scholarly journals Coxsackievirus and Adenovirus Receptor Cytoplasmic and Transmembrane Domains Are Not Essential for Coxsackievirus and Adenovirus Infection

1999 ◽  
Vol 73 (3) ◽  
pp. 2559-2562 ◽  
Author(s):  
Xianghong Wang ◽  
Jeffrey M. Bergelson
Keyword(s):  
Gene Delivery ◽  
Extracellular Domain ◽  
Cytoplasmic Domain ◽  
Transmembrane Domains ◽  
Adenovirus Infection ◽  
Gpi Anchor ◽  
Virus Attachment ◽  
Coxsackievirus And Adenovirus Receptor ◽  
Adenovirus Receptor ◽  
Adenovirus 5

ABSTRACT Coxsackievirus and adenovirus receptor (CAR) from which the cytoplasmic domain had been deleted and glycosylphosphatidylinositol (GPI)-anchored CAR lacking both transmembrane and cytoplasmic domains were both capable of facilitating adenovirus 5-mediated gene delivery and infection by coxsackievirus B3. These results indicate that the CAR extracellular domain is sufficient to permit virus attachment and entry and that the presence of a GPI anchor does not prevent infection.

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 Differential Expression of the Coxsackievirus and Adenovirus Receptor Regulates Adenovirus Infection of the Placenta1

2001 ◽  
Vol 64 (3) ◽  
pp. 1001-1009 ◽  
Author(s):  
Hideki Koi ◽  
Jian Zhang ◽  
Antonis Makrigiannakis ◽  
Spiro Getsios ◽  
Colin D. MacCalman ◽  
...  
Keyword(s):  
Differential Expression ◽  
Adenovirus Infection ◽  
Coxsackievirus And Adenovirus Receptor ◽  
Adenovirus Receptor

scholarly journals Accessibility of the coxsackievirus and adenovirus receptor and its importance in adenovirus gene transduction efficiency

2012 ◽  
Vol 93 (1) ◽  
pp. 155-158 ◽  
Author(s):  
Priyanka Sharma ◽  
Abimbola Olayinka Kolawole ◽  
Sydney Marie Wiltshire ◽  
Kathleen Frondorf ◽  
Katherine Julie Diane Ashbourne Excoffon
Keyword(s):  
Choice Model ◽  
Mdck Cells ◽  
Transduction Efficiency ◽  
Adenovirus Infection ◽  
Vector Systems ◽  
A Cell ◽  
Specific Virus ◽  
Coxsackievirus And Adenovirus Receptor ◽  
Adenovirus Receptor ◽  
Darby Canine Kidney

Viruses are commonly investigated as vector systems for gene therapy. To be effective, virus-mediated gene-delivery systems require the presence of specific virus receptors to enter the target cell. One example is adenovirus and its primary receptor is the coxsackievirus and adenovirus receptor (CAR). Madin–Darby canine kidney (MDCK) cells have become a choice model system for studying CAR and adenovirus infection due to their ability to polarize rapidly into an epithelium with high transepithelial resistance. We show here that, whilst MDCK cells are resistant to adenovirus infection and hence appear functionally CAR-deficient, polarized MDCK cells express significant levels of CAR sequestered on the basolateral surface, where it is inaccessible for virus infection. Thus, although a cell type may be resistant to adenovirus infection, it is impossible to know whether it is due to a deficiency, as both CAR absence and inaccessibility are barriers to adenovirus-mediated gene transfer.

scholarly journals A Zebrafish Coxsackievirus and Adenovirus Receptor Homologue Interacts with Coxsackie B Virus and Adenovirus

2002 ◽  
Vol 76 (20) ◽  
pp. 10503-10506 ◽  
Author(s):  
JenniElizabeth Petrella ◽  
Christopher J. Cohen ◽  
Jedidiah Gaetz ◽  
Jeffrey M. Bergelson
Keyword(s):  
Adenovirus Type ◽  
Extracellular Domain ◽  
Receptor Interaction ◽  
Transfected Cells ◽  
B Virus ◽  
Coxsackie B Virus ◽  
Coxsackievirus And Adenovirus Receptor ◽  
Adenovirus Receptor ◽  
Adenovirus Type 5 ◽  
Coxsackie B

ABSTRACT In this study, a zebrafish homologue of the coxsackievirus and adenovirus receptor (CAR) protein was identified. Although the extracellular domain of zebrafish CAR (zCAR) is less than 50% identical to that of human CAR (hCAR), zCAR mediated infection of transfected cells by both adenovirus type 5 and coxsackievirus B3. CAR residues interacting deep within the coxsackievirus canyon are highly conserved in zCAR and hCAR, which is consistent with the idea that receptor contacts within the canyon are responsible for coxsackievirus attachment. In contrast, CAR residues contacting the south edge of the canyon are not conserved, suggesting that receptor interaction with the viral “puff region” is not essential for attachment.

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