Enterovirus 2C Protein Suppresses IKKα Phosphorylation by Recruiting IKKβ and IKKα into Viral Inclusion Bodies

2020 ◽  
Author(s):  
Lianfu Ji ◽  
Enhui Yang ◽  
Susu He ◽  
Yu Jin ◽  
Deyan Chen
Keyword(s):  
Inclusion Bodies ◽  
Viral Inclusion

High Voltage Electron Microscopy of Viral Inclusion Bodies

1980 ◽  
Vol 38 ◽  
pp. 486-487 ◽  
Author(s):  
H.M. Mazzone ◽  
W.F. Engler ◽  
G. Wray ◽  
A. Szirmae ◽  
J. Conroy ◽  
...  
Keyword(s):  
New York ◽  
Environmental Protection Agency ◽  
Inclusion Bodies ◽  
Host Cells ◽  
High Voltage Electron Microscopy ◽  
Voltage Electron ◽  
Viral Particles ◽  
Pest Insects ◽  
Viral Inclusion ◽  
Insect Gut

Viral inclusion bodies isolated from infected pest insects are being evaluated by the U.S. Dept. of Agriculture as biological insecticides against their hosts. Our research on these inclusion bodies constitutes part of an effort to support their approval by the Environmental Protection Agency as insect control agents. The inclusion bodies in this study are polyhedral in shape and contain rod-shaped viral particles. When ingested by pest insects, the inclusion bodies are broken down in the insect gut and release the viral particles which infect and multiply in the nuclei of host cells. These viruses are termed nucleopolyhedrosis viruses (NPV) and are representatives of the baculoviruses (Wildy, P. 1971 IN J.L. Melnick, ed., Monographs in Virology, vol. 5, S.Karger, New York).

Purification and Immunological Analyses of Plant Viral Inclusion Bodies

1984 ◽  
pp. 225-280 ◽  
Author(s):  
Ernest Hiebert ◽  
Dan E. Purcifull ◽  
Richard G. Christie
Keyword(s):  
Inclusion Bodies ◽  
Viral Inclusion

scholarly journals Measles Virus Forms Inclusion Bodies with Properties of Liquid Organelles

2019 ◽  
Vol 93 (21) ◽  
Author(s):  
Yuqin Zhou ◽  
Justin M. Su ◽  
Charles E. Samuel ◽  
Dzwokai Ma
Keyword(s):  
Phase Separation ◽  
Liquid Phase ◽  
Virus Replication ◽  
Inclusion Bodies ◽  
Measles Virus ◽  
Rna Replication ◽  
Infected Cells ◽  
Viral Inclusion ◽  
P Proteins ◽  
Liquid Liquid Phase Separation

ABSTRACT Nonsegmented negative-strand RNA viruses, including measles virus (MeV), a member of the Paramyxoviridae family, are assumed to replicate in cytoplasmic inclusion bodies. These cytoplasmic viral factories are not membrane bound, and they serve to concentrate the viral RNA replication machinery. Although inclusion bodies are a prominent feature in MeV-infected cells, their biogenesis and regulation are not well understood. Here, we show that infection with MeV triggers inclusion body formation via liquid-liquid phase separation (LLPS), a process underlying the formation of membraneless organelles. We find that the viral nucleoprotein (N) and phosphoprotein (P) are sufficient to trigger MeV phase separation, with the C-terminal domains of the viral N and P proteins playing a critical role in the phase transition. We provide evidence suggesting that the phosphorylation of P and dynein-mediated transport facilitate the growth of these organelles, implying that they may have key regulatory roles in the biophysical assembly process. In addition, our findings support the notion that these inclusions change from liquid to gel-like structures as a function of time after infection, leaving open the intriguing possibility that the dynamics of these organelles can be tuned during infection to optimally suit the changing needs during the viral replication cycle. Our study provides novel insight into the process of formation of viral inclusion factories, and taken together with earlier studies, suggests that Mononegavirales have broadly evolved to utilize LLPS as a common strategy to assemble cytoplasmic replication factories in infected cells. IMPORTANCE Measles virus remains a pathogen of significant global concern. Despite an effective vaccine, outbreaks continue to occur, and globally ∼100,000 measles-related deaths are seen annually. Understanding the molecular basis of virus-host interactions that impact the efficiency of virus replication is essential for the further development of prophylactic and therapeutic strategies. Measles virus replication occurs in the cytoplasm in association with discrete bodies, though little is known of the nature of the inclusion body structures. We recently established that the cellular protein WD repeat-containing protein 5 (WDR5) enhances MeV growth and is enriched in cytoplasmic viral inclusion bodies that include viral proteins responsible for RNA replication. Here, we show that MeV N and P proteins are sufficient to trigger the formation of WDR5-containing inclusion bodies, that these structures display properties characteristic of phase-separated liquid organelles, and that P phosphorylation together with the host dynein motor affect the efficiency of the liquid-liquid phase separation process.

scholarly journals Aquareovirus NS80 Initiates Efficient Viral Replication by Retaining Core Proteins within Replication-Associated Viral Inclusion Bodies

PLoS ONE ◽  
2015 ◽  
Vol 10 (5) ◽  
pp. e0126127 ◽  
Author(s):  
Liming Yan ◽  
Jie Zhang ◽  
Hong Guo ◽  
Shicui Yan ◽  
Qingxiu Chen ◽  
...  
Keyword(s):  
Viral Replication ◽  
Inclusion Bodies ◽  
Core Proteins ◽  
Viral Inclusion ◽  
Efficient Viral Replication

scholarly journals Evasion of Antiviral Immunity through Sequestering of TBK1/IKK /IRF3 into Viral Inclusion Bodies

2013 ◽  
Vol 88 (6) ◽  
pp. 3067-3076 ◽  
Author(s):  
X. Wu ◽  
X. Qi ◽  
B. Qu ◽  
Z. Zhang ◽  
M. Liang ◽  
...  
Keyword(s):  
Inclusion Bodies ◽  
Antiviral Immunity ◽  
Viral Inclusion

scholarly journals Phosphorylation of Bluetongue Virus Nonstructural Protein 2 Is Essential for Formation of Viral Inclusion Bodies

2005 ◽  
Vol 79 (15) ◽  
pp. 10023-10031 ◽  
Author(s):  
Jens Modrof ◽  
Kostas Lymperopoulos ◽  
Polly Roy
Keyword(s):  
Bluetongue Virus ◽  
Inclusion Bodies ◽  
Rna Binding ◽  
Nonstructural Protein ◽  
Binding Activity ◽  
Nonstructural Protein 2 ◽  
The Matrix ◽  
Infected Cells ◽  
Viral Inclusion

ABSTRACT In bluetongue virus (BTV)-infected cells, large cytoplasmic aggregates are formed, termed viral inclusion bodies (VIBs), which are believed to be the sites of viral replication and morphogenesis. The BTV nonstructural protein NS2 is the major component of VIBs. NS2 undergoes intracellular phosphorylation and possesses a strong single-stranded RNA binding activity. By changing phosphorylated amino acids to alanines and aspartates, we have mapped the phosphorylated sites of NS2 to two serine residues at positions 249 and 259. Since both of these serines are within the context of protein kinase CK2 recognition signals, we have further examined if CK2 is involved in NS2 phosphorylation by both intracellular colocalization and an in vitro phosphorylation assay. In addition, we have utilized the NS2 mutants to determine the role of phosphorylation on NS2 activities. The data obtained demonstrate that NS2 phosphorylation is not necessary either for its RNA binding properties or for its ability to interact with the viral polymerase VP1. However, phosphorylated NS2 exhibited VIB formation while unmodified NS2 failed to assemble as VIBs although smaller oligomeric forms of NS2 were readily formed. Our data reveal that NS2 phosphorylation controls VIBs formation consistent with a model in which NS2 provides the matrix for viral assembly.

scholarly journals DEMONSTRATION OF VIRAL INCLUSION BODIES IN UNSTAINED TISSUE SECTIONS WITH THE AID OF THE PHASE MICROSCOPE I.

1949 ◽  
Vol 57 (3) ◽  
pp. 297-303 ◽  
Author(s):  
Juan J. Angulo ◽  
Oscar W. Richards ◽  
Agustin L. Roque
Keyword(s):  
Inclusion Bodies ◽  
Tissue Sections ◽  
Viral Inclusion

scholarly journals Gastrointestinal Pathogenicity of Adenoviruses and Reoviruses Isolated from Broiler Chickens in Alabama

1998 ◽  
Vol 10 (2) ◽  
pp. 145-151 ◽  
Author(s):  
Stephen D. Lenz ◽  
Frederic J. Hoerr ◽  
Alfred C. Ellis ◽  
Maria A. Toivio-Kinnucan ◽  
Maria Yu
Keyword(s):  
Inclusion Bodies ◽  
Broiler Chickens ◽  
Digestive System ◽  
Necrotizing Pancreatitis ◽  
Bursa Of Fabricius ◽  
Pancreatic Acinar Cells ◽  
Control Group ◽  
Specific Pathogen ◽  
Commercial Broiler ◽  
Viral Inclusion

Adenoviruses and reoviruses isolated from commercial broiler chickens were evaluated for gastrointestinal pathogenicity in specific-pathogen-free Leghorn chickens. The viruses were originally isolated from either the proventriculus or a gastrointestinal pool of tissues of broiler chickens with proventriculitis or enteritis. Isolates were cloned by terminal dilution. Day-old chickens were inoculated by oral and ocular routes with undiluted tissue culture fluids (titers of 102-104 TCID50/ml) and then examined at necropsy on days 5, 10, and 15 postinoculation. Chickens in all virus groups (but not the control group) developed wet, unformed fecal droppings that persisted for the duration of the study. Mild lesions occurred in reovirus-inoculated chickens and included hyperplasia of lymphocyte aggregates in various organs and mild gizzard erosions. Chickens inoculated with adenovirus isolates developed marked gizzard erosions and necrotizing pancreatitis as well as mild proventriculitis. Intranuclear viral inclusion bodies occurred in gizzard epithelium and pancreatic acinar cells at the sites of lesions. Lymphocytic atrophy occurred in the bursa of Fabricius. Respective viruses were reisolated from proventriculus and duodenum collected from chickens of each group; no viruses were isolated from controls. Under the conditions of this study, adenovirus isolates were more pathogenic than the reovirus isolates in the digestive system.

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