scholarly journals Soluble Recombinant Coxsackievirus and Adenovirus Receptor Abrogates Coxsackievirus B3–Mediated Pancreatitis and Myocarditis in Mice

2004 ◽  
Vol 189 (8) ◽  
pp. 1431-1439 ◽  
Author(s):  
Bobby Yanagawa ◽  
O. Brad Spiller ◽  
David G. Proctor ◽  
Jonathan Choy ◽  
Honglin Luo ◽  
...  
Keyword(s):  
Coxsackievirus B3 ◽  
Coxsackievirus And Adenovirus Receptor ◽  
Adenovirus Receptor

scholarly journals Coxsackievirus B3—Its Potential as an Oncolytic Virus

Viruses ◽  
2021 ◽  
Vol 13 (5) ◽  
pp. 718
Author(s):  
Anja Geisler ◽  
Ahmet Hazini ◽  
Lisanne Heimann ◽  
Jens Kurreck ◽  
Henry Fechner
Keyword(s):  
Oncolytic Virus ◽  
Coxsackievirus B3 ◽  
Current Status ◽  
Mouse Tumor ◽  
Strong Immune Response ◽  
Cancer Types ◽  
Coxsackievirus And Adenovirus Receptor ◽  
Adenovirus Receptor ◽  
Anti Tumor Activity ◽  
Entry Receptor

Oncolytic virotherapy represents one of the most advanced strategies to treat otherwise untreatable types of cancer. Despite encouraging developments in recent years, the limited fraction of patients responding to therapy has demonstrated the need to search for new suitable viruses. Coxsackievirus B3 (CVB3) is a promising novel candidate with particularly valuable features. Its entry receptor, the coxsackievirus and adenovirus receptor (CAR), and heparan sulfate, which is used for cellular entry by some CVB3 variants, are highly expressed on various cancer types. Consequently, CVB3 has broad anti-tumor activity, as shown in various xenograft and syngeneic mouse tumor models. In addition to direct tumor cell killing the virus induces a strong immune response against the tumor, which contributes to a substantial increase in the efficiency of the treatment. The toxicity of oncolytic CVB3 in healthy tissues is variable and depends on the virus strain. It can be abrogated by genetic engineering the virus with target sites of microRNAs. In this review, we present an overview of the current status of the development of CVB3 as an oncolytic virus and outline which steps still need to be accomplished to develop CVB3 as a therapeutic agent for clinical use in cancer treatment.

scholarly journals The Coxsackievirus and Adenovirus Receptor: Glycosylation and the Extracellular D2 Domain Are Not Required for Coxsackievirus B3 Infection

2016 ◽  
Vol 90 (12) ◽  
pp. 5601-5610 ◽  
Author(s):  
Sandra Pinkert ◽  
Carsten Röger ◽  
Jens Kurreck ◽  
Jeffrey M. Bergelson ◽  
Henry Fechner
Keyword(s):  
Virus Infection ◽  
Immunoglobulin Superfamily ◽  
Minor Importance ◽  
Receptor Function ◽  
Virus Binding ◽  
D2 Domain ◽  
Cvb3 Infection ◽  
Coxsackie B Viruses ◽  
Coxsackievirus And Adenovirus Receptor ◽  
Adenovirus Receptor

ABSTRACTThe coxsackievirus and adenovirus receptor (CAR) is a member of the immunoglobulin superfamily (IgSF) and functions as a receptor for coxsackie B viruses (CVBs). The extracellular portion of CAR comprises two glycosylated immunoglobulin-like domains, D1 and D2. CAR-D1 binds to the virus and is essential for virus infection; however, it is not known whether D2 is also important for infection, and the role of glycosylation has not been explored. To understand the function of these structural components in CAR-mediated CVB3 infection, we generated a panel of human (h) CAR deletion and substitution mutants and analyzed their functionality as CVB receptors, examining both virus binding and replication. Lack of glycosylation of the CAR-D1 or -D2 domains did not adversely affect CVB3 binding or infection, indicating that the glycosylation of CAR is not required for its receptor functions. Deletion of the D2 domain reduced CVB3 binding, with a proportionate reduction in the efficiency of virus infection. Replacement of D2 with the homologous D2 domain from chicken CAR, or with the heterologous type C2 immunoglobulin-like domain from IgSF11, another IgSF member, fully restored receptor function; however, replacement of CAR-D2 with domains from CD155 or CD80 restored function only in part. These data indicate that glycosylation of the extracellular domain of hCAR plays no role in CVB3 receptor function and that CAR-D2 is not specifically required. The D2 domain may function largely as a spacer permitting virus access to D1; however, the data may also suggest that D2 affects virus binding by influencing the conformation of D1.IMPORTANCEAn important step in virus infection is the initial interaction of the virus with its cellular receptor. Although the role in infection of the extracellular CAR-D1, cytoplasmic, and transmembrane domains have been analyzed extensively, nothing is known about the function of CAR-D2 and the extracellular glycosylation of CAR. Our data indicate that glycosylation of the extracellular CAR domain has only minor importance for the function of CAR as CVB3 receptor and that the D2 domain is not essential per se but contributes to receptor function by promoting the exposure of the D1 domain on the cell surface. These results contribute to our understanding of the coxsackievirus-receptor interactions.

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 Coxsackievirus and adenovirus receptor (CAR) mediates atrioventricular-node function and connexin 45 localization in the murine heart

2008 ◽  
Vol 118 (8) ◽  
pp. 2758-2770 ◽  
Author(s):  
Byung-Kwan Lim ◽  
Dingding Xiong ◽  
Andrea Dorner ◽  
Tae-Jin Youn ◽  
Aaron Yung ◽  
...  
Keyword(s):  
Atrioventricular Node ◽  
Coxsackievirus And Adenovirus Receptor ◽  
Adenovirus Receptor
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