Characterization of a Blackeye Cowpea Mosaic Virus Strain from South Carolina

Plant Disease ◽  
1987 ◽  
Vol 71 (3) ◽  
pp. 243 ◽  
Author(s):  
J. F. Murphy
2008 ◽  
Vol 20 (24) ◽  
pp. 4816-4820 ◽  
Author(s):  
Alfredo A. Martinez‐Morales ◽  
Nathaniel G. Portney ◽  
Yu Zhang ◽  
Giuseppe Destito ◽  
Gurer Budak ◽  
...  

1973 ◽  
Vol 18 (3) ◽  
pp. 359-367 ◽  
Author(s):  
L. J. L. D. van Griensven ◽  
A. van Kammen ◽  
G. Rezelman

2006 ◽  
Vol 81 (4) ◽  
pp. 1632-1640 ◽  
Author(s):  
Kristopher J. Koudelka ◽  
Chris S. Rae ◽  
Maria J. Gonzalez ◽  
Marianne Manchester

ABSTRACT Cowpea mosaic virus (CPMV), a plant virus that is a member of the picornavirus superfamily, is increasingly being used for nanotechnology applications, including material science, vascular imaging, vaccine development, and targeted drug delivery. For these applications, it is critical to understand the in vivo interactions of CPMV within the mammalian system. Although the bioavailability of CPMV in the mouse has been demonstrated, the specific interactions between CPMV and mammalian cells need to be characterized further. Here we demonstrate that although the host range for replication of CPMV is confined to plants, mammalian cells nevertheless bind and internalize CPMV in significant amounts. This binding is mediated by a conserved 54-kDa protein found on the plasma membranes of both human and murine cell lines. Studies using a deficient cell line, deglycosidases, and glycosylation inhibitors showed that the CPMV binding protein (CPMV-BP) is not glycosylated. A possible 47-kDa isoform of the CPMV-BP was also detected in the organelle and nuclear subcellular fraction prepared from murine fibroblasts. Further characterization of CPMV-BP is important to understand how CPMV is trafficked through the mammalian system and may shed light on how picornaviruses may have evolved between plant and animal hosts.


Agrosearch ◽  
2017 ◽  
Vol 17 (1) ◽  
pp. 11
Author(s):  
A.D. Ibrahim ◽  
M.T. Salaudeen ◽  
L.Y. Bello ◽  
A.A. Abdullahi ◽  
A.S. Adamu ◽  
...  

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