Experimental Oral Administration of Canine Adenovirus (Type 2) to Raccoons (Procyon lotor)

1992 ◽  
Vol 29 (6) ◽  
pp. 509-513 ◽  
Author(s):  
A. N. Hamir ◽  
N. Raju ◽  
C. E. Rupprecht

Canine adenovirus type 2 (CAV2) has been proposed for recombinant vaccines to control rabies in wild animals. To evaluate the suitability of CAV2 as a safe vector for the genetically engineered vaccines, seven wild-caught raccoons (three males and four females) were administered CAV2 per os. Two of the animals were euthanatized on each of post-infection days 3, 6, and 14, and one was euthanatized on day 21. Two other control raccoons (a male and a female) were also euthanatized on day 21. Microscopic pulmonary lesions of multifocal necrotizing bronchiolitis with basophilic intranuclear inclusions were seen in 3/4 raccoons euthanatized on post-infection days 3 and 6. Ultrastructural examination of lungs with pulmonary lesions revealed hexagonal viral particles characteristic of adenoviruses. CAV2 is potentially pathogenic for raccoons, and this susceptibility should be of concern to developers of recombinant vaccines who intend to use CAV2 as a vaccine vector.

2005 ◽  
Vol 16 (6) ◽  
pp. 2999-3009 ◽  
Author(s):  
Sten Strunze ◽  
Lloyd C. Trotman ◽  
Karin Boucke ◽  
Urs F. Greber

Incoming adenovirus type 2 (Ad2) and Ad5 shuttle bidirectionally along microtubules, biased to the microtubule-organizing center by the dynein/dynactin motor complex. It is unknown how the particles reach the nuclear pore complex, where capsids disassemble and viral DNA enters the nucleus. Here, we identified a novel link between nuclear export and microtubule-mediated transport. Two distinct inhibitors of the nuclear export factor CRM1, leptomycin B (LMB) and ratjadone A (RJA) or CRM1-siRNAs blocked adenovirus infection, arrested cytoplasmic transport of viral particles at the microtubule-organizing center or in the cytoplasm and prevented capsid disassembly and nuclear import of the viral genome. In mitotic cells where CRM1 is in the cytoplasm, adenovirus particles were not associated with microtubules but upon LMB treatment, they enriched at the spindle poles implying that CRM1 inhibited microtubule association of adenovirus. We propose that CRM1, a nuclear factor exported by CRM1 or a protein complex containing CRM1 is part of a sensor mechanism triggering the unloading of the incoming adenovirus particles from microtubules proximal to the nucleus of interphase cells.


1979 ◽  
Vol 30 (2) ◽  
pp. 462-471 ◽  
Author(s):  
M A Mirza ◽  
J Weber

1975 ◽  
Vol 16 (4) ◽  
pp. 767-774 ◽  
Author(s):  
R Schilling ◽  
B Weingärtner ◽  
E L Winnacker

1975 ◽  
Vol 16 (4) ◽  
pp. 759-766 ◽  
Author(s):  
A Tolun ◽  
U Pettersson

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