickly eliminated and all mice survived. These findings indicate that clearance of the virus from the primary site of replication can be mediated by humoral immunity. The relevance of this observation for vaccination against HSV is discussed.
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- Articles
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Depressors of Interferon Synthesis: Further Studies on the Production, Action and Properties of the So-called Enhancer
More LessSUMMARYMode of action, production and some properties of a viral growth-enhancing factor (enhancer) which was detected in allantoic fluids of eggs infected with parainfluenza type 1 virus were investigated. The factor markedly depressed interferon synthesis induced by u.v.-irradiated Newcastle disease virus in chick embryo cells, but did not inhibit the action of exogenous interferon. It had no effect on the multiplication of Newcastle disease virus in chick embryo cells. The depression of interferon synthesis by the factor was unlikely, therefore, to be due to an inhibition of the early steps of virus cell interaction. On the basis of its biological properties the factor should be termed ‘interferon depressor’. The appearance of the factor in allantoic fluids of eggs infected with parainfluenza type 1 virus could be determined by selectively destroying the interferon also contained in the materials. The activity of the factor reached a peak 24 hr after virus inoculation and remained stationary thereafter. Present data on the chemical nature of the factor are compatible with the view that it is a carbohydrate.
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- Animal
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A mutant of herpes simplex virus type 1 in which the UL13 protein kinase gene is disrupted
More LessGene UL13 of herpes simplex virus type 1 (HSV-1) has previously been proposed to encode a protein kinase. An HSV-1 mutant with UL13 inactivated by insertion of the Escherichia coli lacZ gene was constructed. This UL13-lacZ mutant was found to grow to near wild-type (wt) titres in tissue culture. Comparison of silver-stained SDS-PAGE profiles of wt and UL13-lacZ virions demonstrated that the UL13 protein is a readily detectable component of wt virions, located in the tegument and probably equivalent to the previously described species VP18.8. Studies of in vitro phosphorylation with nuclear extracts of virus-infected cells and with detergent-treated virions showed that the UL13 protein is involved in phosphorylation of the tegument protein VP22. Extracts of cells engineered to express UL13, and infected with UL13-lacZ virus, were also capable of VP22 phosphorylation.
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The herpes simplex virus type 1 US11 gene product is a phosphorylated protein found to be non-specifically associated with both ribosomal subunits
Microsequencing of a cyanogen bromide peptide obtained from a basic phosphoprotein co-sedimenting with purified ribosomes extracted from herpes simplex virus type 1-infected human epidermoid carcinoma 2 cells identified this protein as a product of the true late US11 gene. An antibody was raised against a recombinant fusion protein expressed in Escherichia coli from a plasmid carrying 75% of the US11 coding sequence including the carboxy terminus. This antibody was used to prode Western blots carried out under various conditions of one- and two-dimensional electrophoresis. The electrophoretic behaviour of the immunoreactive proteins offered further proof that they were indeed products of the US11 gene. This US11 protein, which has phosphates on multiple serine residues, is brought into the cell by the virion and found to be present within ribosome fractions early after infection. This association with ribosomes is non-specific and due to probable aggregation or oligomerization of this proline-rich basic protein allowing its co-sedimentation with ribosomes during the different subcellular fractionation steps used for the purification of ribosomal subunits.
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Trans-complementation among naturally occurring deletion mutants of hepatitis B virus and integrated viral DNA for the production of viral particles with mutant genomes in hepatoma cell lines
More LessCultured hepatoma cells (HepG2) were cotransfected with two different plasmids carrying a head-to-tail dimer of recombinant hepatitis B virus (HBV) DNA cloned from deletion mutants isolated from the circulation of persistently infected hosts. They were tested for the secretion of viral particles with mutant genome encapsidation. A recombinant plasmid defective in the S gene and one defective in both the C and P genes complemented in trans for the production of viral particles. Mutant genomes from either of the recombinants were encapsidated. Similarly, a recombinant defective in the C gene and another defective in the P gene trans-complemented for the production of viral particles containing mutant genomes. A hepatoma cell line with integrated HBV DNA sequences defective in the C and P genes (PLC/PRF/5) when transfected with a recombinant defective in the S gene produced viral particles with the HBV genome from the transfecting recombinants. These results confirm the expected trans-complementation among the S, C and P genes of HBV, when either episomal or integrated into chromosomes, for the maintenance of defective HBV mutants in persistently infected hosts.
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Characterization of new baculovirus genotypes arising from inoculation of Pieris brassicae with granulosis viruses
More LessPrevious studies have shown that of 15 Artogeia (Pieris) rapae granulosis virus isolates (ArGV1 to ArGV15) only two, ArGV1 and ArGV2, gave a normal dose-mortality response in larvae from an established colony of Pieris brassicae. We report here that at extremely high doses, approaching 10000 times the LD50 for ArGV1 and ArGV2, three other ArGV isolates caused low and irregular levels of mortality in P. brassicae. At similar doses Agrotis segetum GV caused 43% mortality in one infection, but no deaths ensued from other inoculations with this virus. Restriction endonuclease analysis of viral DNA recovered from individual larval cadavers revealed that, in most cases, progeny virus differed from the inoculum and consisted either of ArGV1 or of novel genotypes explicable as recombinants between genomes of the inoculum and of ArGV1. Field-collected P. brassicae inoculated with ArGV8 yielded a similar range of progeny genotypes. Physical maps were constructed for two such recombinants, based on comparative restriction analysis with reference to the published map of ArGV1 and to those of ArGV5 and ArGV8, which are presented. Replication of the inoculum genotype was observed in only two infections. The origin of ArGV1 DNA appearing among progeny from these infections and the relevance of our results to identifying ArGV DNA sequences that modulate pathogenicity for P. brassicae are discussed.
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Evolution of structural proteins of feline immunodeficiency virus: molecular epidemiology and evidence of selection for change
More LessThe DNA sequences of structural genes of several U.K. and European isolates of feline immunodeficiency virus (FIV) were determined and compared with those of other worldwide isolates. Phylogenetic analyses of both gag and env sequences demonstrate that a Japanese isolate represents a distinct sequence subgroup, with corrected amino acid distances to the other isolates averaging 23% in env and 8% in gag. Analysis also reveals that an evolutionary radiation of FIV occurred with many isolates diverging at approximately the same time, and that although isolates from similar geographical sources often cluster together, there is evidence of more than one origin for FIV in the U.K., The Netherlands and Italy. Estimation of the numbers of silent and replacement nucleotide substitutions indicates the presence of constraints against amino acid changes in gag and conserved regions of env but suggests that positive selection for protein sequence changes operates in variable regions of env. The possible immunological forces underlying these changes are discussed.
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Molecular characterization of two isolates of human T cell leukaemia virus type II from Italian drug abusers and comparison of genome structure with other isolates
The human T cell leukaemia virus type II (HTLV-II), whose pathogenicity is as yet unclear, was recently found to be associated with intravenous drug abuse in North America and Europe. HTLV-II was isolated from two Italian drug abusers belonging to the same cohort and coinfected with human immunodeficiency virus type 1. Two new isolates, HTLV-II Gu and Va, were established in a culture of BJAB cells, a continuous B cell line (Epstein–Barr virus-negative), and characterized by nucleotide sequence analysis of the long terminal repeat (LTR) and portions of the gag, env and X regions. These sequences were compared to those of the HTLV-II Mo isolate reported in the literature. No major variations were observed in important regulatory elements of LTR nor in the stem-bulge-loop configuration known to be essential for binding of rex protein. The results obtained from the sequence of the 1988 nucleotides examined indicated a 1.6% variability between the Gu and Va isolates and about 6% with respect to Mo. Notable differences were found in the structure of putative open reading frames of the X region when compared to those reported for the Mo isolate. Restriction analysis of proviral DNA of two isolates and comparison with the physical map of the Mo isolate confirmed the existence of genetic heterogeneity in the HTLV-II group and demonstrated that the new isolates Gu and Va belong to the HTLV-IIb subtype. The results of this study show that the new isolates have distinct features with respect to the Mo isolate though all important regulatory elements of the LTR appear to be well conserved.
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Mapping cell-mediated immunodominant domains of the rubella virus structural proteins using recombinant proteins and synthetic peptides
More LessAlthough it is known that rubella-immune individuals have T cells that proliferate in vitro in response to rubella virus (RV), the determinants that evoke this response have not been identified. This study utilized recombinant proteins that express overlapping sequences of the RV structural open reading frame to identify domains of the structural proteins that contain cell-mediated immunodominant sequences. Lysates enriched with RV fusion proteins (RecA-RV-LacZ) were prepared from Escherichia coli transformed with plasmids which contained specific RV cDNA inserts. Approximately 62% of RV-immune individuals gave RV-specific responses to one or more of the RV fusion proteins. Over 10% of immune individuals recognized the capsid sequence C1-C29. Lymphoproliferation data from studies using six overlapping synthetic peptides representing this sequence suggested that as much as 70% of the immune population may recognize this domain. An E1 sequence, E1202-E1283, was recognized by 15% of the RV-immune individuals with the fusion proteins. Five synthetic peptides representing this sequence had an overall response rate of 50%. The sequence C64-C97 failed to evoke any RV-specific responses with the fusion proteins and synthetic peptides representing this sequence were used to verify that the RV fusion proteins and the criteria used to identify RV-specific responses were adequate. These peptides gave a response rate of only 6%. In general, significant responses to specific fusion proteins correlated with high responses (stimulation index ≥ 4.0) to representative synthetic peptides. This study suggests that the recombinant proteins were beneficial in identifying cell-mediated immunodominant domains of the RV structural proteins which could be further characterized with synthetic peptides.
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Expression of the G glycoprotein gene of human respiratory syncytial virus in Salmonella typhimurium
The attachment protein, G, of human respiratory syncytial virus (RSV) is an M r 84K to 90K species which has a high content of N-linked and O-linked carbohydrates. The unglycosylated form of this protein was expressed by inserting a full-length cDNA copy of the mRNA from the A2 strain of RSV into a prokaryotic expression vector under the control of the lambda PL promoter. Salmonella typhimurium cells transformed with the G-containing plasmid synthesized a protein of M r 40000 that specifically reacted with polyclonal and two neutralizing monoclonal antibodies raised against the native RSV G glycoprotein. Recombinant G protein was purified by immunoaffinity chromatography using a neutralizing monoclonal antibody. Cotton rats immunized with the recombinant G protein produced serum antibodies to the G glycoprotein that neutralized RSV in vitro. The study demonstrates that the G protein of RSV can be expressed in bacteria and that at least one neutralizing epitope is not structurally dependent on carbohydrates.
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Comparison of soluble and secreted forms of human parainfluenza virus type 3 glycoproteins expressed from mammalian and insect cells as subunit vaccines
Human parainfluenza virus type 3 (PIV-3) is one of the leading causes of paediatric viral respiratory disease. The PIV-3 genome encodes two envelope glycoproteins, F and HN, which are the major targets for the host antibody response. We have expressed secreted forms of the F and HN proteins and a novel chimeric FHN glycoprotein in insect cells using recombinant baculovirus vectors and secreted forms of the F and FHN glycoproteins in stably transformed Chinese hamster ovary (CHO) cells. Comparison of the mammalian cell- and insect cell-expressed F and FHN proteins by SDS-PAGE showed that the CHO cell-expressed proteins are several kilodaltons larger in size than the baculovirus-produced proteins. A partial characterization of the oligosaccharide structures of the F and FHN proteins revealed that the size difference is due to the different oligosaccharide structures added to these proteins by the two cell lines. The F, HN and FHN proteins were immunoaffinity-purified from the culture medium of baculovirus-infected Sf9 cells and the F and FHN proteins were immunoaffinity-purified from the culture medium of CHO cells. A comparison of the immunogenicity and efficacy of the mammalian cell- and insect cell-produced FHN proteins was tested in cotton rats. The CHO cell- and baculovirus-produced FHN proteins were found to induce similar levels of PIV-3-specific ELISA-positive and neutralizing antibodies and both proteins provided near complete protection when animals were vaccinated with low doses of the FHN protein.
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Protection of cotton rats against human parainfluenza virus type 3 by vaccination with a chimeric FHN subunit glycoprotein
More LessA cotton rat model of experimental human parainfluenza virus type 3 (PIV-3) infection was used to examine the efficacy of FHN, a novel chimeric glycoprotein which contains the extracellular regions of the fusion (F) and haemagglutinin—neuraminidase (HN) glycoproteins of PIV-3. The FHN protein was expressed in insect cells using a baculovirus vector system. FHN vaccination resulted in induction of neutralizing antibodies, was completely protective at doses of 100 ng, and was superior to vaccination with secreted forms F and HN proteins, or mixtures of the F and HN glycoproteins. In addition, FHN immunization induced lymphoproliferative responses in mice which were directed against both the F and HN glycoproteins. Fusion of the F and HN proteins into a single chimeric glycoprotein appeared to enhance the protective immune response compared to that elicited by the individual glycoproteins or mixtures of the two glycoproteins.
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Expression of the HN, F, NP and M proteins of Sendai virus by recombinant vaccinia viruses and their contribution to protective immunity against Sendai virus infections in mice
Recombinant vaccinia viruses (RVVs) expressing each of the haemagglutinin—neuraminidase (HN), fusion (F), nucleocapsid (NP) and matrix (M) proteins of Sendai virus were constructed to investigate their capacities to induce protective immunity against Sendai virus infections. The proteins expressed in cultured cells appeared to be authentic with respect to their antigenicity, electrophoretic mobility, surface expression of the HN and F proteins and, in the case of the HN protein, biological activities. Mice inoculated intranasally with these RVVs developed serum antibodies to the respective Sendai virus proteins, suggesting their in vivo expression. In mice immunized with RVV carrying either the HN or the F gene, growth of the challenging Sendai virus was almost completely suppressed in the lung, indicating their capacities to induce effective protective immunity against Sendai virus infections. In contrast, in mice immunized with RVV carrying the NP or M gene, the challenging virus propagated as well as in the control mice, but the virus titres were significantly lower at the late stage of infection than those in the control mice, suggesting that they can also induce protective immunity especially at the late stage of the challenge infection.
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The structure of the 5′ terminal cap of the respiratory syncytial virus mRNA
More LessThe 5′ terminal cap structure of the mRNAs of human respiratory syncytial virus synthesized in vitro in the presence of S-adenosyl-l-methionine consists of a 7-methyl guanosine linked to an unmethylated guanosine through a 5′-5′ pyrophosphate linkage formed by using the α and β phosphates of GTP. The complete cap structure is m7G (5′)ppp(5′)Gp… which is devoid of ribose 2′-O-methylation. Capping, including methylation, is coupled to transcription. These results constitute the first report of a pneumoviral mRNA cap structure.
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Induction of neutralizing antibodies by varicella-zoster virus gpII glycoprotein expressed from recombinant vaccinia virus
More LessThe gpII glycoprotein of varicella-zoster virus (VZV) was produced in CV1 cells via vaccinia virus recombinants. Two different DNA constructs were expressed: the first one encodes the complete gpII protein (gpII s+a+) and the second a truncated species lacking the membrane anchorage domain (gpII s+a-). To achieve expression both coding sequences had to be engineered at the 5′ end by substituting the unusually short (24 bp) natural signal sequence by a more conventional one encoding 29 amino acids. Recombinant gpII proteins were detected in vaccinia virus-infected cells by ELISA and immunoprecipitation. Both forms of recombinant gpII proteins were produced as glycosylated single-chain molecules of respectively 110K and 90K. Upon reduction these were only partially converted into subunits. A rabbit infected with the vaccinia virus recombinant expressing the complete gpII produced antibodies which recognized VZV antigens and neutralized VZV infectivity in vitro, independent of complement.
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The glycoprotein B homologue of human herpesvirus 6
More LessThe gene for the homologue of herpesvirus glycoprotein B (gB) has been identified in the genome of human herpesvirus 6 (HHV-6), strain U1102, and the nucleotide sequence was determined. The open reading frame encodes a protein of 830 amino acids (93.2K) with the characteristics of a transmembrane glycoprotein and close similarity to the gp58/116 complex of human cytomegalovirus (HCMV). Monoclonal antibodies 2D10 and 2B9 have been shown previously to react with an HHV-6 glycoprotein of apparent M r 112K, and its proteolytic cleavage products of M r 64K and 58K. We show that both monoclonal antibodies detect prokaryotically expressed carboxy-terminal fragments of the HHV-6 gB homologue. This indicates that the HHV-6 gB homologue is probably processed by proteolytic cleavage similar to its equivalents in HCMV and various other herpesviruses.
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