Norovirus Capsid Proteins Self-Assemble through Biphasic Kinetics via Long-Lived Stave-like Intermediates

2013 ◽  
Vol 135 (41) ◽  
pp. 15373-15381 ◽  
Author(s):  
Guillaume Tresset ◽  
Clémence Le Coeur ◽  
Jean-François Bryche ◽  
Mouna Tatou ◽  
Mehdi Zeghal ◽  
...  
Keyword(s):  
Capsid Proteins ◽  
Biphasic Kinetics

The concentration of Ca2+ that solubilizes outer capsid proteins from rotavirus particles is dependent on the strain.

1996 ◽  
Vol 70 (8) ◽  
pp. 4877-4883 ◽  
Author(s):  
M C Ruiz ◽  
A Charpilienne ◽  
F Liprandi ◽  
R Gajardo ◽  
F Michelangeli ◽  
...  
Keyword(s):  
Capsid Proteins ◽  
Outer Capsid

scholarly journals Asymmetric reconstruction of mammalian reovirus reveals interactions among RNA, transcriptional factor µ2 and capsid proteins

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Muchen Pan ◽  
Ana L. Alvarez-Cabrera ◽  
Joon S. Kang ◽  
Lihua Wang ◽  
Chunhai Fan ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Molecular Interactions ◽  
Messenger Rna ◽  
Rna Binding ◽  
Capsid Proteins ◽  
Rna Transcription ◽  
Infectious Particle ◽  
Virion Assembly ◽  
Rna Capping

AbstractMammalian reovirus (MRV) is the prototypical member of genus Orthoreovirus of family Reoviridae. However, lacking high-resolution structures of its RNA polymerase cofactor μ2 and infectious particle, limits understanding of molecular interactions among proteins and RNA, and their contributions to virion assembly and RNA transcription. Here, we report the 3.3 Å-resolution asymmetric reconstruction of transcribing MRV and in situ atomic models of its capsid proteins, the asymmetrically attached RNA-dependent RNA polymerase (RdRp) λ3, and RdRp-bound nucleoside triphosphatase μ2 with a unique RNA-binding domain. We reveal molecular interactions among virion proteins and genomic and messenger RNA. Polymerase complexes in three Spinoreovirinae subfamily members are organized with different pseudo-D3d symmetries to engage their highly diversified genomes. The above interactions and those between symmetry-mismatched receptor-binding σ1 trimers and RNA-capping λ2 pentamers balance competing needs of capsid assembly, external protein removal, and allosteric triggering of endogenous RNA transcription, before, during and after infection, respectively.

scholarly journals Rotaviruses and Rotavirus Vaccines

Pathogens ◽  
2021 ◽  
Vol 10 (8) ◽  
pp. 959
Author(s):  
Celeste M. Donato ◽  
Julie E. Bines
Keyword(s):  
Capsid Proteins ◽  
Virus Family ◽  
Rotavirus Vaccines ◽  
Group A Rotaviruses ◽  
Group A ◽  
Outer Capsid

Group A rotaviruses belong to the Reoviridae virus family and are classified into G and P genotypes based on the outer capsid proteins VP7 and VP4, respectively [...]

scholarly journals Identification of a DNA binding domain in simian virus 40 capsid proteins Vp2 and Vp3.

1993 ◽  
Vol 268 (28) ◽  
pp. 20877-20883
Author(s):  
J Clever ◽  
D.A. Dean ◽  
H Kasamatsu
Keyword(s):  
Dna Binding ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
Binding Domain ◽  
Capsid Proteins ◽  
Dna Binding Domain

Immunogenicity of a DNA vaccine for coxsackievirus B3 in mice: protective effects of capsid proteins against viral challenge

Vaccine ◽  
2005 ◽  
Vol 23 (14) ◽  
pp. 1672-1679 ◽  
Author(s):  
Joo-Young Kim ◽  
Eun-Seok Jeon ◽  
Byung-Kwan Lim ◽  
Sun-Mi Kim ◽  
Sun-Ku Chung ◽  
...  
Keyword(s):  
Dna Vaccine ◽  
Coxsackievirus B3 ◽  
Capsid Proteins ◽  
Protective Effects ◽  
Viral Challenge

Endocytosis of adenovirus and adenovirus capsid proteins

2003 ◽  
Vol 55 (11) ◽  
pp. 1485-1496 ◽  
Author(s):  
Lali K. Medina-Kauwe
Keyword(s):  
Capsid Proteins

scholarly journals Capsid Proteins of Cowpea Mosaic Virus Transiently Expressed in Protoplasts Form Virus-like Particles

Virology ◽  
1996 ◽  
Vol 224 (1) ◽  
pp. 352-355 ◽  
Author(s):  
Joan Wellink ◽  
Jan Verver ◽  
Jan Van Lent ◽  
A.Van Kammen
Keyword(s):  
Mosaic Virus ◽  
Capsid Proteins ◽  
Cowpea Mosaic Virus ◽  
Virus Like Particles

scholarly journals NMR Experiments Shed New Light on Glycan Recognition by Human and Murine Norovirus Capsid Proteins

Viruses ◽  
2021 ◽  
Vol 13 (3) ◽  
pp. 416
Author(s):  
Robert Creutznacher ◽  
Thorben Maass ◽  
Patrick Ogrissek ◽  
Georg Wallmann ◽  
Clara Feldmann ◽  
...  
Keyword(s):  
Blood Group ◽  
Protein Interactions ◽  
Capsid Proteins ◽  
Blood Group Antigens ◽  
Biological Processes ◽  
Murine Norovirus ◽  
Human Norovirus ◽  
Head Groups ◽  
Significant Difference

Glycan–protein interactions are highly specific yet transient, rendering glycans ideal recognition signals in a variety of biological processes. In human norovirus (HuNoV) infection, histo-blood group antigens (HBGAs) play an essential but poorly understood role. For murine norovirus infection (MNV), sialylated glycolipids or glycoproteins appear to be important. It has also been suggested that HuNoV capsid proteins bind to sialylated ganglioside head groups. Here, we study the binding of HBGAs and sialoglycans to HuNoV and MNV capsid proteins using NMR experiments. Surprisingly, the experiments show that none of the norovirus P-domains bind to sialoglycans. Notably, MNV P-domains do not bind to any of the glycans studied, and MNV-1 infection of cells deficient in surface sialoglycans shows no significant difference compared to cells expressing respective glycans. These findings redefine glycan recognition by noroviruses, challenging present models of infection.

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