The Polarity of an Amino Acid at Position 1891 of Severe Fever with Thrombocytopenia Syndrome Virus L Protein Is Critical for the Polymerase Activity
Severe fever with thrombocytopenia syndrome virus subclone B7 shows strong plaque formation and cytopathic effect induction compared with other subclones and the parental strain YG1. Compared to YG1 and the other subclones, only B7 possesses a single substitution in the L protein at the amino acid p...
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MDPI AG
2020-12-01
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| Series: | Viruses |
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| Online Access: | https://www.mdpi.com/1999-4915/13/1/33 |
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| author | Kisho Noda Yoshimi Tsuda Fumiya Kozawa Manabu Igarashi Kenta Shimizu Jiro Arikawa Kumiko Yoshimatsu |
| author_facet | Kisho Noda Yoshimi Tsuda Fumiya Kozawa Manabu Igarashi Kenta Shimizu Jiro Arikawa Kumiko Yoshimatsu |
| author_sort | Kisho Noda |
| collection | DOAJ |
| description | Severe fever with thrombocytopenia syndrome virus subclone B7 shows strong plaque formation and cytopathic effect induction compared with other subclones and the parental strain YG1. Compared to YG1 and the other subclones, only B7 possesses a single substitution in the L protein at the amino acid position 1891, in which N is changed to K (N1891K). In this study, we evaluate the effects of this mutation on L protein activity via a cell-based minigenome assay. Substitutions of N with basic amino acids (K or R) enhanced polymerase activity, while substitutions with an acidic amino acid (E) decreased this activity. Mutation to other neutral amino acids showed no significant effect on activity. These results suggest that the characteristic of the amino acid at position 1891 of the L protein are critical for its function, especially with respect to the charge status. Our data indicate that this C-terminal domain of the L protein may be crucial to its functions in genome transcription and viral replication. |
| first_indexed | 2024-03-10T13:44:22Z |
| format | Article |
| id | doaj.art-3508cae2d9064b759de4b191f6065743 |
| institution | Directory Open Access Journal |
| issn | 1999-4915 |
| language | English |
| last_indexed | 2024-03-10T13:44:22Z |
| publishDate | 2020-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Viruses |
| spelling | doaj.art-3508cae2d9064b759de4b191f60657432023-11-21T02:44:19ZengMDPI AGViruses1999-49152020-12-011313310.3390/v13010033The Polarity of an Amino Acid at Position 1891 of Severe Fever with Thrombocytopenia Syndrome Virus L Protein Is Critical for the Polymerase ActivityKisho Noda0Yoshimi Tsuda1Fumiya Kozawa2Manabu Igarashi3Kenta Shimizu4Jiro Arikawa5Kumiko Yoshimatsu6School of Medicine, Hokkaido University, Sapporo 060-8638, JapanDepartment of Microbiology and Immunology, Faculty of Medicine, Hokkaido University, Sapporo 060-8638, JapanSchool of Medicine, Hokkaido University, Sapporo 060-8638, JapanResearch Center for Zoonosis Control, Hokkaido University, Sapporo 001-0020, JapanDepartment of Microbiology and Immunology, Faculty of Medicine, Hokkaido University, Sapporo 060-8638, JapanDepartment of Microbiology and Immunology, Faculty of Medicine, Hokkaido University, Sapporo 060-8638, JapanLaboratory of Animal Experimentation, Institute for Genetic Medicine, Hokkaido University, Sapporo 060-0815, JapanSevere fever with thrombocytopenia syndrome virus subclone B7 shows strong plaque formation and cytopathic effect induction compared with other subclones and the parental strain YG1. Compared to YG1 and the other subclones, only B7 possesses a single substitution in the L protein at the amino acid position 1891, in which N is changed to K (N1891K). In this study, we evaluate the effects of this mutation on L protein activity via a cell-based minigenome assay. Substitutions of N with basic amino acids (K or R) enhanced polymerase activity, while substitutions with an acidic amino acid (E) decreased this activity. Mutation to other neutral amino acids showed no significant effect on activity. These results suggest that the characteristic of the amino acid at position 1891 of the L protein are critical for its function, especially with respect to the charge status. Our data indicate that this C-terminal domain of the L protein may be crucial to its functions in genome transcription and viral replication.https://www.mdpi.com/1999-4915/13/1/33SFTSVL proteinbunyaviruspolymerase activity |
| spellingShingle | Kisho Noda Yoshimi Tsuda Fumiya Kozawa Manabu Igarashi Kenta Shimizu Jiro Arikawa Kumiko Yoshimatsu The Polarity of an Amino Acid at Position 1891 of Severe Fever with Thrombocytopenia Syndrome Virus L Protein Is Critical for the Polymerase Activity Viruses SFTSV L protein bunyavirus polymerase activity |
| title | The Polarity of an Amino Acid at Position 1891 of Severe Fever with Thrombocytopenia Syndrome Virus L Protein Is Critical for the Polymerase Activity |
| title_full | The Polarity of an Amino Acid at Position 1891 of Severe Fever with Thrombocytopenia Syndrome Virus L Protein Is Critical for the Polymerase Activity |
| title_fullStr | The Polarity of an Amino Acid at Position 1891 of Severe Fever with Thrombocytopenia Syndrome Virus L Protein Is Critical for the Polymerase Activity |
| title_full_unstemmed | The Polarity of an Amino Acid at Position 1891 of Severe Fever with Thrombocytopenia Syndrome Virus L Protein Is Critical for the Polymerase Activity |
| title_short | The Polarity of an Amino Acid at Position 1891 of Severe Fever with Thrombocytopenia Syndrome Virus L Protein Is Critical for the Polymerase Activity |
| title_sort | polarity of an amino acid at position 1891 of severe fever with thrombocytopenia syndrome virus l protein is critical for the polymerase activity |
| topic | SFTSV L protein bunyavirus polymerase activity |
| url | https://www.mdpi.com/1999-4915/13/1/33 |
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