Human pancreatic islet endothelial cells express coxsackievirus and adenovirus receptor and are activated by coxsackie B virus infection

2007 ◽  
Vol 21 (12) ◽  
pp. 3308-3317 ◽  
Author(s):  
Maria M. Zanone ◽  
Enrica Favaro ◽  
Elena Ferioli ◽  
Guo C. Huang ◽  
Nigel J. Klein ◽  
...  
2002 ◽  
Vol 76 (20) ◽  
pp. 10503-10506 ◽  
Author(s):  
JenniElizabeth Petrella ◽  
Christopher J. Cohen ◽  
Jedidiah Gaetz ◽  
Jeffrey M. Bergelson

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.


2004 ◽  
Vol 163 (4-5) ◽  
pp. 223-228 ◽  
Author(s):  
Penelope A. Bryant ◽  
David Tingay ◽  
Peter A. Dargaville ◽  
Mike Starr ◽  
Nigel Curtis

2003 ◽  
Vol 77 (4) ◽  
pp. 2559-2567 ◽  
Author(s):  
Katherine J. D. Ashbourne Excoffon ◽  
Thomas Moninger ◽  
Joseph Zabner

ABSTRACT The coxsackie B virus and adenovirus receptor (CAR) is a member of the immunoglobulin superfamily. In addition to activity as a viral receptor, it may play a role in cellular adhesion. We asked what determines the cell membrane microdomain of CAR. We found that CAR is localized to a novel lipid-rich microdomain similar to that of the low-density lipoprotein receptor (LDLR) but distinct from that of a CAR variant that exhibited traditional lipid raft localization via fusion to a glycosylphosphatidylinositol (GPI) tail. The cytoplasmic tail determines its membrane localization, since deletion of this domain resulted in mislocalization. Results indicate that CAR, CAR-LDLR, and LDLR reside in a novel lipid raft that is distinct from caveolin-1-containing caveolae and GPI-linked proteins. Residence in a lipid-rich domain provides a mechanism that allows CAR to interact with other cell adhesion proteins and yet function as an adenovirus receptor.


2016 ◽  
Vol 136 ◽  
pp. 1-8 ◽  
Author(s):  
Sandra Pinkert ◽  
Babette Dieringer ◽  
Sabine Diedrich ◽  
Heinz Zeichhardt ◽  
Jens Kurreck ◽  
...  

2000 ◽  
Vol 45 (1) ◽  
pp. 61-63
Author(s):  
S. A. Bopegamage ◽  
A. Petrovičová ◽  
M. Stará

1985 ◽  
Vol 31 (2) ◽  
pp. 96-100 ◽  
Author(s):  
F. M. Paul ◽  
M. Yin-Murphy

1992 ◽  
Vol 55 (7) ◽  
pp. 613-615 ◽  
Author(s):  
G Pavesi ◽  
F Gemignani ◽  
G M Macaluso ◽  
P Ventrua ◽  
G Magnani ◽  
...  

Diabetologia ◽  
1974 ◽  
Vol 10 (6) ◽  
pp. 755-759 ◽  
Author(s):  
T. J. Coleman ◽  
K. W. Taylor ◽  
D. R. Gamble

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