scholarly journals Intracellular Hepadnavirus Nucleocapsids Are Selected for Secretion by Envelope Protein-Independent Membrane Binding

2000 ◽  
Vol 74 (24) ◽  
pp. 11472-11478 ◽  
Author(s):  
Hélène Mabit ◽  
Heinz Schaller
Keyword(s):  
Envelope Protein ◽  
Core Protein ◽  
Membrane Binding ◽  
Dna Viruses ◽  
Virus Particles ◽  
Duck Hepatitis ◽  
Double Stranded Dna ◽  
Selective Membrane ◽  
Membrane Attachment ◽  
Different Populations

ABSTRACT Hepadnaviruses are DNA viruses but, as pararetroviruses, their morphogenesis initiates with the encapsidation of an RNA pregenome, and these viruses have therefore evolved mechanisms to exclude nucleocapsids that contain incompletely matured genomes from participating in budding and secretion. We provide here evidence that binding of hepadnavirus core particles from the cytosol to their target membranes is a distinct step in morphogenesis, discriminating among different populations of intracellular capsids. Using the duck hepatitis B virus (DHBV) and a flotation assay, we found about half of the intracellular capsids to be membrane associated due to an intrinsic membrane-binding affinity. In contrast to free cytosolic capsids, this subpopulation contained largely mature, double-stranded DNA genomes and lacked core protein hyperphosphorylation, both features characteristic for secreted virions. Against expectation, however, the selective membrane attachment observed did not require the presence of the large DHBV envelope protein, which has been considered to be crucial for nucleocapsid-membrane interaction. Furthermore, removal of surface-exposed phosphate residues from nonfloating capsids by itself did not suffice to confer membrane affinity and, finally, hyperphosphorylation was absent from nonenveloped nucleocapsids that were released from DHBV-transfected cells. Collectively, these observations argue for a model in which nucleocapsid maturation, involving the viral genome, capsid structure, and capsid dephosphorylation, leads to the exposure of a membrane-binding signal as a step crucial for selecting the matured nucleocapsid to be incorporated into the capsid-independent budding of virus particles.

scholarly journals Regulation of Hepadnavirus Reverse Transcription by Dynamic Nucleocapsid Phosphorylation

2006 ◽  
Vol 81 (4) ◽  
pp. 1641-1649 ◽  
Author(s):  
Suresh H. Basagoudanavar ◽  
David H. Perlman ◽  
Jianming Hu
Keyword(s):  
Dna Synthesis ◽  
Reverse Transcription ◽  
Core Protein ◽  
Early Stage ◽  
Phosphorylation Site ◽  
Duck Hepatitis ◽  
Double Stranded Dna ◽  
B Virus ◽  
Multistep Process

ABSTRACT Reverse transcription, an essential step in the life cycle of all retroelements, is a complex, multistep process whose regulation is not yet clearly understood. We have recently shown that reverse transcription in the pararetrovirus duck hepatitis B virus is associated with complete dephosphorylation of the viral core protein, which forms the nucleocapsid wherein reverse transcription takes place. Here we present a genetic study of the role of this dynamic nucleocapsid phosphorylation in regulating viral reverse transcription. Detailed analyses of the reverse transcription products synthesized within nucleocapsids composed of core phosphorylation site mutants revealed that alanine substitutions, mimicking the nonphosphorylated state, completely blocked reverse transcription at a very early stage. In contrast, aspartate substitutions, mimicking the phosphorylated state, allowed complete first-strand DNA synthesis but were severely defective in accumulating mature double-stranded DNA. The latter defect was due to a combination of mutant nucleocapsid instability during maturation and a block in mature second-strand DNA synthesis. Thus, the reversible phosphorylation of the nucleocapsids regulates the ordered progression of reverse transcription.

scholarly journals Identification of Two Virus Integration Sites in the Brown Alga Feldmannia Chromosome

2007 ◽  
Vol 82 (3) ◽  
pp. 1407-1413 ◽  
Author(s):  
Russel H. Meints ◽  
Richard G. Ivey ◽  
Amy M. Lee ◽  
Tae-Jin Choi
Keyword(s):  
Vegetative Cells ◽  
Stem Loop ◽  
Dna Viruses ◽  
Viral Genomes ◽  
Virus Particles ◽  
Double Stranded Dna ◽  
Stem Loop Structure ◽  
Integration Sites ◽  
Virus Integration ◽  
Cg Dinucleotide

ABSTRACT Two similar, large double-stranded DNA viruses, Feldmannia species virus 158 (FsV-158) and FsV-178, replicate only in the unilocular reproductive cells (sporangia) of a brown filamentous alga in the genus Feldmannia. Virus particles are not present in vegetative cells but they are produced in the sporangia formed on vegetative filaments that have been transferred newly into culture. Thus, we proposed that these viruses exist in the vegetative cells in a latent form (R. G. Ivey, E. C. Henry, A. M. Lee, L. Klepper, S. K. Krueger, and R. H. Meints, Virology 220:267-273, 1996). In this article we present evidence that the two FsV genomes are integrated into the host genome during vegetative growth. The FsV genome integration sites were identified by cloning the regions where the FsV genome is linked to the host DNA. FsV-158 and FsV-178 are integrated into two distinct locations in the algal genome. In contrast, the integration sites in the two viral genomes are identical. Notably, the integration sites in the host and viruses contain GC and CG dinucleotide sequences, respectively, from which the GC sequences are recovered at both host-virus junctions. The splice sites in the two FsV genomes are predicted to form a stem-loop structure with the CG dinucleotide in the loop portion.

scholarly journals Conformational Plasticity of Hepatitis B Core Protein Spikes Promotes Peptide Binding Independent of the Secretion Phenotype

2021 ◽  
Vol 9 (5) ◽  
pp. 956
Author(s):  
Cihan Makbul ◽  
Vladimir Khayenko ◽  
Hans Michael Maric ◽  
Bettina Böttcher
Keyword(s):  
Hepatitis B ◽  
Core Protein ◽  
Peptide Binding ◽  
Surface Proteins ◽  
Binding Motif ◽  
Virus Particles ◽  
Enveloped Virus ◽  
Conformational Plasticity ◽  
Viral Maturation ◽  
Hepatitis B Core Protein

Hepatitis B virus is a major human pathogen, which forms enveloped virus particles. During viral maturation, membrane-bound hepatitis B surface proteins package hepatitis B core protein capsids. This process is intercepted by certain peptides with an “LLGRMKG” motif that binds to the capsids at the tips of dimeric spikes. With microcalorimetry, electron cryo microscopy and peptide microarray-based screens, we have characterized the structural and thermodynamic properties of peptide binding to hepatitis B core protein capsids with different secretion phenotypes. The peptide “GSLLGRMKGA” binds weakly to hepatitis B core protein capsids and mutant capsids with a premature (F97L) or low-secretion phenotype (L60V and P5T). With electron cryo microscopy, we provide novel structures for L60V and P5T and demonstrate that binding occurs at the tips of the spikes at the dimer interface, splaying the helices apart independent of the secretion phenotype. Peptide array screening identifies “SLLGRM” as the core binding motif. This shortened motif binds only to one of the two spikes in the asymmetric unit of the capsid and induces a much smaller conformational change. Altogether, these comprehensive studies suggest that the tips of the spikes act as an autonomous binding platform that is unaffected by mutations that affect secretion phenotypes.

scholarly journals Evolution of a major virion protein of the giant pandoraviruses from an inactivated bacterial glycoside hydrolase

2020 ◽  
Vol 6 (2) ◽  
Author(s):  
Mart Krupovic ◽  
Natalya Yutin ◽  
Eugene Koonin
Keyword(s):  
Glycoside Hydrolase ◽  
Carbohydrate Binding ◽  
Virion Protein ◽  
Gene Encoding ◽  
Dna Viruses ◽  
Virus Particles ◽  
Major Increase ◽  
A Minor ◽  
Particle Shapes ◽  
Icosahedral Capsid

Abstract The diverse viruses in the phylum Nucleocytoviricota (also known as NLCDVs, Nucleo-cytoplasmic Large DNA Viruses) typically possess large icosahedral virions. However, in several families of Nucleocytoviricota, the icosahedral capsid was replaced by irregular particle shapes, most notably, the amphora-like virions of pandoraviruses and pithoviruses, the largest known virus particles in the entire virosphere. Pandoraviruses appear to be the most highly derived viruses in this phylum because their evolution involved not only the change in the virion shape, but also, the actual loss of the gene encoding double-jelly roll major capsid protein (DJR MCP), the main building block of icosahedral capsids in this virus assemblage. Instead, pandoravirus virions are built of unrelated abundant proteins. Here we show that the second most abundant virion protein of pandoraviruses, major virion protein 2 (MVP2), evolved from an inactivated derivative of a bacterial glycoside hydrolase of the GH16 family. The ancestral form of MVP2 was apparently acquired early in the evolution of the Nucleocytoviricota, to become a minor virion protein. After a duplication in the common ancestor of pandoraviruses and molliviruses, one of the paralogs displaces DJR MCP in pandoraviruses, conceivably, opening the way for a major increase in the size of the virion and the genome. Exaptation of a carbohydrate-binding protein for the function of the MVP is a general trend in virus evolution and might underlie the transformation of the virion shape in other groups of the Nucleocytoviricota as well.

scholarly journals Extrachromosomal Histone H2B Mediates Innate Antiviral Immune Responses Induced by Intracellular Double-Stranded DNA

2009 ◽  
Vol 84 (2) ◽  
pp. 822-832 ◽  
Author(s):  
Kouji Kobiyama ◽  
Fumihiko Takeshita ◽  
Nao Jounai ◽  
Asako Sakaue-Sawano ◽  
Atsushi Miyawaki ◽  
...  
Keyword(s):  
Immune Responses ◽  
Rna Virus ◽  
Cellular Signaling ◽  
Helical Structure ◽  
Human Cells ◽  
Type I Interferons ◽  
Type I ◽  
Histone H2b ◽  
Dna Viruses ◽  
Double Stranded Dna

ABSTRACT Fragments of double-stranded DNA (dsDNA) forming a right-handed helical structure (B-DNA) stimulate cells to produce type I interferons (IFNs). While an adaptor molecule, IFN-β promoter stimulator 1 (IPS-1), mediates dsDNA-induced cellular signaling in human cells, the underlying molecular mechanism is not fully understood. Here, we demonstrate that the extrachromosomal histone H2B mediates innate antiviral immune responses in human cells. H2B physically interacts with IPS-1 through the association with a newly identified adaptor, CIAO (COOH-terminal importin 9-related adaptor organizing histone H2B and IPS-1), to transmit the cellular signaling for dsDNA but not immunostimulatory RNA. Extrachromosomal histone H2B was biologically crucial for cell-autonomous responses to protect against multiplication of DNA viruses but not an RNA virus. Thus, the present findings provide evidence indicating that the extrachromosomal histone H2B is engaged in the signaling pathway initiated by dsDNA to trigger antiviral innate immune responses.

scholarly journals The Fourth International Symposium on Ranaviruses: Summary of North American Herpetological Content and Points of Interest

2020 ◽  
pp. 29
Author(s):  
Lauren Ash ◽  
Rachel Marschang ◽  
Jolianne Rijks ◽  
Amanda Duffus
Keyword(s):  
North America ◽  
International Symposium ◽  
North American ◽  
Fourth International Symposium ◽  
Dna Viruses ◽  
The North ◽  
Double Stranded Dna ◽  
Points Of Interest ◽  
The Family ◽  
Globally Distributed

Ranaviruses are large double stranded DNA viruses from the family Iridoviridae. They are globally distributed and are currently known to affect fish, reptiles and amphibians. In North America, ranaviruses are also widely distributed, and cause frequent morbidity and mortality events in both wild and cultured populations. This is a synopsys of the North American content of the 4th International Symposium on Ranaviruses held in May 2017 in Budapest, Hungary.

scholarly journals Exceptionally diverse morphotypes and genomes of crenarchaeal hyperthermophilic viruses

2004 ◽  
Vol 32 (2) ◽  
pp. 204-208 ◽  
Author(s):  
D. Prangishvili ◽  
R.A. Garrett
Keyword(s):  
Aquatic Ecosystems ◽  
African Swine Fever Virus ◽  
African Swine Fever ◽  
Open Reading Frames ◽  
Dna Viruses ◽  
Double Stranded Dna ◽  
Sequence Patterns ◽  
Hydrothermal Environments ◽  
Homologous Orfs ◽  
Reading Frames

The remarkable diversity of the morphologies of viruses found in terrestrial hydrothermal environments with temperatures >80°C is unprecedented for aquatic ecosystems. The best-studied viruses from these habitats have been assigned to novel viral families: Fuselloviridae, Lipothrixviridae and Rudiviridae. They all have double-stranded DNA genomes and infect hyperthermophilic crenarchaea of the orders Sulfolobales and Thermoproteales. Representatives of the different viral families share a few homologous ORFs (open reading frames). However, about 90% of all ORFs in the seven sequenced genomes show no significant matches to sequences in public databases. This suggests that these hyperthermophilic viruses have exceptional biochemical solutions for biological functions. Specific features of genome organization, as well as strategies for DNA replication, suggest that phylogenetic relationships exist between crenarchaeal rudiviruses and the large eukaryal DNA viruses: poxviruses, the African swine fever virus and Chlorella viruses. Sequence patterns at the ends of the linear genome of the lipothrixvirus AFV1 are reminiscent of the telomeric ends of linear eukaryal chromosomes and suggest that a primitive telomeric mechanism operates in this virus.

Sign in / Sign up

Export Citation Format

Share Document