scholarly journals Laminin receptor is an interacting partner for viral outer capsid protein VP5 in grass carp reovirus infection

Virology ◽  
2016 ◽  
Vol 490 ◽  
pp. 59-68 ◽  
Author(s):  
Hao Wang ◽  
Fei Yu ◽  
Jiale Li ◽  
Liqun Lu
Keyword(s):  
Capsid Protein ◽  
Grass Carp ◽  
Laminin Receptor ◽  
Outer Capsid Protein ◽  
Grass Carp Reovirus ◽  
Reovirus Infection ◽  
Outer Capsid

scholarly journals Grass Carp Reovirus VP56 Allies VP4, Recruits, Blocks, and Degrades RIG-I to More Effectively Attenuate IFN Responses and Facilitate Viral Evasion

2021 ◽  
Author(s):  
Hang Su ◽  
Zhiwei Liao ◽  
Chunrong Yang ◽  
Yongan Zhang ◽  
Jianguo Su
Keyword(s):  
Capsid Protein ◽  
Outer Surface ◽  
Grass Carp ◽  
Cell Attachment ◽  
Outer Capsid Protein ◽  
Grass Carp Reovirus ◽  
Black Carp ◽  
Reovirus Infection ◽  
Outer Capsid ◽  
Viral Evasion

Grass carp reovirus (GCRV) fibrin VP56 and major outer capsid protein VP4 inlay and locate on the outer surface of GCRV-II and GCRV-III, which causes tremendous loss in grass carp and black carp industries. Fibrin is involved in cell attachment and plays an important role in reovirus infection.

Development and efficacy of a grass carp reovirus (GCRV) outer capsid protein VP7 subunit vaccine

2012 ◽  
Vol 37 (6) ◽  
pp. 659-664 ◽  
Author(s):  
Shi-ying XU ◽  
Jing-hui LI ◽  
Yong ZOU ◽  
Lin LIU ◽  
Cheng-liang GONG ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Grass Carp ◽  
Subunit Vaccine ◽  
Outer Capsid Protein ◽  
Grass Carp Reovirus ◽  
Outer Capsid

scholarly journals Grass Carp Reovirus Major Outer Capsid Protein VP4 Interacts with RNA Sensor RIG-I to Suppress Interferon Response

Biomolecules ◽  
2020 ◽  
Vol 10 (4) ◽  
pp. 560
Author(s):  
Hang Su ◽  
Chengjian Fan ◽  
Zhiwei Liao ◽  
Chunrong Yang ◽  
Jihong Liu Clarke ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Grass Carp ◽  
Cytopathic Effect ◽  
Interferon Response ◽  
Molecular Function ◽  
Outer Capsid Protein ◽  
Grass Carp Reovirus ◽  
Outer Capsid ◽  
Production Industry ◽  
Insight Into

Diseases caused by viruses threaten the production industry and food safety of aquaculture which is a great animal protein source. Grass carp reovirus (GCRV) has caused tremendous loss, and the molecular function of viral proteins during infection needs further research, as for most aquatic viruses. In this study, interaction between GCRV major outer capsid protein VP4 and RIG-I, a critical viral RNA sensor, was screened out by GST pull-down, endogenous immunoprecipitation and subsequent LC-MS/MS, and then verified by co-IP and an advanced far-red fluorescence complementation system. VP4 was proved to bind to the CARD and RD domains of RIG-I and promoted K48-linked ubiquitination of RIG-I to degrade RIG-I. VP4 reduced mRNA and promoter activities of key genes of RLR pathway and sequential IFN production. As a consequence, antiviral effectors were suppressed and GCRV replication increased, resulting in intensified cytopathic effect. Furthermore, results of transcriptome sequencing of VP4 stably expressed CIK (C. idella kidney) cells indicated that VP4 activated the MyD88-dependent TLR pathway. Knockdown of VP4 obtained opposite effects. These results collectively revealed that VP4 interacts with RIG-I to restrain interferon response and assist GCRV invasion. This study lays the foundation for anti-dsRNA virus molecular function research in teleost and provides a novel insight into the strategy of immune evasion for aquatic virus.

Expression of outer capsid protein VP5 of grass carp reovirus in E.coli and analysis of its immunogenicity

2009 ◽  
Vol 24 (6) ◽  
pp. 545-551 ◽  
Author(s):  
Lan-lan Zhang ◽  
Jin-yu Shen ◽  
Cheng-feng Lei ◽  
Chao Fan ◽  
Gui-jie Hao ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Grass Carp ◽  
Outer Capsid Protein ◽  
Grass Carp Reovirus ◽  
Outer Capsid

scholarly journals Reovirus Infection or Ectopic Expression of Outer Capsid Protein  1 Induces Apoptosis Independently of the Cellular Proapoptotic Proteins Bax and Bak

2010 ◽  
Vol 85 (1) ◽  
pp. 296-304 ◽  
Author(s):  
M. L. Wisniewski ◽  
B. G. Werner ◽  
L. G. Hom ◽  
L. J. Anguish ◽  
C. M. Coffey ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Ectopic Expression ◽  
Outer Capsid Protein ◽  
Reovirus Infection ◽  
Outer Capsid

scholarly journals Structure of the Three N-Terminal Immunoglobulin Domains of the Highly Immunogenic Outer Capsid Protein from a T4-Like Bacteriophage

2011 ◽  
Vol 85 (16) ◽  
pp. 8141-8148 ◽  
Author(s):  
A. Fokine ◽  
M. Z. Islam ◽  
Z. Zhang ◽  
V. D. Bowman ◽  
V. B. Rao ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Outer Capsid Protein ◽  
Outer Capsid

Targeting Heat Shock Protein 70 as an antiviral strategy against grass carp reovirus infection

2018 ◽  
Vol 247 ◽  
pp. 1-9 ◽  
Author(s):  
Li-Peng Shan ◽  
Xiao-Hui Chen ◽  
Fei Ling ◽  
Bin Zhu ◽  
Gao-Xue Wang
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Grass Carp ◽  
Heat Shock Protein 70 ◽  
Grass Carp Reovirus ◽  
Reovirus Infection

scholarly journals Cryo-EM structure of the bacteriophage T4 isometric head at 3.3-Å resolution and its relevance to the assembly of icosahedral viruses

2017 ◽  
Vol 114 (39) ◽  
pp. E8184-E8193 ◽  
Author(s):  
Zhenguo Chen ◽  
Lei Sun ◽  
Zhihong Zhang ◽  
Andrei Fokine ◽  
Victor Padilla-Sanchez ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Major Capsid Protein ◽  
Bacteriophage T4 ◽  
Hexagonal Lattice ◽  
Scaffolding Proteins ◽  
Outer Capsid Protein ◽  
Head Assembly ◽  
Icosahedral Viruses ◽  
End Caps ◽  
Outer Capsid

The 3.3-Å cryo-EM structure of the 860-Å-diameter isometric mutant bacteriophage T4 capsid has been determined. WT T4 has a prolate capsid characterized by triangulation numbers (T numbers) Tend= 13 for end caps and Tmid= 20 for midsection. A mutation in the major capsid protein, gp23, produced T=13 icosahedral capsids. The capsid is stabilized by 660 copies of the outer capsid protein, Soc, which clamp adjacent gp23 hexamers. The occupancies of Soc molecules are proportional to the size of the angle between the planes of adjacent hexameric capsomers. The angle between adjacent hexameric capsomers is greatest around the fivefold vertices, where there is the largest deviation from a planar hexagonal array. Thus, the Soc molecules reinforce the structure where there is the greatest strain in the gp23 hexagonal lattice. Mutations that change the angles between adjacent capsomers affect the positions of the pentameric vertices, resulting in different triangulation numbers in bacteriophage T4. The analysis of the T4 mutant head assembly gives guidance to how other icosahedral viruses reproducibly assemble into capsids with a predetermined T number, although the influence of scaffolding proteins is also important.

scholarly journals Putative Autocleavage of Outer Capsid Protein μ1, Allowing Release of Myristoylated Peptide μ1N during Particle Uncoating, Is Critical for Cell Entry by Reovirus

2004 ◽  
Vol 78 (16) ◽  
pp. 8732-8745 ◽  
Author(s):  
Amy L. Odegard ◽  
Kartik Chandran ◽  
Xing Zhang ◽  
John S. L. Parker ◽  
Timothy S. Baker ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Structural Changes ◽  
General Mechanism ◽  
Membrane Penetration ◽  
Outer Capsid Protein ◽  
Core Proteins ◽  
Peptide Release ◽  
Outer Capsid

ABSTRACT Several nonenveloped animal viruses possess an autolytic capsid protein that is cleaved as a maturation step during assembly to yield infectious virions. The 76-kDa major outer capsid protein μ1 of mammalian orthoreoviruses (reoviruses) is also thought to be autocatalytically cleaved, yielding the virion-associated fragments μ1N (4 kDa; myristoylated) and μ1C (72 kDa). In this study, we found that μ1 cleavage to yield μ1N and μ1C was not required for outer capsid assembly but contributed greatly to the infectivity of the assembled particles. Recoated particles containing mutant, cleavage-defective μ1 (asparagine → alanine substitution at amino acid 42) were competent for attachment; processing by exogenous proteases; structural changes in the outer capsid, including μ1 conformational change and σ1 release; and transcriptase activation but failed to mediate membrane permeabilization either in vitro (no hemolysis) or in vivo (no coentry of the ribonucleotoxin α-sarcin). In addition, after these particles were allowed to enter cells, the δ region of μ1 continued to colocalize with viral core proteins in punctate structures, indicating that both elements remained bound together in particles and/or trapped within the same subcellular compartments, consistent with a defect in membrane penetration. If membrane penetration activity was supplied in trans by a coinfecting genome-deficient particle, the recoated particles with cleavage-defective μ1 displayed much higher levels of infectivity. These findings led us to propose a new uncoating intermediate, at which particles are trapped in the absence of μ1N/μ1C cleavage. We additionally showed that this cleavage allowed the myristoylated, N-terminal μ1N fragment to be released from reovirus particles during entry-related uncoating, analogous to the myristoylated, N-terminal VP4 fragment of picornavirus capsid proteins. The results thus suggest that hydrophobic peptide release following capsid protein autocleavage is part of a general mechanism of membrane penetration shared by several diverse nonenveloped animal viruses.

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