Genetic evolution analysis of novel recombinant pseudorabies virus strain in Sichuan, China

2020 ◽  
Vol 67 (4) ◽  
pp. 1428-1432 ◽  
Author(s):  
Jianbo Huang ◽  
Ling Zhu ◽  
Jun Zhao ◽  
Xinhuan Yin ◽  
Yu Feng ◽  
...  
2020 ◽  
Vol 17 (1) ◽  
Author(s):  
Hui-Hua Zheng ◽  
Lin-Qing Wang ◽  
Peng-Fei Fu ◽  
Lan-Lan Zheng ◽  
Hong-Ying Chen ◽  
...  

2012 ◽  
Vol 26 (17) ◽  
pp. 1621-1625 ◽  
Author(s):  
Franco Matías Escobar ◽  
María Carola Sabini ◽  
Silvia Matilde Zanon ◽  
Carlos Eugenio Tonn ◽  
Liliana Inés Sabini

1998 ◽  
Vol 330 (1) ◽  
pp. 55-59 ◽  
Author(s):  
Chien-Yun HSIANG ◽  
Tin-Yun HO ◽  
Chin-Hui HSIANG ◽  
Tien-Jye CHANG

The pseudorabies virus (PRV) DNase gene has previously been mapped within the PRV genome. To characterize further the enzymic properties of PRV DNase, this enzyme was expressed in Escherichia coli with the use of a pET expression vector. The protein was purified to homogeneity and assayed for nuclease activity in vitro. Recombinant PRV DNase exhibited an alkaline pH preference and an absolute requirement for Mg2+ ions that could not be replaced by Ca2+ and Na+ ions. Further studies showed that PRV DNase exhibited endonuclease, 5ʹ-exonuclease and 3ʹ-exonuclease activities in both single-stranded and double-stranded DNA. This activity occurred randomly and no significant base preference was demonstrated. The multiple biochemical activities of PRV DNase are similar to the activities of Neurospora crassa endo-exonuclease and E. coli RecBCD, two additional enzymes that are involved in recombination. Taken together, the similarity of action between N. crassa endo-exonuclease, E. coli RecBCD, and PRV DNase suggests that PRV DNase might have a role in the process of recombination that occurs during PRV infection.


2011 ◽  
Vol 8 (1) ◽  
pp. 307 ◽  
Author(s):  
Yang Chen ◽  
Wanzhu Guo ◽  
Zhiwen Xu ◽  
Qigui Yan ◽  
Yan Luo ◽  
...  

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