生物
核糖核酸酶P
病毒学
非洲猪瘟病毒
重组DNA
病毒
生物化学
核糖核酸
基因
作者
Saswati Nandy,Nalini S. Bora,Shubham Gaurav,Sachin Kumar
出处
期刊:Virology
[Elsevier]
日期:2024-02-01
卷期号:590: 109967-109967
标识
DOI:10.1016/j.virol.2023.109967
摘要
The African Swine Fever Virus (ASFV) is responsible for causing African Swine Fever (ASF), a severe contagious disease characterized by hemorrhagic symptoms. The p30 protein of ASFV is the most abundantly expressed viral protein. It is reported to be antigenic and has recognized phosphorylation, glycosylation, and membrane attachment sites, which also shows that the C-terminal region of p30 is more active than the N-terminal region. The present study reports the unique RNase activity of recombinant p30. The RNase activity of p30 was stable at an optimum temperature of 37 °C, and the maximum activity was recorded at pH 7–9 in the presence of monovalent salts. The mutant of p30 (p30m), where cysteine was mutated to alanine at position 109, showed a loss of RNase activity. Our understanding of ASFV biology is significantly less; until now, we have little knowledge about the functions of its proteins. The results of the present study will assist in exploring the biology of ASFV and the role of its protein in counteracting the host immune response.
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