Structural perspective on the formation of ribonucleoprotein complex in negative-sense single-stranded RNA viruses

•Ribonucleoprotein (RNP) plays essential roles in the life cycles of negative-sense single-stranded RNA viruses (NSRVs).•RNP formation in NSRVs has different molecular mechanisms.•Viral nucleoprotein can have enzymatic activities beyond RNA encapsidation.•Blockage of RNP formation provides great pot...

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Published inTrends in microbiology (Regular ed.) Vol. 21; no. 9; pp. 475 - 484
Main Authors Zhou, Honggang, Sun, Yuna, Guo, Yu, Lou, Zhiyong
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 01.09.2013
Subjects
Online AccessGet full text
ISSN0966-842X
1878-4380
1878-4380
DOI10.1016/j.tim.2013.07.006

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Abstract •Ribonucleoprotein (RNP) plays essential roles in the life cycles of negative-sense single-stranded RNA viruses (NSRVs).•RNP formation in NSRVs has different molecular mechanisms.•Viral nucleoprotein can have enzymatic activities beyond RNA encapsidation.•Blockage of RNP formation provides great potential for antiviral development. Negative-sense single-stranded RNA viruses (NSRVs) possess a ribonucleoprotein (RNP) complex composed of viral polymerase and genomic RNA surrounded by viral nucleoprotein. The RNP facilitates virus replication, transcription, and assembly. To date, a large body of structural work, through crystallography and electron microscopy (EM) analysis, has been performed to aid understanding the molecular mechanism of RNP formation in NSRVs, and provides great potential for the discovery of antiviral agents targeting viral RNP formation.
AbstractList Negative-sense single-stranded RNA viruses (NSRVs) possess a ribonucleoprotein (RNP) complex composed of viral polymerase and genomic RNA surrounded by viral nucleoprotein. The RNP facilitates virus replication, transcription, and assembly. To date, a large body of structural work, through crystallography and electron microscopy (EM) analysis, has been performed to aid understanding the molecular mechanism of RNP formation in NSRVs, and provides great potential for the discovery of antiviral agents targeting viral RNP formation.Negative-sense single-stranded RNA viruses (NSRVs) possess a ribonucleoprotein (RNP) complex composed of viral polymerase and genomic RNA surrounded by viral nucleoprotein. The RNP facilitates virus replication, transcription, and assembly. To date, a large body of structural work, through crystallography and electron microscopy (EM) analysis, has been performed to aid understanding the molecular mechanism of RNP formation in NSRVs, and provides great potential for the discovery of antiviral agents targeting viral RNP formation.
Highlights • Ribonucleoprotein (RNP) plays essential roles in the life cycles of negative-sense single-stranded RNA viruses (NSRVs). • RNP formation in NSRVs has different molecular mechanisms. • Viral nucleoprotein can have enzymatic activities beyond RNA encapsidation. • Blockage of RNP formation provides great potential for antiviral development.
Negative-sense single-stranded RNA viruses (NSRVs) possess a ribonucleoprotein (RNP) complex composed of viral polymerase and genomic RNA surrounded by viral nucleoprotein. The RNP facilitates virus replication, transcription, and assembly. To date, a large body of structural work, through crystallography and electron microscopy (EM) analysis, has been performed to aid understanding the molecular mechanism of RNP formation in NSRVs, and provides great potential for the discovery of antiviral agents targeting viral RNP formation.
•Ribonucleoprotein (RNP) plays essential roles in the life cycles of negative-sense single-stranded RNA viruses (NSRVs).•RNP formation in NSRVs has different molecular mechanisms.•Viral nucleoprotein can have enzymatic activities beyond RNA encapsidation.•Blockage of RNP formation provides great potential for antiviral development. Negative-sense single-stranded RNA viruses (NSRVs) possess a ribonucleoprotein (RNP) complex composed of viral polymerase and genomic RNA surrounded by viral nucleoprotein. The RNP facilitates virus replication, transcription, and assembly. To date, a large body of structural work, through crystallography and electron microscopy (EM) analysis, has been performed to aid understanding the molecular mechanism of RNP formation in NSRVs, and provides great potential for the discovery of antiviral agents targeting viral RNP formation.
Author Guo, Yu
Zhou, Honggang
Lou, Zhiyong
Sun, Yuna
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Keywords antiviral drugs
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ribonucleoprotein complex
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negative-sense single-stranded RNA virus
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Snippet •Ribonucleoprotein (RNP) plays essential roles in the life cycles of negative-sense single-stranded RNA viruses (NSRVs).•RNP formation in NSRVs has different...
Highlights • Ribonucleoprotein (RNP) plays essential roles in the life cycles of negative-sense single-stranded RNA viruses (NSRVs). • RNP formation in NSRVs...
Negative-sense single-stranded RNA viruses (NSRVs) possess a ribonucleoprotein (RNP) complex composed of viral polymerase and genomic RNA surrounded by viral...
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SubjectTerms Animals
antiviral agents
antiviral drugs
crystallography
electron microscopy
formation
Humans
Internal Medicine
negative-sense single-stranded RNA virus
nucleoproteins
ribonucleoprotein complex
ribonucleoproteins
Ribonucleoproteins - chemistry
Ribonucleoproteins - genetics
Ribonucleoproteins - metabolism
RNA
RNA Viruses - chemistry
RNA Viruses - genetics
RNA Viruses - metabolism
RNA, Viral - chemistry
RNA, Viral - genetics
RNA, Viral - metabolism
structure
Viral Proteins - chemistry
Viral Proteins - genetics
Viral Proteins - metabolism
Virus Diseases - drug therapy
Virus Diseases - virology
virus replication
viruses
Title Structural perspective on the formation of ribonucleoprotein complex in negative-sense single-stranded RNA viruses
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https://www.ncbi.nlm.nih.gov/pubmed/23953596
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https://www.proquest.com/docview/1803092760
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