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.

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.

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 Chimpanzee adenovirus CV-68 adapted as a gene delivery vector interacts with the coxsackievirus and adenovirus receptor

2002 ◽  
Vol 83 (1) ◽  
pp. 151-155 ◽  
Author(s):  
Christopher J. Cohen ◽  
Zhi Quan Xiang ◽  
Guang-Ping Gao ◽  
Hildegund C. J. Ertl ◽  
James M. Wilson ◽  
...  
Keyword(s):  
Gene Delivery ◽  
Cho Cells ◽  
Human Adenovirus ◽  
Adenovirus Type ◽  
Soluble Form ◽  
Delivery Vector ◽  
Coxsackievirus And Adenovirus Receptor ◽  
Adenovirus Receptor ◽  
Adenovirus Type 5 ◽  
Dependent Mechanism

A replication-defective form of chimpanzee adenovirus type 68 (C68) has been developed to circumvent problems posed by widespread preexisting immunity to common human adenovirus vectors. To investigate the determinants of C68 tropism, its interaction with the coxsackievirus and adenovirus receptor (CAR) was studied. Although CHO cells were resistant to transduction by C68 as well as by adenovirus type 5 (Ad5), CHO cells expressing either human or murine CAR were transduced readily. C68 transduction, like Ad5 transduction, was blocked when cells were exposed to anti-CAR antibody or when virus was exposed to a soluble form of the CAR extracellular domain. These results indicate that gene delivery by C68 occurs by a CAR-dependent mechanism.

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 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 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 Taenia solium Oncosphere Adhesion to Intestinal Epithelial and Chinese Hamster Ovary Cells In Vitro

2007 ◽  
Vol 75 (11) ◽  
pp. 5158-5166 ◽  
Author(s):  
Manuela Verastegui ◽  
Robert H. Gilman ◽  
Yanina Arana ◽  
Dylan Barber ◽  
Jeanette Velásquez ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Chinese Hamster Ovary ◽  
Cho Cells ◽  
Colorectal Adenocarcinoma ◽  
Chinese Hamster Ovary Cells ◽  
Taenia Solium ◽  
Chinese Hamster ◽  
Host Cells ◽  
Ovary Cells

ABSTRACT The specific mechanisms underlying Taenia solium oncosphere adherence and penetration in the host have not been studied previously. We developed an in vitro adhesion model assay to evaluate the mechanisms of T. solium oncosphere adherence to the host cells. The following substrates were used: porcine intestinal mucosal scrapings (PIMS), porcine small intestinal mucosal explants (PSIME), Chinese hamster ovary cells (CHO cells), epithelial cells from ileocecal colorectal adenocarcinoma (HCT-8 cells), and epithelial cells from colorectal adenocarcinoma (Caco-2 cells). CHO cells were used to compare oncosphere adherence to fixed and viable cells, to determine the optimum time of oncosphere incubation, to determine the role of sera and monolayer cell maturation, and to determine the effect of temperature on oncosphere adherence. Light microscopy, scanning microscopy, and transmission microscopy were used to observe morphological characteristics of adhered oncospheres. This study showed in vitro adherence of activated T. solium oncospheres to PIMS, PSIME, monolayer CHO cells, Caco-2 cells, and HCT-8 cells. The reproducibility of T. solium oncosphere adherence was most easily measured with CHO cells. Adherence was enhanced by serum-binding medium with >5% fetal bovine serum, which resulted in a significantly greater number of oncospheres adhering than the number adhering when serum at a concentration less than 2.5% was used (P < 0.05). Oncosphere adherence decreased with incubation of cells at 4°C compared with the adherence at 37°C. Our studies also demonstrated that T. solium oncospheres attach to cells with elongated microvillus processes and that the oncospheres expel external secretory vesicles that have the same oncosphere processes.

scholarly journals Mechanistic Aspects of Adenovirus Serotype 2 Inactivation with Free Chlorine

2010 ◽  
Vol 76 (9) ◽  
pp. 2946-2954 ◽  
Author(s):  
Martin A. Page ◽  
Joanna L. Shisler ◽  
Benito J. Mariñas
Keyword(s):  
Life Cycle ◽  
Cell Attachment ◽  
Adenovirus Type ◽  
Free Chlorine ◽  
Host Cells ◽  
Coxsackie Adenovirus Receptor ◽  
Genome Damage ◽  
Fiber Proteins ◽  
Molecular Components

ABSTRACT Free chlorine is an effective disinfectant for controlling adenoviruses in drinking water, but little is known about the underlying inactivation mechanisms. The objective of this study was to elucidate the molecular components of adenovirus type 2 (Ad2) targeted by free chlorine during the inactivation process. The effects of free chlorine treatment on several Ad2 molecular components and associated life cycle events were compared to its effect on the ability of adenovirus to complete its life cycle, i.e., viability. Free chlorine treatment of Ad2 virions did not impair their ability to interact with monoclonal antibodies specific for hexon and fiber proteins of the Ad2 capsid, as measured by enzyme-linked immunosorbent assays, nor did it impair their interaction with recombinant, purified Coxsackie-adenovirus receptor (CAR) proteins in vitro. Free chlorine-treated Ad2 virions also retained their ability to bind to CAR receptors on A549 cell monolayers, despite being unable to form plaques, suggesting that free chlorine inactivates Ad2 by inhibiting a postbinding event of the Ad2 life cycle. DNA isolated from Ad2 virions that had been inactivated by free chlorine was able to be amplified by PCR, indicating that genome damage was not the cause of inactivation. However, inactivated Ad2 virions were unable to express E1A viral proteins during infection of A549 host cells, as measured by using immunoblotting. Collectively, these results indicate that free chlorine inactivates adenovirus by damaging proteins that govern life cycle processes occurring after host cell attachment, such as endocytosis, endosomal lysis, or nuclear delivery.

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 Core2 beta-1,6-N-acetylglucosaminyltransferase enzyme activity is critical for P-selectin glycoprotein ligand-1 binding to P-selectin

Blood ◽  
1996 ◽  
Vol 88 (10) ◽  
pp. 3872-3879 ◽  
Author(s):  
R Kumar ◽  
RT Camphausen ◽  
FX Sullivan ◽  
DA Cumming
Keyword(s):  
Cho Cells ◽  
Chinese Hamster ◽  
Sialyl Lewis X ◽  
Activated T Cells ◽  
Transfected Cells ◽  
High Affinity ◽  
Sialyl Lewis ◽  
Selectin Ligand

P-selectin glycoprotein ligand-1 (PSGL-1) is a high-affinity counterreceptor for P-selectin on myeloid cells and activated T-cells. In addition, PSGL-1 can serve, both in vitro and in vivo, as an E- selectin ligand. Appropriate glycosylation of PSGL-1 is crucial for binding to P-selectin. Functional PSGL-1 is known to bear sialyl lewis X (SLex) or a closely related oligosaccharide. In this study, we show that Chinese hamster ovary (CHO) cells expressing PSGL-1 and fucosyltransferase show a dramatic increase in binding to P-selectin when transfected with “core2” transferase, the enzyme that initiates branching of O-linked glycans. Moreover, only PSGL-1 from core2 transfectant CHO cells can be affinity-captured with P-selectin, suggesting that branched O-linked glycans are required for high-affinity binding to P-selectin. Analysis of PSGL-1-derived O-linked oligosaccharides produced in core2 transfected cells shows the presence of more elaborated glycans. Interestingly, transfection of core2 in these cells does not alter binding to E-selectin.

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