Endocytosis of adenovirus and adenovirus capsid proteins

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

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 [...]

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

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.

scholarly journals Nonstructural Protein NP1 of Human Bocavirus 1 Plays a Critical Role in the Expression of Viral Capsid Proteins

2016 ◽  
Vol 90 (9) ◽  
pp. 4658-4669 ◽  
Author(s):  
Wei Zou ◽  
Fang Cheng ◽  
Weiran Shen ◽  
John F. Engelhardt ◽  
Ziying Yan ◽  
...  
Keyword(s):  
Cystic Fibrosis ◽  
Capsid Protein ◽  
Nonstructural Protein ◽  
Critical Role ◽  
The Other ◽  
Capsid Proteins ◽  
Viral Capsid ◽  
Human Bocavirus ◽  
Human Airway ◽  
Viral Capsid Proteins

ABSTRACTA novel chimeric parvoviral vector, rAAV2/HBoV1, in which the recombinant adeno-associated virus 2 (rAAV2) genome is pseudopackaged by the human bocavirus 1 (HBoV1) capsid, has been shown to be highly efficient in gene delivery to human airway epithelia (Z. Yan et al., Mol Ther 21:2181–2194, 2013,http://dx.doi.org/10.1038/mt.2013.92). In this vector production system, we used an HBoV1 packaging plasmid, pHBoV1NSCap, that harbors HBoV1 nonstructural protein (NS) and capsid protein (Cap) genes. In order to simplify this packaging plasmid, we investigated the involvement of the HBoV1 NS proteins in capsid protein expression. We found that NP1, a small NS protein encoded by the middle open reading frame, is required for the expression of the viral capsid proteins (VP1, VP2, and VP3). We also found that the other NS proteins (NS1, NS2, NS3, and NS4) are not required for the expression of VP proteins. We performed systematic analyses of the HBoV1 mRNAs transcribed from the pHBoV1NSCap packaging plasmid and its derivatives in HEK 293 cells. Mechanistically, we found that NP1 is required for both the splicing and the read-through of the proximal polyadenylation site of the HBoV1 precursor mRNA, essential functions for the maturation of capsid protein-encoding mRNA. Thus, our study provides a unique example of how a small viral nonstructural protein facilitates the multifaceted regulation of capsid gene expression.IMPORTANCEA novel chimeric parvoviral vector, rAAV2/HBoV1, expressing a full-length cystic fibrosis transmembrane conductance regulator (CFTR) gene, is capable of correcting CFTR-dependent chloride transport in cystic fibrosis human airway epithelium. Previously, an HBoV1 nonstructural and capsid protein-expressing plasmid, pHBoV1NSCap, was used to package the rAAV2/HBoV1 vector, but yields remained low. In this study, we demonstrated that the nonstructural protein NP1 is required for the expression of capsid proteins. However, we found that the other four nonstructural proteins (NS1 to -4) are not required for expression of capsid proteins. By mutating theciselements that function as internal polyadenylation signals in the capsid protein-expressing mRNA, we constructed a simple HBoV1 capsid protein-expressing gene that expresses capsid proteins as efficiently as pHBoV1NSCap does, and at similar ratios, but independently of NP1. Our study provides a foundation to develop a better packaging system for rAAV2/HBoV1 vector production.

A dose-response study in mice of a tetravalent vaccine candidate composed of domain III-capsid proteins from dengue viruses

2017 ◽  
Vol 162 (8) ◽  
pp. 2247-2256 ◽  
Author(s):  
Iris Valdés ◽  
Ernesto Marcos ◽  
Edith Suzarte ◽  
Yusleidi Pérez ◽  
Enma Brown ◽  
...  
Keyword(s):  
Dose Response ◽  
Vaccine Candidate ◽  
Capsid Proteins ◽  
Dengue Viruses ◽  
Tetravalent Vaccine ◽  
Domain Iii ◽  
Dose Response Study
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