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PubMed1994

The E1 sequence of bovine adenovirus type 3 and complementation of human adenovirus type 5 E1A function in bovine cells.

The bovine adenovirus type 3 (BAV3) genome was sequenced from the left end to the HindIII site at 11%. This region comprises the entire E1 transcription unit including the open reading frames (ORF) for proteins homologous to the E1A, E1B proteins and protein IX of human adenovirus type 5 (Ad5). A portion of the BAV3 E1A protein showed significant homology with conserved region 3 (CR3), the principal transactivation region of Ad5 E1A. The BAV3 E1A protein also contains a consensus sequence known to be important for interaction with the cellular Rb protein but lacks most of the sequence corresponding to the second exon of Ad5 E1A. Promoter sequences for BAV3 E1B were not defined though the relevant region contains a 35-base pair repeat sequence. Two ORFs define the BAV3 E1B coding unit; one with regions homologous to sequences within the Ad5 E1B 19k protein, and an overlapping ORF with significant homology to the Ad5 E1B 55k protein. The encoded BAV3 E1B proteins of 157 and 420 amino acid residues (R) have predicted unmodified molecular weights of 17,393 and 46,734 respectively. Immediately following the E1B coding region there is a transcription unit containing an SP1 binding site and TATA box followed by an ORF which encodes a protein of 125R and predicted molecular weight of 13,706 with homology to protein IX of Ad5. Five concensus poly A addition sites are located in the 350 base pairs immediately following the protein IX coding region. The homology of sequences in the Ad5 E1A CR3 region and the corresponding BAV3 protein suggested that the BAV3 protein could transactivate certain Ad5 genes normally transactivated by the Ad5 E1A product. Evidence for this hypothesis was obtained in studies in which bovine cells in culture were coinfected with BAV3 and a human adenovirus type 5 (Ad5) recombinant viral vector lacking the E1A region and having a lacZ reporter gene within the E3 region dependent on E1A for its expression. Coinfection resulted in the induction of beta-galactosidase activity and the increased expression of other Ad5 early (E2A 72k) and late (hexon) proteins.

Adenoviridae↗
PubMed2004

Adenovirus type 5 pseudotyped with adenovirus type 37 fiber uses sialic acid as a cellular receptor.

For purposes of gene therapy, the tropism of adenovirus (Ad) serotype 5 vectors can be altered with fibers derived from alternative serotypes. However, there is currently limited information available on the cellular receptors used by the approximately 51 known Ad serotypes. Recently, alpha(2-->3)-linked sialic acid (2,3-SA) has been implicated as the cellular receptor for wild-type Ad37. However, some studies have demonstrated that wild-type Ad37 uses a 50-kDa protein and not sialic acid as its primary receptor for binding of human conjunctival cells. The sialic acid receptor has also been shown not to play a major role in the infection of these cells by an Ad5 virion pseudotyped with Ad37 fiber (Ad5.GFP.DeltaF/37F). In this study, we demonstrate that a similar virus (Ad5F37) can indeed use alpha(2-->3)-linked sialic acid as a cellular receptor. We also find that the receptor used by Ad5F37 is sensitive to proteases and that Ad5F37 can use integrin more efficiently than sialic acid for cell entry. Unlike Ad5 vectors, Ad5F37 does not efficiently employ the coxsackie and adenovirus receptor (CAR) to infect cells. Similar to Ad5, Ad5F37 infection of cells that form tight junctions can be enhanced by ethylenediaminetetraacetic acid (EDTA). These results have implications in the design of pseudotyped adenovirus vectors for gene therapy and may have particular use in the treatment of diseases involving breakdown of the blood-retinal barrier.

Adenoviruses, Human↗
PubMed1979

Extrapulmonary manifestations of adenovirus type 7 pneumonia simulating Reye syndrome and the possible role of an adenovirus toxin.

Three children developed extensive extrapulmonary disease in the course of fatal adenovirus type 7 pneumonia. Several clinical features, including the unexpected onset of coma, suggested the development of Reye syndrome, but biochemical and histopathologic findings were inconsistent with this diagnosis. Virologic and pathologic studies did not reveal evidence of extrapulmonary adenovirus infection, despite clinical involvement of the liver, skeletal muscle, and central nervous system. The detection in premortem sera from all three patients of adenovirus penton antigen, known to be cytotoxic in vitro, suggests a possible mechanism for the production of extrapulmonary pathology in the absence of extrapulmonary virus infection.

Adenoviridae Infections↗
PubMed2006

Adenovirus vectors based on human adenovirus type 19a have high potential for human muscle-directed gene therapy.

Until recently, adenovirus-based gene therapy has been almost exclusively based on human adenovirus serotype 5 (Ad5). The aim of this study was to systematically compare the efficiency of transduction of primary muscle cells from various species by two adenoviral vectors from subgroups C and D. Transduction of a panel of myoblasts demonstrated a striking specificity of an Ad19a-based replication-defective E1-deleted vector (Ad19aEGFP) for human cells, whereas the Ad5-based vector had high affinity for nonhuman primate myoblasts. Transgene expression correlated well with cell-associated vector genomes. Up to 6.59% of the initially applied Ad19aEGFP vector particles were taken up by human myoblasts, as compared with 0.1% of the corresponding Ad5 vector. Remarkably, Ad19aEGFP but not Ad5EGFP efficiently transduced differentiated human myotubes, an in vitro model for skeletal muscle transduction. Uptake of Ad19aEGFP vector particles in human myotubes was 12-fold more efficient than that of Ad5EGFP. Moreover, both vectors demonstrated an early block at the level of vector uptake in mouse myoblasts and rat L6 cells. Investigation of the underlying mechanism for binding and uptake of the two vectors by human myoblasts showed high susceptibility for Ad19a to neuraminidase and wheat germ agglutinin (WGA) lectin, whereas Ad5-mediated transduction was dependent on binding to the coxsackie-adenovirus receptor (CAR) and sensitive to soluble RGD peptide and heparin. Our study offers insights into species-dependent factors that determine Ad tropism and, moreover, provides a basis for application of the novel Ad19a-based vector for gene transfer into human skeletal muscle.

Adenoviruses, Human↗
PubMed1988

Nosocomial adenovirus infections: molecular epidemiology of an outbreak due to adenovirus 3a.

An immunocompromised woman died of disseminated infection due to adenovirus type 3. During her hospitalization and after her death, 38 hospital personnel developed an acute respiratory illness. Adenovirus type 3 infection was documented by culture in 18 of the 38 individuals and by seroconversion in one additional employee. Four of 34 asymptomatic hospital personnel exposed to the index case also seroconverted. Thus, 23 personnel were considered to have confirmed infections, and 22 of these 23 reported direct contact with the index case. Acquisition of infection was associated with the number and type of contacts. Protection against infection was associated with detectable serum-neutralizing antibody in the early serological sample. Restriction enzyme analysis using six different endonucleases indicated that all isolates of virus were type 3a and had identical genetic composition. This study underscores the importance of adenovirus as a cause of nosocomial infection and indicates that genetic analysis of viral DNA is a powerful tool for studying common-source outbreaks.

Adenoviridae Infections↗
PubMed1991

The amino-terminal portion of CD1 of the adenovirus E1A proteins is required to induce susceptibility to tumor necrosis factor cytolysis in adenovirus-infected mouse cells.

Previous work by our laboratory and others has shown that mouse cells normally resistant to tumor necrosis factor can be made sensitive to the cytokine by the expression of adenovirus E1A. The E1A gene can be introduced by either infection or transfection, and either of the two major E1A proteins, 289R or 243R, can induce this sensitivity. The E1A proteins are multifunctional and modular, with specific domains associated with specific functions. Here, we report that the CD1 domain of E1A is required to induce susceptibility to tumor necrosis factor cytolysis in adenovirus-infected mouse C3HA fibroblasts. Amino acids C terminal to residue 60 and N terminal to residue 36 are not necessary for this function. This conclusion is based on 51Cr-release assays for cytolysis in cells infected with adenovirus mutants with deletions in various portions of E1A. These E1A mutants are all in an H5dl309 background and therefore they lack the tumor necrosis factor protection function provided by the 14.7-kilodalton (14.7K) protein encoded by region E3. Western blot (immunoblot) analysis indicated that most of the mutant E1A proteins were stable in infected C3HA cells, although with certain large deletions the E1A proteins were unstable. The region between residues 36 and 60 is included within but does not precisely correlate with domains in E1A that have been implicated in nuclear localization, enhancer repression, cellular immortalization, cell transformation in cooperation with ras, induction of cellular DNA synthesis and proliferation, induction of DNA degradation, and binding to the 300K protein and the 105K retinoblastoma protein.

Adenovirus Early Proteins↗
PubMed1993

Deletion mutation analysis of the adenovirus type 2 E3-gp19K protein: identification of sequences within the endoplasmic reticulum lumenal domain that are required for class I antigen binding and protection from adenovirus-specific cytotoxic T lymphocytes.

Adenovirus E3-gp19K is a transmembrane glycoprotein, localized in the endoplasmic reticulum (ER), which forms a complex with major histocompatibility complex (MHC) class I antigens and retains them in the ER, thereby preventing cytolysis by cytotoxic T lymphocytes (CTL). The ER lumenal domain of gp19K, residues 1 to 107, is known to be sufficient for binding to class I antigens; the transmembrane and cytoplasmic ER retention domains are located at residues ca. 108 to 127 and 128 to 142, respectively. To identify more precisely which gp19K regions are involved in binding to class I antigens, we constructed 13 in-frame virus deletion mutants (4 to 12 amino acids deleted) in the ER lumenal domain of gp19K, and we analyzed the ability of the mutant proteins to form a complex with class I antigens, retain them in the ER, and prevent cytolysis by adenovirus-specific CTL. All mutant proteins except one (residues 102 to 107 deleted) were defective for these properties, indicating that the ability of gp19K to bind to class I antigens is highly sensitive to mutation. All mutant proteins were stable and were retained in the ER. Sequence comparisons among adenovirus serotypes reveal that the ER lumenal domain of gp19K consists of a variable region (residues 1 to 76) and a conserved region (residues 77 to 98). We show, using the mutant proteins, that the gp19K-specific monoclonal antibody Tw1.3 recognizes a noncontiguous epitope in the variable region and that disruption of the variable region by deletion destroys the epitope. The monoclonal antibody and class I antigen binding results, together with the serotype sequence comparisons, are consistent with the idea that the ER lumenal domain of gp19K has three subdomains that we have termed the ER lumenal variable domain (residues 1 to ca. 77 to 83), the ER lumenal conserved domain (residues ca. 84 to 98), and the ER lumenal spacer domain (residues 99 to 107). We suggest that the ER lumenal variable domain of gp19K has a specific tertiary structure that is important for binding to the polymorphic alpha 1 and alpha 2 domains of class I heavy (alpha) chains. We suggest that the ER lumenal conserved domain of gp19K may interact with some conserved protein, perhaps the highly conserved alpha 3 domain of class I heavy chains. Finally, the ER lumenal spacer domain may allow the ER lumenal variable and conserved domains to extend out from the ER membrane so that they can interact with class I heavy chains.

Adenoviridae↗
PubMed1983

Control of cellular gene expression during adenovirus infection: induction and shut-off of dihydrofolate reductase gene expression by adenovirus type 2.

Infection of human cells by adenovirus results in multiple alterations of host gene expression. To examine the effects of viral infection on the expression of a single gene, a line of human cells was developed which is resistant to growth in methotrexate and which contains amplified RNA and protein specific for dihydrofolate reductase (DHFR). Cytogenetic evidence indicated the presence of amplified DNA. Adenovirus infection of these cells caused an induction and subsequent decline in the synthesis of DHFR protein. The maximum DHFR induction occurred 16 to 19 h after infection and reached a level 2.5-fold greater than that observed in uninfected cells. Induction of DHFR protein synthesis was accompanied by concomitant increases in the level of steady-state DHFR-specific cytoplasmic RNA. The relative rate of DHFR mRNA production (i.e., the appearance of DHFR-specific mRNA sequences in the cytoplasm) also increased 2.5-fold during induction. Later in infection, the relative rate of DHFR protein synthesis declined, reaching a level below that observed in uninfected cells. This decline was accompanied by a similar decline in the steady-state levels of DHFR RNA and in the relative rate of synthesis of DHFR mRNA. These data suggest that adenovirus infection controls DHFR gene expression by increasing and subsequently decreasing the relative rate at which DHFR-specific mRNA sequences appear in the cytoplasm and enter the pool of mRNA available for translation.

Adenovirus Infections, Human↗
PubMed1989

Chimpanzee adenoviruses are related to four subgenera of human adenoviruses.

Nine adenovirus strains isolated from chimpanzees were studied with regard to their relatedness to each other and to human adenovirus prototypes by neutralization and hemagglutination inhibition. The strains belonged to six serotypes, and all of them were clearly related to, but not identical to human adenoviruses of subgenus A, B, C, or E respectively. DNA restriction analysis corroborated these relationships.

Adenoviridae↗
PubMedDate not supplied

[Oligopeptide analysis of the hexons of human adenovirus types 1, 2 and 6 and simian adenovirus SA7].

A comparative analysis of hexons of human adenovirus (HAdV) types 1, 2, 6 and simian adenovirus type 7 (SA7) was carried out by peptide mapping. Common and unique peptides were found in hexons from virions of human adenovirus types 2 and 6 and SA7. The similarity of hexons of HAdV types 2 and 6 was shown to be more marked than HAdV and SA7 hexons. Similar data were obtained in the analysis of excessively synthesized (soluble) hexons of HAdV types 1 and 6 and SA7. A significant homology between structural and soluble hexons of HAdV-6 HAdV-6 was established, and several peptides unique for each of them were discovered. The significance of the experimental results is discussed.

Adenoviridae↗
PubMedDate not supplied

[Isolation of cell lines transformed by highly oncogenic simian adenovirus SA7 and nononcogenic human adenovirus type 6 and their DNAs].

Methods for generation of cell lines transformed by highly oncogenic simian adenovirus SA7, nononcogenic human adenovirus type 6 and their DNAs are described. WAG rat kidney cells were used for transformation. To produce 1 focus of transformation, 1.7 X 10(6) PFU of SA7 virus is required. Intact and fragmented DNA of both viruses may be quite effectively used for transformation. For production of 1 transformation focus 1.2 microgram SA7 DNA and 1.1 microgram type 6 adenovirus DNA is required. In most cases, DNA fragmentation increases the transforming activity which has been shown to be associated with the left genome region of both viruses under study.

Adenoviridae↗
PubMed2005

Effective repetitive dystrophin gene transfer into skeletal muscle of adult mdx mice using a helper-dependent adenovirus vector expressing the coxsackievirus and adenovirus receptor (CAR) and dystrophin.

BACKGROUND: The helper-dependent adenovirus (HDAd) vector is less immunogenic and has a larger cloning capacity of up to 37 kb enough to carry the full-length dystrophin cDNA. However, high and long-term expression of dystrophin transduced to mature muscle still remains difficult. One of the main reasons for this is that the expression of the coxsackievirus and adenovirus receptor (CAR) is very low in mature muscle. METHODS: We have constructed two different HDAd vectors. One contains the LacZ and the murine full-length dystrophin expression cassette (HDAdLacZ-dys), and the other is a new, improved vector containing the CAR and the dystrophin expression cassette (HDAdCAR-dys). RESULTS: We initially demonstrated high dystrophin expression and prevention of the dystrophic pathology in mdx muscle injected during the neonatal phase with HDAdLacZ-dys. Furthermore, we demonstrated that repeated injections of HDAdCAR-dys into mature muscle led to approximately nine times greater dystrophin-positive fibers in number than a single injection, thereby recovering the expression of dystrophin-associated proteins. This data has also shown that HDAdCAR-dys enabled administration of adenovirus (Ad) vector to the host with pre-existing immunity to the same serotype of Ad. CONCLUSIONS: Repetitive injections of the HDAd vector containing the CAR and the dystrophin expression cassette could improve the efficiency of subsequent dystrophin gene transfer to mature mdx muscle. This result suggests that our new HDAd vector will provide a novel gene therapy strategy for Duchenne muscular dystrophy, raising the prospects for gene therapy of other hereditary myopathies.

Adenoviridae↗
PubMed1987

Gastroenteritis in infants, associated with a genome type of adenovirus 31 and with combined rotavirus and adenovirus 31 infection.

In an infants' ward, gastroenteritis occurred in five children in two groups, probably by nosocomial spread of adenovirus 31 (three cases) and adenovirus 31 + rotavirus (two cases). The infants recovered well. The DNA of adenovirus 31 isolates was analysed with ten restriction endonucleases and found identical for all five strains, but different from the prototype.

Adenoviruses, Human↗
PubMed1987

A new human adenovirus of subgenus D: candidate adenovirus type 42.

A new serotype, candidate adenovirus type 42, a member of subgenus D, was isolated from the feces of a healthy child. It shared its hemagglutinin with adenovirus type 15, but had no relationship in neutralization to other human adenoviruses. It also had a distinct DNA restriction pattern.

Adenoviruses, Human↗
PubMed1988

Antigenic relationship between human and animal adenovirus hexons determined by means of monoclonal antibodies directed against bovine adenovirus type 2 hexon.

Eight monoclonal antibodies (MAbs) directed against bovine adenovirus (BAV) 2 subtype B hexon were studied with 12 different hexon types of human adenoviruses (AV) belonging to 5 different subgenera using indirect ELISA, passive hemagglutination (HA), and gel diffusion assays. Two hexon types of animal origin (BAV3 and SAV16) were investigated, too. The reactivity of the MAb IV.F3 was the broadest, i.e. in ELISA and HA experiments it reacted with all hexon types studied. Based on these results as well as on the results of gel diffusion assays, this MAb should recognize the genus specific epitope of adenovirus hexons. Three MAbs (CA12, III.B11, and A12) could recognize different epitopes showing intersubgenus or intertype specificities. In spite of the fact, that all the eight MAbs proved to be bound by the hexon of ORT/111 (BAV2 subtype B) blotted onto nitrocellulose filter, four of the eight MAbs (BB7, BH5, II.A9, and IV.F5) failed to react with any human, and animal hexon types used in the present experiments. The results suggest that a gradient of antigenic relationship may exist between BAV2 hexon and the hexons of human serotypes.

Adenoviridae↗
PubMed1980

New human adenovirus (candidate adenovirus 36), a novel member of subgroup D.

A new adenovirus (candidate Ad36) was isolated from the feces of a girl with enteritis. It has been biological and biophysical properties of an adenovirus, with a particle diameter of 750 +/- 10 A in thin sections and with a fiber length of 190 A. The virus belongs to subgroup D. It is distinct both in neutralization and hemagglutination-inhibition from all other human adenoviruses; it also shows a unique DNA restriction pattern.

Adenoviruses, Human↗
PubMed1988

CTL recognition of adenovirus-transformed cells infected with influenza virus: lysis by anti-influenza CTL parallels adenovirus-12-induced suppression of class I MHC molecules.

We examined the ability of influenza-specific cytotoxic T lymphocytes to lyse adenovirus-transformed cells infected with influenza virus. Cytotoxic T lymphocyte lysis of Ad12-transformed cells was greatly reduced relative to that of Ad5-transformed cells. Lysability of adenovirus-12-transformed cells was restored in parallel with interferon-gamma induced increases in major histocompatibility complex class I gene products. These findings establish that recognition of foreign molecules by self-restricted cytotoxic T lymphocytes is reduced in adenovirus-12-transformed cells. This provides further evidence that Ad12 tumorigenicity is related to its ability to suppress class I major histocompatability complex molecule expression thereby avoiding recognition by the host immune system.

Adenoviridae Infections↗