scholarly journals CD46 Is a Cellular Receptor for All Species B Adenoviruses except Types 3 and 7

2005 ◽  
Vol 79 (22) ◽  
pp. 14429-14436 ◽  
Author(s):  
Marko Marttila ◽  
David Persson ◽  
Dan Gustafsson ◽  
M. Kathryn Liszewski ◽  
John P. Atkinson ◽  
...  
Keyword(s):  
Chinese Hamster Ovary Cells ◽  
Rabbit Antiserum ◽  
Chinese Hamster ◽  
A549 Cells ◽  
Adenovirus Type ◽  
Host Cells ◽  
Cellular Receptor ◽  
Coxsackie Adenovirus Receptor ◽  
Tract Infections ◽  
Adenovirus Receptor

ABSTRACT The 51 human adenovirus serotypes are divided into six species (A to F). Adenovirus serotypes from all species except species B utilize the coxsackie-adenovirus receptor for attachment to host cells in vitro. Species B adenoviruses primarily cause ocular and respiratory tract infections, but certain serotypes are also associated with renal disease. We have previously demonstrated that adenovirus type 11 (species B) uses CD46 (membrane cofactor protein) as a cellular receptor instead of the coxsackie-adenovirus receptor (A. Segerman et al., J. Virol. 77:9183-9191, 2003). In the present study, we found that transfection with human CD46 cDNA rendered poorly permissive Chinese hamster ovary cells more permissive to infection by all species B adenovirus serotypes except adenovirus types 3 and 7. Moreover, rabbit antiserum against human CD46 blocked or efficiently inhibited all species B serotypes except adenovirus types 3 and 7 from infecting human A549 cells. We also sequenced the gene encoding the fiber protein of adenovirus type 50 (species B) and compared it with the corresponding amino acid sequences from selected serotypes, including all other serotypes of species B. From the results obtained, we conclude that CD46 is a major cellular receptor on A549 cells for all species B adenoviruses except types 3 and 7.

scholarly journals Adenovirus Type 11 Uses CD46 as a Cellular Receptor

2003 ◽  
Vol 77 (17) ◽  
pp. 9183-9191 ◽  
Author(s):  
Anna Segerman ◽  
John P. Atkinson ◽  
Marko Marttila ◽  
Veronica Dennerquist ◽  
Göran Wadell ◽  
...  
Keyword(s):  
Cho Cells ◽  
Chinese Hamster ◽  
Human Adenovirus ◽  
Adenovirus Type ◽  
Host Cells ◽  
Cellular Receptor ◽  
Transfected Cells ◽  
Coxsackie Adenovirus Receptor ◽  
Adenovirus Receptor

ABSTRACT The 51 human adenovirus serotypes are divided into six species (A to F). Many adenoviruses use the coxsackie-adenovirus receptor (CAR) for attachment to host cells in vitro. Species B adenoviruses do not compete with CAR-binding serotypes for binding to host cells, and it has been suggested that species B adenoviruses use a receptor other than CAR. Species B adenoviruses mainly cause disease in the respiratory tract, the eyes, and in the urinary tract. Here we demonstrate that adenovirus type 11 (Ad11; of species B) binds to Chinese hamster ovary (CHO) cells transfected with CD46 (membrane cofactor protein)-cDNA at least 10 times more strongly than to CHO cells transfected with cDNAs encoding CAR or CD55 (decay accelerating factor). Nonpermissive CHO cells were rendered permissive to Ad11 infection upon transfection with CD46-cDNA. Soluble Ad11 fiber knob but not Ad7 or Ad5 knob inhibited binding of Ad11 virions to CD46-transfected cells, and anti-CD46 antibodies inhibited both binding of and infection by Ad11. From these results we conclude that CD46 is a cellular receptor for Ad11.

The endosomal epsilon-coatomer protein is involved in human adenovirus type 5 internalisation

2002 ◽  
Vol 50 (4) ◽  
pp. 481-489 ◽  
Author(s):  
Cs. Jeney ◽  
Boglárka Banizs ◽  
Orsolya Dobay ◽  
Keyword(s):  
Chinese Hamster ◽  
Human Adenovirus ◽  
Adenovirus Type ◽  
Inhibitory Effect ◽  
Bafilomycin A1 ◽  
Cho Cell ◽  
Coxsackie Adenovirus Receptor ◽  
Downstream Effector ◽  
Adenovirus Receptor ◽  
Adenovirus Type 5

The effects of bafilomycin A1 and of the reduced level of endosomal epsilon-COP (coatomer protein) on the infectivity of human adenovirus type 5 were investigated in Coxsackie adenovirus receptor- (CAR-) transfected Chinese hamster ovary (CHO) cells. The endosomal proton pump inhibitor bafilomycin A1 was able to cause only partial inhibition. Using ldlF cells (an epsilon-COP thermosensitive mutant CHO cell line) the reduction of epsilon-COP level also had partial inhibitory effect. Based on these results and comparing them to existing models of the adenovirus entry, we propose a refined model in which there are two pathways of adenoviral entry: the first one involves the epsilon-COP as the downstream effector of the acidification and can be blocked by bafilomycin A1 and the second one is a pH-independent pathway.

scholarly journals The Arg279Glu Substitution in the Adenovirus Type 11p (Ad11p) Fiber Knob Abolishes EDTA-Resistant Binding to A549 and CHO-CD46 Cells, Converting the Phenotype to That of Ad7p

2006 ◽  
Vol 80 (4) ◽  
pp. 1897-1905 ◽  
Author(s):  
Dan J. Gustafsson ◽  
Anna Segerman ◽  
Kristina Lindman ◽  
Ya-Fang Mei ◽  
Göran Wadell
Keyword(s):  
Amino Acid ◽  
Adenovirus Type ◽  
Cell Interaction ◽  
Amino Acid Identity ◽  
Host Cells ◽  
Single Amino Acid ◽  
Receptor Interaction ◽  
Coxsackie Adenovirus Receptor ◽  
Cellular Attachment ◽  
Adenovirus Receptor

ABSTRACT The major determinant of adenovirus (Ad) attachment to host cells is the C-terminal knob domain of the trimeric fiber protein. Ad type 11p (Ad11p; species B2) in contrast to Ad7p (species B1) utilizes at least two different cellular attachment receptors, designated sBAR (species B adenovirus receptor) and sB2AR (species B2 adenovirus receptor). CD46 has recently been identified as one of the Ad11p attachment receptors. However, CD46 did not seem to constitute a functional receptor for Ad7p. Although Ad7p shares high knob amino acid identity with Ad11p, Ad7p is deficient in binding to both sB2AR and CD46. To determine what regions of the Ad11p fiber knob are necessary for sB2AR-CD46 interaction, we constructed recombinant fiber knobs (rFK) with Ad11p/Ad7p chimeras and Ad11p sequences having a single amino acid substitution from Ad7p. Binding of the constructs to A549 and CHO-CD46 BC1 isoform-expressing cells was analyzed by flow cytometry. Our results indicate that an Arg279Glu substitution is sufficient to convert the Ad11p receptor-interaction phenotype to that of Ad7p and abolish sB2AR and CD46 interaction. Also a Glu279Arg substitution in Ad7p rFKs increases CD46 binding. Thus, the lateral HI loop of the Ad11p fiber knob seems to be the key determinant for Ad11p sB2AR-CD46 interaction. This result is comparable to another non-coxsackie-adenovirus receptor binding Ad (Ad37p), where substitution of one amino acid abolishes virus-cell interaction. In conjunction with previous results, our findings also strongly suggest that sB2AR is equivalent to CD46.

scholarly journals Initial Interactions of Subgenus D Adenoviruses with A549 Cellular Receptors: Sialic Acid versus αvIntegrins

2000 ◽  
Vol 74 (16) ◽  
pp. 7691-7693 ◽  
Author(s):  
Niklas Arnberg ◽  
Alistair H. Kidd ◽  
Karin Edlund ◽  
Farzad Olfat ◽  
Göran Wadell
Keyword(s):  
Sialic Acid ◽  
Adenovirus Type ◽  
Target Cells ◽  
Cellular Receptor ◽  
Cellular Receptors ◽  
Coxsackie Adenovirus Receptor ◽  
Acid Versus ◽  
Adenovirus Receptor

ABSTRACT Selected members of the adenovirus family have been shown to interact with the coxsackie adenovirus receptor, αvintegrins, and sialic acid on target cells. Initial interactions of subgenus D adenoviruses with target cells have until now been poorly characterized. Here, we demonstrate that adenovirus type 8 (Ad8), Ad19a, and Ad37 use sialic acid as a functional cellular receptor, whereas the Ad9 and Ad19 prototypes do not.

scholarly journals Chinese hamster ovary cells replicate adenovirus deoxyribonucleic acid.

1981 ◽  
Vol 1 (3) ◽  
pp. 208-215 ◽  
Author(s):  
M Longiaru ◽  
M S Horwitz
Keyword(s):  
Dna Synthesis ◽  
Chinese Hamster Ovary ◽  
Cho Cells ◽  
Deoxyribonucleic Acid ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Adenovirus Type ◽  
Viral Dna ◽  
Nuclear Extracts

Chinese hamster ovary (CHO) cells infected with adenovirus type 2 (Ad2) produced amounts of viral deoxyribonucleic acid (DNA) equal to that synthesized in permissively infected HeLa cells. However, there was 6,000-fold less virion produced in CHO cells. Since the structural viral polypeptides were not detected by pulse-labeling CHO cells at various times postinfection, the block in virion formation is located between the synthesis of viral DNA and late proteins. Extracts of CHO cells could also function in a recently reported in vitro Ad2 DNA synthesis system which is dependent upon the addition of exogenous Ad2 DNA covalently linked to a 5'-terminal protein (Ikeda et al., Proc. Natl. Acad. Sci. U.S.A. 77:5827-5831, 1980). Extracts of infected CHO cytoplasm were able to complement uninfected CHO nuclear extracts to synthesize viral DNA on Ad2 templates. This in vitro replication system has the potential to probe host DNA synthesis requirements as well as viral factors.

scholarly journals Use of Chinese hamster ovary cells with altered glycosylation patterns to define the carbohydrate specificity of Entamoeba histolytica adhesion.

1988 ◽  
Vol 167 (5) ◽  
pp. 1725-1730 ◽  
Author(s):  
E Li ◽  
A Becker ◽  
S L Stanley
Keyword(s):  
Entamoeba Histolytica ◽  
Chinese Hamster Ovary ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Cellular Receptor ◽  
Carbohydrate Specificity ◽  
Complex Type ◽  
Ovary Cells ◽  
Altered Glycosylation ◽  
Inhibition Studies

We compared the adherence of E. histolytica trophozoites with a panel of lectin-resistant CHO mutants with altered glycosylation patterns. Our results coupled with data from saccharide inhibition studies indicate that terminal N-acetyllactosamine units on Asn-linked complex type oligosaccharides provide the major determinants on the cellular receptor for E. histolytica adhesion.

scholarly journals Junctional Adhesion Molecule A Serves as a Receptor for Prototype and Field-Isolate Strains of Mammalian Reovirus

2005 ◽  
Vol 79 (13) ◽  
pp. 7967-7978 ◽  
Author(s):  
Jacquelyn A. Campbell ◽  
Pierre Schelling ◽  
J. Denise Wetzel ◽  
Elizabeth M. Johnson ◽  
J. Craig Forrest ◽  
...  
Keyword(s):  
Adhesion Molecule ◽  
Chinese Hamster Ovary Cells ◽  
Field Isolate ◽  
Gene Segment ◽  
Chinese Hamster ◽  
Amino Acid Sequences ◽  
Host Cells ◽  
Ovary Cells ◽  
Viral Attachment ◽  
Type 3

ABSTRACT Reovirus infections are initiated by the binding of viral attachment protein σ1 to receptors on the surface of host cells. The σ1 protein is an elongated fiber comprised of an N-terminal tail that inserts into the virion and a C-terminal head that extends from the virion surface. The prototype reovirus strains type 1 Lang/53 (T1L/53) and type 3 Dearing/55 (T3D/55) use junctional adhesion molecule A (JAM-A) as a receptor. The C-terminal half of the T3D/55 σ1 protein interacts directly with JAM-A, but the determinants of receptor-binding specificity have not been identified. In this study, we investigated whether JAM-A also mediates the attachment of the prototype reovirus strain type 2 Jones/55 (T2J/55) and a panel of field-isolate strains representing each of the three serotypes. Antibodies specific for JAM-A were capable of inhibiting infections of HeLa cells by T1L/53, T2J/55, and T3D/55, demonstrating that strains of all three serotypes use JAM-A as a receptor. To corroborate these findings, we introduced JAM-A or the structurally related JAM family members JAM-B and JAM-C into Chinese hamster ovary cells, which are poorly permissive for reovirus infection. Both prototype and field-isolate reovirus strains were capable of infecting cells transfected with JAM-A but not those transfected with JAM-B or JAM-C. A sequence analysis of the σ1-encoding S1 gene segment of the strains chosen for study revealed little conservation in the deduced σ1 amino acid sequences among the three serotypes. This contrasts markedly with the observed sequence variability within each serotype, which is confined to a small number of amino acids. Mapping of these residues onto the crystal structure of σ1 identified regions of conservation and variability, suggesting a likely mode of JAM-A binding via a conserved surface at the base of the σ1 head domain.

scholarly journals Adenovirus Serotype 30 Fiber Does Not Mediate Transduction via the Coxsackie-Adenovirus Receptor

2002 ◽  
Vol 76 (2) ◽  
pp. 656-661 ◽  
Author(s):  
Lane K. Law ◽  
Beverly L. Davidson
Keyword(s):  
Viral Entry ◽  
Cho Cells ◽  
Chinese Hamster ◽  
Wild Type Virus ◽  
Adenovirus Serotype ◽  
Coxsackie Adenovirus Receptor ◽  
Serotype 5 ◽  
Overlap Pcr ◽  
Adenovirus Receptor ◽  
Group D

ABSTRACT Prior work by members of our laboratory and others demonstrated that adenovirus serotype 30 (Ad30), a group D adenovirus, exhibited novel transduction characteristics compared to those of serotype 5 (Ad5, belonging to group C). While some serotype D adenoviruses bind to the coxsackie-adenovirus receptor (CAR), the ability of Ad30 fiber to bind CAR is unknown. We amplified and purified Ad30 and cloned the Ad30 fiber by overlap PCR. Alignment of Ad30 fiber with Ad3, Ad35, Ad5, Ad9, and Ad17 revealed that Ad30, like Ad9 and Ad17, has a shortened fiber sequence relative to that of Ad5. The knob region of fiber was 45% identical to that of the Ad5 knob regions. We made a chimeric recombinant virus (Ad5GFPf30) in which the Ad5 fiber (amino acids [aa]47 to 582) was replaced with Ad30 fiber sequences (aa 46 to 372), and CAR-mediated viral entry was determined on CAR-expressing Chinese hamster ovary (CHO) cells. While CAR expression significantly increased Ad5GFP-mediated transduction in CHO cells (from 1 to 36%), it did not enhance Ad5GFPf30 gene transfer. Binding of radiolabeled Ad5GFPf30 or Ad30 wild-type virus was also not improved by the expression of CAR. These results suggest that Ad30 fiber is distinct from Ad5, Ad9, and Ad17 fibers in its inability to direct transduction via CAR.

scholarly journals Generation of Transduction-Competent Retroviral Vectors by Infection with a Single Hybrid Vaccinia Virus

2003 ◽  
Vol 77 (12) ◽  
pp. 7017-7025 ◽  
Author(s):  
Christian Konetschny ◽  
Georg W. Holzer ◽  
Carsten Urban ◽  
Thomas Hämmerle ◽  
Josef Mayrhofer ◽  
...  
Keyword(s):  
Vaccinia Virus ◽  
Host Range ◽  
Fluorescent Protein ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Retroviral Vectors ◽  
Host Cells ◽  
Rabbit Kidney ◽  
Single Infection ◽  
Broad Host Range

ABSTRACT Recombinant vaccinia viruses that express defective retroviral vectors upon a single infection event in normal host cells were constructed. The gag-pol and envelope genes and a retroviral vector unit were inserted as vaccinia virus promoter-controlled transcription units at three separate loci. The triple recombinant virus was used to infect such diverse cell types as monkey and rabbit kidney, human lung, and primary chicken cells, resulting in the production of transduction-competent defective retroviral vectors. Infection of Chinese hamster ovary cells, which are nonpermissive for vaccinia virus replication, also resulted in production of retroviral vectors and secondary permanent transduction of the host cells. Since vaccinia virus supports the expression of cytotoxic proteins, the vesicular stomatitis virus G glycoprotein could be chosen as the envelope allowing a broad host range of transduction. Functionality of particles was monitored by expression of the green fluorescent protein in transduced 3T3 cell clones. This is the first description of a single chimeric virus encoding and releasing functional retroviral vectors, providing proof of principle of the new concept. No replication-competent retrovirus was detectable by sensitive reverse transcriptase assays. Since vaccinia virus has a broad host range, is extremely robust, and can be obtained at high titers and safe nonreplicating vaccinia virus strains are available, the hybrid system may open new perspectives for gene delivery.

scholarly journals Interaction of Adenovirus Type 5 Fiber with the Coxsackievirus and Adenovirus Receptor Activates Inflammatory Response in Human Respiratory Cells

2006 ◽  
Vol 80 (22) ◽  
pp. 11241-11254 ◽  
Author(s):  
Anna Tamanini ◽  
Elena Nicolis ◽  
Alberto Bonizzato ◽  
Valentino Bezzerri ◽  
Paola Melotti ◽  
...  
Keyword(s):  
Heparan Sulfate ◽  
Nuclear Translocation ◽  
A549 Cells ◽  
Adenovirus Type ◽  
Nuclear Factor Κb ◽  
Mitogen Activated Protein Kinase ◽  
Penton Base ◽  
Respiratory Cells ◽  
Inducible Protein ◽  
Adenovirus Receptor

ABSTRACT The innate immune response to adenovirus (Ad)-derived gene transfer vectors has been shown to initiate immediately after interaction of Ad with respiratory epithelial cells, through the induction of extracellular signal-regulated kinase 1 and 2 (ERK1/2) and JNK mitogen-activated protein kinase (MAPK), nuclear factor κB (NF-κB), and different proinflammatory genes. Ad serotypes 2 or 5 (Ad2/5) enter respiratory epithelia after initial binding of fiber with the coxsackievirus-adenovirus receptor (CAR) or, alternatively, with cell surface heparan sulfate glycosaminoglycans. Ad2/5 internalization is triggered by binding of penton base to cellular RGD-binding integrins. Here we investigated the role of the Ad5 surface domain proteins constituting the vector capsid, namely, the fiber, the penton base, and the hexon, on the transmembrane signals leading to the transcription of the different proinflammatory genes in the human respiratory A549 cell line. Interaction of Ad fiber with CAR activates both ERK1/2 and JNK MAPK and the nuclear translocation of NF-κB, whereas no activation was observed after exposing A549 cells to penton base and hexon proteins. Moreover, interaction of Ad fiber with CAR, but not heparan sulfate proteoglycans, promotes transcription of the chemokines interleukin-8, GRO-α, GRO-γ, RANTES, and interferon-inducible protein 10. These results identify the binding of Ad5 fiber with the cellular CAR as a key proinflammatory activation event in epithelial respiratory cells that is independent of the transcription of Ad5 genes.

Sign in / Sign up

Export Citation Format

Share Document