Amino acid substitutions affecting aspartic acid 605 and valine 606 decrease the interaction strength between the influenza virus RNA polymerase PB2 '627' domain and the viral nucleoprotein
Publication in refereed journal

替代計量分析
.

其它資訊
摘要The influenza virus RNA genome is transcribed and replicated in the context of the viral ribonucleoprotein (vRNP) complex by the viral RNA polymerase. The nucleoprotein (NP) is the structural component of the vRNP providing a scaffold for the viral RNA. In the vRNP as well as during transcription and replication the viral polymerase interacts with NP but it is unclear which parts of the polymerase and NP mediate these interactions. Previously the C-terminal '627' domain (amino acids 538-693) of PB2 was shown to interact with NP. Here we report that a fragment encompassing amino acids 146-185 of NP is sufficient to mediate this interaction. Using NMR chemical shift perturbation assays we show that amino acid region 601 to 607 of the PB2 '627' domain interacts with this fragment of NP. Substitutions of these PB2 amino acids resulted in diminished RNP activity and surface plasmon resonance assays showed that amino acids D605 was essential for the interaction with NP and V606 may also play a partial role in the interaction. Collectively these results reveal a possible interaction surface between NP and the PB2 subunit of the RNA polymerase complex.
出版社接受日期29.12.2017
著者Ho-Pan Hsia, Yin-Hua Yang, Wun-Chung Szeto, Benjamin E. Nilsson, Chun-Yeung Lo, Andy Ka-Leung Ng, Ervin Fodor, Pang-Chui Shaw
期刊名稱PLoS ONE
出版年份2018
月份1
日期16
卷號13
期次1
文章號碼e0191226
國際標準期刊號1932-6203
語言美式英語

上次更新時間 2020-30-09 於 01:04