Amino acid sites related to the PB2 subunits of IDV affect polymerase activity
Abstract Background In 2011, a new influenza virus, named Influenza D Virus (IDV), was isolated from pigs, and then cattle, presenting influenza-like symptoms. IDV is one of the causative agents of Bovine Respiratory Disease (BRD), which causes high morbidity and mortality in feedlot cattle worldwid...
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BMC
2021
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oai:doaj.org-article:7e6fe9a271234b668b540526405db7852021-11-28T12:03:07ZAmino acid sites related to the PB2 subunits of IDV affect polymerase activity10.1186/s12985-021-01703-z1743-422Xhttps://doaj.org/article/7e6fe9a271234b668b540526405db7852021-11-01T00:00:00Zhttps://doi.org/10.1186/s12985-021-01703-zhttps://doaj.org/toc/1743-422XAbstract Background In 2011, a new influenza virus, named Influenza D Virus (IDV), was isolated from pigs, and then cattle, presenting influenza-like symptoms. IDV is one of the causative agents of Bovine Respiratory Disease (BRD), which causes high morbidity and mortality in feedlot cattle worldwide. To date, the molecular mechanisms of IDV pathogenicity are unknown. Recent IDV outbreaks in cattle, along with serological and genetic evidence of IDV infection in humans, have raised concerns regarding the zoonotic potential of this virus. Influenza virus polymerase is a determining factor of viral pathogenicity to mammals. Methods Here we take a prospective approach to this question by creating a random mutation library about PB2 subunit of the IDV viral polymerase to test which amino acid point mutations will increase viral polymerase activity, leading to increased pathogenicity of the virus. Results Our work shows some exact sites that could affect polymerase activities in influenza D viruses. For example, two single-site mutations, PB2-D533S and PB2-G603Y, can independently increase polymerase activity. The PB2-D533S mutation alone can increase the polymerase activity by 9.92 times, while the PB2-G603Y mutation increments the activity by 8.22 times. Conclusion Taken together, our findings provide important insight into IDV replication fitness mediated by the PB2 protein, increasing our understanding of IDV replication and pathogenicity and facilitating future studies.Yutian WangWeiyang SunZhenfei WangMenglin ZhaoXinghai ZhangYunyi KongXuefeng WangNa FengTiecheng WangFeihu YanYongkun ZhaoXianzhu XiaSongtao YangYuwei GaoBMCarticleInfluenza D virusViral polymerasePB2 proteinSingle-site mutationRandom mutation libraryMini-replicon reporter constructsInfectious and parasitic diseasesRC109-216ENVirology Journal, Vol 18, Iss 1, Pp 1-8 (2021) |
| institution |
DOAJ |
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DOAJ |
| language |
EN |
| topic |
Influenza D virus Viral polymerase PB2 protein Single-site mutation Random mutation library Mini-replicon reporter constructs Infectious and parasitic diseases RC109-216 |
| spellingShingle |
Influenza D virus Viral polymerase PB2 protein Single-site mutation Random mutation library Mini-replicon reporter constructs Infectious and parasitic diseases RC109-216 Yutian Wang Weiyang Sun Zhenfei Wang Menglin Zhao Xinghai Zhang Yunyi Kong Xuefeng Wang Na Feng Tiecheng Wang Feihu Yan Yongkun Zhao Xianzhu Xia Songtao Yang Yuwei Gao Amino acid sites related to the PB2 subunits of IDV affect polymerase activity |
| description |
Abstract Background In 2011, a new influenza virus, named Influenza D Virus (IDV), was isolated from pigs, and then cattle, presenting influenza-like symptoms. IDV is one of the causative agents of Bovine Respiratory Disease (BRD), which causes high morbidity and mortality in feedlot cattle worldwide. To date, the molecular mechanisms of IDV pathogenicity are unknown. Recent IDV outbreaks in cattle, along with serological and genetic evidence of IDV infection in humans, have raised concerns regarding the zoonotic potential of this virus. Influenza virus polymerase is a determining factor of viral pathogenicity to mammals. Methods Here we take a prospective approach to this question by creating a random mutation library about PB2 subunit of the IDV viral polymerase to test which amino acid point mutations will increase viral polymerase activity, leading to increased pathogenicity of the virus. Results Our work shows some exact sites that could affect polymerase activities in influenza D viruses. For example, two single-site mutations, PB2-D533S and PB2-G603Y, can independently increase polymerase activity. The PB2-D533S mutation alone can increase the polymerase activity by 9.92 times, while the PB2-G603Y mutation increments the activity by 8.22 times. Conclusion Taken together, our findings provide important insight into IDV replication fitness mediated by the PB2 protein, increasing our understanding of IDV replication and pathogenicity and facilitating future studies. |
| format |
article |
| author |
Yutian Wang Weiyang Sun Zhenfei Wang Menglin Zhao Xinghai Zhang Yunyi Kong Xuefeng Wang Na Feng Tiecheng Wang Feihu Yan Yongkun Zhao Xianzhu Xia Songtao Yang Yuwei Gao |
| author_facet |
Yutian Wang Weiyang Sun Zhenfei Wang Menglin Zhao Xinghai Zhang Yunyi Kong Xuefeng Wang Na Feng Tiecheng Wang Feihu Yan Yongkun Zhao Xianzhu Xia Songtao Yang Yuwei Gao |
| author_sort |
Yutian Wang |
| title |
Amino acid sites related to the PB2 subunits of IDV affect polymerase activity |
| title_short |
Amino acid sites related to the PB2 subunits of IDV affect polymerase activity |
| title_full |
Amino acid sites related to the PB2 subunits of IDV affect polymerase activity |
| title_fullStr |
Amino acid sites related to the PB2 subunits of IDV affect polymerase activity |
| title_full_unstemmed |
Amino acid sites related to the PB2 subunits of IDV affect polymerase activity |
| title_sort |
amino acid sites related to the pb2 subunits of idv affect polymerase activity |
| publisher |
BMC |
| publishDate |
2021 |
| url |
https://doaj.org/article/7e6fe9a271234b668b540526405db785 |
| work_keys_str_mv |
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| _version_ |
1718408268528746496 |