The Polarity of an Amino Acid at Position 1891 of Severe Fever with Thrombocytopenia Syndrome Virus L Protein Is Critical for the Polymerase Activity

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...

Full description

Bibliographic Details
Main Authors: Kisho Noda, Yoshimi Tsuda, Fumiya Kozawa, Manabu Igarashi, Kenta Shimizu, Jiro Arikawa, Kumiko Yoshimatsu
Format: Article
Language:English
Published: MDPI AG 2021-12-01
Series:Viruses
Subjects:
SFTSV
L protein
bunyavirus
polymerase activity
Online Access:https://www.mdpi.com/1999-4915/13/1/33
id doaj-3508cae2d9064b759de4b191f6065743
record_format Article
spelling doaj-3508cae2d9064b759de4b191f60657432020-12-28T00:01:40ZengMDPI AGViruses1999-49152021-12-0113333310.3390/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
collection DOAJ
language English
format Article
sources DOAJ
author Kisho Noda
Yoshimi Tsuda
Fumiya Kozawa
Manabu Igarashi
Kenta Shimizu
Jiro Arikawa
Kumiko Yoshimatsu
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
author_facet Kisho Noda
Yoshimi Tsuda
Fumiya Kozawa
Manabu Igarashi
Kenta Shimizu
Jiro Arikawa
Kumiko Yoshimatsu
author_sort Kisho Noda
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_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_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_sort polarity of an amino acid at position 1891 of severe fever with thrombocytopenia syndrome virus l protein is critical for the polymerase activity
publisher MDPI AG
series Viruses
issn 1999-4915
publishDate 2021-12-01
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.
topic SFTSV
L protein
bunyavirus
polymerase activity
url https://www.mdpi.com/1999-4915/13/1/33
work_keys_str_mv AT kishonoda thepolarityofanaminoacidatposition1891ofseverefeverwiththrombocytopeniasyndromeviruslproteiniscriticalforthepolymeraseactivity
AT yoshimitsuda thepolarityofanaminoacidatposition1891ofseverefeverwiththrombocytopeniasyndromeviruslproteiniscriticalforthepolymeraseactivity
AT fumiyakozawa thepolarityofanaminoacidatposition1891ofseverefeverwiththrombocytopeniasyndromeviruslproteiniscriticalforthepolymeraseactivity
AT manabuigarashi thepolarityofanaminoacidatposition1891ofseverefeverwiththrombocytopeniasyndromeviruslproteiniscriticalforthepolymeraseactivity
AT kentashimizu thepolarityofanaminoacidatposition1891ofseverefeverwiththrombocytopeniasyndromeviruslproteiniscriticalforthepolymeraseactivity
AT jiroarikawa thepolarityofanaminoacidatposition1891ofseverefeverwiththrombocytopeniasyndromeviruslproteiniscriticalforthepolymeraseactivity
AT kumikoyoshimatsu thepolarityofanaminoacidatposition1891ofseverefeverwiththrombocytopeniasyndromeviruslproteiniscriticalforthepolymeraseactivity
AT kishonoda polarityofanaminoacidatposition1891ofseverefeverwiththrombocytopeniasyndromeviruslproteiniscriticalforthepolymeraseactivity
AT yoshimitsuda polarityofanaminoacidatposition1891ofseverefeverwiththrombocytopeniasyndromeviruslproteiniscriticalforthepolymeraseactivity
AT fumiyakozawa polarityofanaminoacidatposition1891ofseverefeverwiththrombocytopeniasyndromeviruslproteiniscriticalforthepolymeraseactivity
AT manabuigarashi polarityofanaminoacidatposition1891ofseverefeverwiththrombocytopeniasyndromeviruslproteiniscriticalforthepolymeraseactivity
AT kentashimizu polarityofanaminoacidatposition1891ofseverefeverwiththrombocytopeniasyndromeviruslproteiniscriticalforthepolymeraseactivity
AT jiroarikawa polarityofanaminoacidatposition1891ofseverefeverwiththrombocytopeniasyndromeviruslproteiniscriticalforthepolymeraseactivity
AT kumikoyoshimatsu polarityofanaminoacidatposition1891ofseverefeverwiththrombocytopeniasyndromeviruslproteiniscriticalforthepolymeraseactivity
_version_ 1724368917876441088

Similar Items