Advances in Virus Research最新文献_第8页

Modulation of disease severity by plant positive-strand RNA viruses: The complex interplay of multifunctional viral proteins, subviral RNAs and virus-associated RNAs with plant signaling pathways and defense responses. 植物正链RNA病毒对疾病严重程度的调节:多功能病毒蛋白、亚病毒RNA和病毒相关RNA与植物信号通路和防御反应的复杂相互作用

2区医学

Advances in Virus Research Pub Date : 2020-01-01 Epub Date: 2020-05-21 DOI: 10.1016/bs.aivir.2020.04.003

Hélène Sanfaçon

{"title":"Modulation of disease severity by plant positive-strand RNA viruses: The complex interplay of multifunctional viral proteins, subviral RNAs and virus-associated RNAs with plant signaling pathways and defense responses.","authors":"Hélène Sanfaçon","doi":"10.1016/bs.aivir.2020.04.003","DOIUrl":"https://doi.org/10.1016/bs.aivir.2020.04.003","url":null,"abstract":"Plant viruses induce a range of symptoms of varying intensity, ranging from severe systemic necrosis to mild or asymptomatic infection. Several evolutionary constraints drive virus virulence, including the dependence of viruses on host factors to complete their infection cycle, the requirement to counteract or evade plant antiviral defense responses and the mode of virus transmission. Viruses have developed an array of strategies to modulate disease severity. Accumulating evidence has highlighted not only the multifunctional role that viral proteins play in disrupting or highjacking plant factors, hormone signaling pathways and intracellular organelles, but also the interaction networks between viral proteins, subviral RNAs and/or other viral-associated RNAs that regulate disease severity. This review focusses on positive-strand RNA viruses, which constitute the majority of characterized plant viruses. Using well-characterized viruses with different genome types as examples, recent advances are discussed as well as knowledge gaps and opportunities for further research.","PeriodicalId":50977,"journal":{"name":"Advances in Virus Research","volume":"107 ","pages":"87-131"},"PeriodicalIF":0.0,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/bs.aivir.2020.04.003","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38191543","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 3

Structure and assembly of double-stranded RNA mycoviruses. 双链RNA分枝病毒的结构与组装。

2区医学

Advances in Virus Research Pub Date : 2020-01-01 Epub Date: 2020-09-16 DOI: 10.1016/bs.aivir.2020.08.001

Carlos P Mata, Javier M Rodríguez, Nobuhiro Suzuki, José R Castón

{"title":"Structure and assembly of double-stranded RNA mycoviruses.","authors":"Carlos P Mata, Javier M Rodríguez, Nobuhiro Suzuki, José R Castón","doi":"10.1016/bs.aivir.2020.08.001","DOIUrl":"https://doi.org/10.1016/bs.aivir.2020.08.001","url":null,"abstract":"Mycoviruses are a diverse group that includes ssRNA, dsRNA, and ssDNA viruses, with or without a protein capsid, as well as with a complex envelope. Most mycoviruses are transmitted by cytoplasmic interchange and are thought to lack an extracellular phase in their infection cycle. Structural analysis has focused on dsRNA mycoviruses, which usually package their genome in a 120-subunit T=1 icosahedral capsid, with a capsid protein (CP) dimer as the asymmetric unit. The atomic structure is available for four dsRNA mycovirus from different families: Saccharomyces cerevisiae virus L-A (ScV-L-A), Penicillium chrysogenum virus (PcV), Penicillium stoloniferum virus F (PsV-F), and Rosellinia necatrix quadrivirus 1 (RnQV1). Their capsids show structural variations of the same framework, with asymmetric or symmetric CP dimers respectively for ScV-L-A and PsV-F, dimers of similar domains of a single CP for PcV, or of two different proteins for RnQV1. The CP dimer is the building block, and assembly proceeds through dimers of dimers or pentamers of dimers, in which the genome is packed as ssRNA by interaction with CP and/or viral polymerase. These capsids remain structurally undisturbed throughout the viral cycle. The T=1 capsid participates in RNA synthesis, organizing the viral polymerase (1-2 copies) and a single loosely packaged genome segment. It also acts as a molecular sieve, to allow the passage of viral transcripts and nucleotides, but to prevent triggering of host defense mechanisms. Due to the close mycovirus-host relationship, CP evolved to allocate peptide insertions with enzyme activity, as reflected in a rough outer capsid surface.","PeriodicalId":50977,"journal":{"name":"Advances in Virus Research","volume":"108 ","pages":"213-247"},"PeriodicalIF":0.0,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/bs.aivir.2020.08.001","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25587079","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 8

Immunopathogenesis of alphaviruses. 甲病毒的免疫发病机制。

2区医学

Advances in Virus Research Pub Date : 2020-01-01 Epub Date: 2020-07-08 DOI: 10.1016/bs.aivir.2020.06.002

Victoria K Baxter, Mark T Heise

{"title":"Immunopathogenesis of alphaviruses.","authors":"Victoria K Baxter, Mark T Heise","doi":"10.1016/bs.aivir.2020.06.002","DOIUrl":"https://doi.org/10.1016/bs.aivir.2020.06.002","url":null,"abstract":"Alphaviruses, members of the enveloped, positive-sense, single-stranded RNA Togaviridae family, represent a reemerging public health threat as mosquito vectors expand into new geographic territories. The Old World alphaviruses, which include chikungunya virus, Ross River virus, and Sindbis virus, tend to cause a clinical syndrome characterized by fever, rash, and arthritis, whereas the New World alphaviruses, which consist of Venezuelan equine encephalitis virus, eastern equine encephalitis virus, and western equine encephalitis virus, induce encephalomyelitis. Following recovery from the acute phase of infection, many patients are left with debilitating persistent joint and neurological complications that can last for years. Clues from human cases and studies using animal models strongly suggest that much of the disease and pathology induced by alphavirus infection, particularly atypical and chronic manifestations, is mediated by the immune system rather than directly by the virus. This review discusses the current understanding of the immunopathogenesis of the arthritogenic and neurotropic alphaviruses accumulated through both natural infection of humans and experimental infection of animals, particularly mice. As treatment following alphavirus infection is currently limited to supportive care, understanding the contribution of the immune system to the disease process is critical to developing safe and effective therapies.","PeriodicalId":50977,"journal":{"name":"Advances in Virus Research","volume":"107 ","pages":"315-382"},"PeriodicalIF":0.0,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/bs.aivir.2020.06.002","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38191548","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 17

Host protein chaperones, RNA helicases and the ubiquitin network highlight the arms race for resources between tombusviruses and their hosts. 宿主蛋白伴侣、RNA解旋酶和泛素网络凸显了tombusvirus与其宿主之间资源的军备竞赛。

2区医学

Advances in Virus Research Pub Date : 2020-01-01 Epub Date: 2020-07-07 DOI: 10.1016/bs.aivir.2020.06.006

Peter D Nagy

{"title":"Host protein chaperones, RNA helicases and the ubiquitin network highlight the arms race for resources between tombusviruses and their hosts.","authors":"Peter D Nagy","doi":"10.1016/bs.aivir.2020.06.006","DOIUrl":"https://doi.org/10.1016/bs.aivir.2020.06.006","url":null,"abstract":"Positive-strand RNA viruses need to arrogate many cellular resources to support their replication and infection cycles. These viruses co-opt host factors, lipids and subcellular membranes and exploit cellular metabolites to built viral replication organelles in infected cells. However, the host cells have their defensive arsenal of factors to protect themselves from easy exploitation by viruses. In this review, the author discusses an emerging arms race for cellular resources between viruses and hosts, which occur during the early events of virus-host interactions. Recent findings with tomato bushy stunt virus and its hosts revealed that the need of the virus to exploit and co-opt given members of protein families provides an opportunity for the host to deploy additional members of the same or associated protein family to interfere with virus replication. Three examples with well-established heat shock protein 70 and RNA helicase protein families and the ubiquitin network will be described to illustrate this model on the early arms race for cellular resources between tombusviruses and their hosts. We predict that arms race for resources with additional cellular protein families will be discovered with tombusviruses. These advances will fortify research on interactions among other plant and animal viruses and their hosts.","PeriodicalId":50977,"journal":{"name":"Advances in Virus Research","volume":"107 ","pages":"133-158"},"PeriodicalIF":0.0,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/bs.aivir.2020.06.006","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38192137","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 10

From foes to friends: Viral infections expand the limits of host phenotypic plasticity. 从敌人到朋友:病毒感染扩大了宿主表型可塑性的极限。

2区医学

Advances in Virus Research Pub Date : 2020-01-01 Epub Date: 2020-01-27 DOI: 10.1016/bs.aivir.2020.01.003

Rubén González, Anamarija Butković, Santiago F Elena

{"title":"From foes to friends: Viral infections expand the limits of host phenotypic plasticity.","authors":"Rubén González, Anamarija Butković, Santiago F Elena","doi":"10.1016/bs.aivir.2020.01.003","DOIUrl":"https://doi.org/10.1016/bs.aivir.2020.01.003","url":null,"abstract":"Phenotypic plasticity enables organisms to survive in the face of unpredictable environmental stress. Intimately related to the notion of phenotypic plasticity is the concept of the reaction norm that places phenotypic plasticity in the context of a genotype-specific response to environmental gradients. Whether reaction norms themselves evolve and which factors might affect their shape has been the object of intense debates among evolutionary biologists along the years. Since their discovery, viruses have been considered as pathogens. However, new viromic techniques and a shift in conceptual paradigms are showing that viruses are mostly non-pathogenic ubiquitous entities. Recent studies have shown how viral infections can even be beneficial for their hosts. This may happen especially in the context of stressed hosts, where the virus infection can induce beneficial changes in the host's physiological homeostasis, hence changing the shape of the reaction norm. Despite the fact that underlying physiological mechanisms and evolutionary dynamics are still not well understood, such beneficial interactions are being discovered in a growing number of plant-virus systems. Here, we aim to review these disperse studies and place them into the context of phenotypic plasticity and the evolution of reaction norms. This is an emerging field that is posing many questions that still need to be properly answered. The answers would clearly interest virologists, plant pathologists and evolutionary biologists and likely they will suggest possible future biotechnological applications, including the development of crops with higher survival rates and yield under adverse environmental situations.","PeriodicalId":50977,"journal":{"name":"Advances in Virus Research","volume":"106 ","pages":"85-121"},"PeriodicalIF":0.0,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/bs.aivir.2020.01.003","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37866013","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 16

Virus Assembly and Exit Pathways 病毒组装和退出途径

2区医学

Advances in Virus Research Pub Date : 2020-01-01 DOI: 10.1016/s0065-3527(20)x0004-2

引用次数: 0

Potyviral coat protein and genomic RNA: A striking partnership leading virion assembly and more. 波病毒外壳蛋白和基因组RNA:引领病毒粒子组装和更多的惊人伙伴关系。

2区医学

Advances in Virus Research Pub Date : 2020-01-01 Epub Date: 2020-09-18 DOI: 10.1016/bs.aivir.2020.09.001

Sandra Martínez-Turiño, Juan Antonio García

{"title":"Potyviral coat protein and genomic RNA: A striking partnership leading virion assembly and more.","authors":"Sandra Martínez-Turiño, Juan Antonio García","doi":"10.1016/bs.aivir.2020.09.001","DOIUrl":"https://doi.org/10.1016/bs.aivir.2020.09.001","url":null,"abstract":"Potyvirus genus clusters a significant and expanding number of widely distributed plant viruses, responsible for large losses impacting most crops of economic interest. The potyviral genome is a single-stranded, linear, positive-sense RNA of around 10kb that is encapsidated in flexuous rod-shaped filaments, mostly made up of a helically arranged coat protein (CP). Beyond its structural role of protecting the viral genome, the potyviral CP is a multitasking protein intervening in practically all steps of the virus life cycle. In particular, interactions between the CP and the viral RNA must be tightly controlled to allow the correct assignment of the RNA to each of its functions through the infection process. This review attempts to bring together the most relevant available information regarding the architecture and modus operandi of potyviral CP and virus particles, highlighting significant discoveries, but also substantial gaps in the existing knowledge on mechanisms orchestrating virion assembly and disassembly. Biotechnological applications based on potyvirus nanoparticles is another important topic addressed here.","PeriodicalId":50977,"journal":{"name":"Advances in Virus Research","volume":"108 ","pages":"165-211"},"PeriodicalIF":0.0,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/bs.aivir.2020.09.001","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25593411","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 12

Structural and cellular biology of adeno-associated virus attachment and entry. 腺相关病毒附着和侵入的结构和细胞生物学。

2区医学

Advances in Virus Research Pub Date : 2020-01-01 Epub Date: 2020-02-13 DOI: 10.1016/bs.aivir.2020.01.002

James Zengel, Jan E Carette

{"title":"Structural and cellular biology of adeno-associated virus attachment and entry.","authors":"James Zengel, Jan E Carette","doi":"10.1016/bs.aivir.2020.01.002","DOIUrl":"https://doi.org/10.1016/bs.aivir.2020.01.002","url":null,"abstract":"Adeno-associated virus (AAV) is a nonenveloped, ssDNA virus in the parvovirus family, which has become one of the leading candidate vectors for human gene therapy. AAV has been studied extensively to identify host cellular factors involved in infection, as well as to identify capsid variants that confer clinically favorable transduction profiles ex vivo and in vivo. Recent advances in technology have allowed for direct genetic approaches to be used to more comprehensively characterize host factors required for AAV infection and allowed for identification of a critical multi-serotype receptor, adeno-associated virus receptor (AAVR). In this chapter, we will discuss the interactions of AAV with its glycan and proteinaceous receptors and describe the host and viral components involved in AAV entry, which requires cellular attachment, endocytosis, trafficking to the trans-Golgi network and nuclear import. AAV serves as a paradigm for entry of nonenveloped viruses. Furthermore, we will discuss the potential of utilizing our increased understanding of virus-host interactions during AAV entry to develop better AAV-based therapeutics, with a focus on host factors and capsid interactions involved in in vivo tropism.","PeriodicalId":50977,"journal":{"name":"Advances in Virus Research","volume":"106 ","pages":"39-84"},"PeriodicalIF":0.0,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/bs.aivir.2020.01.002","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37866012","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 14

Preface. 前言。

2区医学

Advances in Virus Research Pub Date : 2020-01-01 DOI: 10.1016/S0065-3527(20)30034-8

John P Carr, Marilyn J Roossinck

引用次数: 0

Influenza A virus uncoating. 甲型流感病毒脱落。

2区医学

Advances in Virus Research Pub Date : 2020-01-01 Epub Date: 2020-02-13 DOI: 10.1016/bs.aivir.2020.01.001

Yohei Yamauchi

{"title":"Influenza A virus uncoating.","authors":"Yohei Yamauchi","doi":"10.1016/bs.aivir.2020.01.001","DOIUrl":"https://doi.org/10.1016/bs.aivir.2020.01.001","url":null,"abstract":"Influenza A virus (IAV) is an enveloped virus of the Orthomyxoviridae with a negative-sense single-stranded RNA genome. During virus cell entry, viral and cellular cues are delivered in a stepwise manner within two distinct cellular compartments-the endosomes and the cytosol. Endosome maturation primes the viral core for uncoating by cytosolic host proteins and host-mediated virus disaggregation is essential for genome import and replication in the nucleus. Recent evidence shows that two well-known cellular proteins-histone deacetylase 6 (HDAC6) and karyopherin-β2 (kapβ2)-uncoat influenza virus. HDAC6 is 1 of 11 HDACs and an X-linked, cytosolic lysine deacetylase. Under normal cellular conditions HDAC6 is the tubulin deacetylase. Under proteasomal stress HDAC6 binds unanchored ubiquitin, dynein and myosin II to sequester misfolded protein aggregates for autophagy. Kapβ2 is a member of the importin β family that transports RNA-binding proteins into the nucleus by binding to disordered nuclear localization signals (NLSs) known as PY-NLS. Kapβ2 is emerging as a universal uncoating factor for IAV and human immunodeficiency virus type 1 (HIV-1). Kapβ2 can also reverse liquid-liquid phase separation (LLPS) of RNA-binding proteins by promoting their disaggregation. Thus, it is becoming evident that key players in the management of cellular condensates and membraneless organelles are potent virus uncoating factors. This emerging concept reveals implications in viral pathogenesis, as well as, the promise for cell-targeted therapeutic strategies to block universal virus uncoating pathways hijacked by enveloped RNA viruses.","PeriodicalId":50977,"journal":{"name":"Advances in Virus Research","volume":"106 ","pages":"1-38"},"PeriodicalIF":0.0,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/bs.aivir.2020.01.001","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37866088","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 21