scholarly journals Virus Assembly Pathways Inside a Host Cell

ACS Nano ◽  
2022 ◽  
Author(s):  
Sanaz Panahandeh ◽  
Siyu Li ◽  
Bogdan Dragnea ◽  
Roya Zandi
Keyword(s):  
Host Cell ◽  
Virus Assembly ◽  
Assembly Pathways

Chapter 2a: Virology

2021 ◽  
Author(s):  
Daniel Růžek ◽  
Kentaro Yoshii ◽  
Marshall E. Bloom ◽  
Ernest A. Gould
Keyword(s):  
Host Cell ◽  
Secretory Pathway ◽  
Virus Assembly ◽  
Close Association ◽  
Spherical Particles ◽  
Structural Proteins ◽  
Membrane Structures ◽  
Vesicle Membrane ◽  
Reading Frame ◽  
Tbe Virus

TBEV is the most medically important member of the tick-borne serocomplex group within the genus Flavivirus, family Flaviviridae. Three antigenic subtypes of TBEV correspond to the 3 recognized genotypes: European (TBEV-EU), also known as Western, Far Eastern (TBEV-FE), and Siberian (TBEV-SIB). An additional 2 genotypes have been identified in the Irkutsk region of Russia, currently named TBE virus Baikalian subtype (TBEV-BKL) and TBE virus Himalayan subtype (Himalayan and “178-79” group; TBEV-HIM). TBEV virions are small enveloped spherical particles about 50 nm in diameter. The TBEV genome consists of a single-stranded positive sense RNA molecule. The genome encodes one open reading frame (ORF), which is flanked by untranslated (non-coding) regions (UTRs). The 5′-UTR end has a methylated nucleotide cap for canonical cellular translation. The 3′-UTR is not polyadenylated and is characterized by extensive length and sequence heterogeneity. The ORF encodes one large polyprotein, which is co- and post-translationally cleaved into 3 structural proteins (C, prM, and E) and 7 non-structural proteins (NS1, NS2A, NS2B, NS3, NS4A, NS4B, and NS5). TBEV replicates in the cytoplasm of the host cell in close association with virus-induced intracellular membrane structures. Virus assembly occurs in the endoplasmic reticulum. The immature virions are transported to the Golgi complex, and mature virions pass through the host secretory pathway and are finally released from the host cell by fusion of the transport vesicle membrane with the plasma membrane.

scholarly journals Relationship between Vaccinia Virus Intracellular Cores, Early mRNAs, and DNA Replication Sites

2002 ◽  
Vol 76 (10) ◽  
pp. 5167-5183 ◽  
Author(s):  
Massimo Mallardo ◽  
Edward Leithe ◽  
Sibylle Schleich ◽  
Norbert Roos ◽  
Laura Doglio ◽  
...  
Keyword(s):  
Dna Replication ◽  
Vaccinia Virus ◽  
Host Cell ◽  
Virus Assembly ◽  
Mrna Accumulation ◽  
Structural Relationships ◽  
Late Event ◽  
Cytosolic Side ◽  
Replication Sites ◽  
Combined Data

ABSTRACT Virus assembly, a late event in the life cycle of vaccinia virus (VV), is preceded by a number of steps that all occur in the cytoplasm of the infected host cell: virion entry, delivery of the viral core into the cytoplasm, and transcription from these cores of early mRNAs, followed by the process of DNA replication. In the present study the quantitative and structural relationships between these distinct steps of VV morphogenesis were investigated. We show that viral RNA and DNA synthesis increases linearly with increasing amounts of incoming cores. Moreover, at multiplicities of infection that result in 10 to 40 cores per cell, an approximately 1:1 ratio between cores and sites of DNA replication exists, suggesting that each core is infectious. We have shown previously that VV early mRNAs collect in distinct granular structures that recruit components of the host cell translation machinery. Strikingly, these structures appeared to form some distance away from intracellular cores (M. Mallardo, S. Schleich, and J. Krijnse Locker, Mol. Biol. Cell 12:3875-3891, 2001). In the present study the intracellular locations of the sites of early mRNA accumulation and those of the subsequent process of DNA replication were compared. We show that these are distinct structures that have different intracellular locations. Finally, we study the fate of the parental DNA after core uncoating. By electron microscopy, cores were found close to membranes of the endoplasmic reticulum (ER) and the parental DNA, once it had left the core, appeared to associate preferentially with the cytosolic side of those membranes. Since we have previously shown that the process of DNA replication occurs in an ER-enclosed cytosolic “subcompartment” (N. Tolonen, L. Doglio, S. Schleich, and J. Krijnse Locker, Mol. Biol. Cell 12:2031-2046, 2001), the present data suggest that the parental DNA is released into the cytosol and associates with the same membranes where DNA replication is subsequently initiated. The combined data are discussed with respect to the cytosolic organization of VV morphogenesis.

scholarly journals Biochemical Characterization of Rous Sarcoma Virus MA Protein Interaction with Membranes

2005 ◽  
Vol 79 (10) ◽  
pp. 6227-6238 ◽  
Author(s):  
Amanda K. Dalton ◽  
Paul S. Murray ◽  
Diana Murray ◽  
Volker M. Vogt
Keyword(s):  
Host Cell ◽  
Rous Sarcoma Virus ◽  
Biochemical Characterization ◽  
Virus Assembly ◽  
Membrane Association ◽  
Host Cell Membrane ◽  
Rous Sarcoma ◽  
Sarcoma Virus

ABSTRACT The MA domain of retroviral Gag proteins mediates association with the host cell membrane during assembly. The biochemical nature of this interaction is not well understood. We have used an in vitro flotation assay to directly measure Rous sarcoma virus (RSV) MA-membrane interaction in the absence of host cell factors. The association of purified MA and MA-containing proteins with liposomes of defined composition was electrostatic in nature and depended upon the presence of a biologically relevant concentration of negatively charged lipids. A mutant MA protein known to be unable to promote Gag membrane association and budding in vivo failed to bind to liposomes. These results were supported by computational modeling. The intrinsic affinity of RSV MA for negatively charged membranes appears insufficient to promote efficient plasma membrane binding during assembly. However, an artificially dimerized form of MA bound to liposomes by at least an order of magnitude more tightly than monomeric MA. This result suggests that the clustering of MA domains, via Gag-Gag interactions during virus assembly, drives membrane association in vivo.

scholarly journals African Swine Fever Virus Protein pE199L Mediates Virus Entry by Enabling Membrane Fusion and Core Penetration

mBio ◽  
2020 ◽  
Vol 11 (4) ◽  
Author(s):  
Tania Matamoros ◽  
Alí Alejo ◽  
Javier María Rodríguez ◽  
Bruno Hernáez ◽  
Milagros Guerra ◽  
...  
Keyword(s):  
Membrane Fusion ◽  
Host Cell ◽  
Virus Assembly ◽  
African Swine Fever Virus ◽  
Virus Entry ◽  
African Swine Fever ◽  
Viral Envelope ◽  
Fever Virus ◽  
Virus Protein ◽  
Hemorrhagic Disease

ABSTRACT African swine fever virus (ASFV) is a complex nucleocytoplasmic large DNA virus (NCLDV) causing a lethal hemorrhagic disease that currently threatens the global pig industry. Despite its relevance in the infectious cycle, very little is known about the internalization of ASFV in the host cell. Here, we report the characterization of ASFV protein pE199L, a cysteine-rich structural polypeptide with similarity to proteins A16, G9, and J5 of the entry fusion complex (EFC) of poxviruses. Using biochemical and immunomicroscopic approaches, we found that, like the corresponding poxviral proteins, pE199L localizes to the inner viral envelope and behaves as an integral transmembrane polypeptide with cytosolic intramolecular disulfide bonds. Using an ASFV recombinant that inducibly expresses the E199L gene, we found that protein pE199L is not required for virus assembly and egress or for virus-cell binding and endocytosis but is required for membrane fusion and core penetration. Interestingly, similar results have been previously reported for ASFV protein pE248R, an inner membrane virion component related to the poxviral L1 and F9 EFC proteins. Taken together, these findings indicate that ASFV entry relies on a form of fusion machinery comprising proteins pE248R and pE199L that displays some similarities to the unconventional fusion apparatus of poxviruses. Also, these results provide novel targets for the development of strategies that block the first stages of ASFV replication. IMPORTANCE African swine fever virus (ASFV) causes a highly lethal swine disease that is currently present in many countries of Eastern Europe, the Russian Federation, and Southeast Asia, severely affecting the pig industry. Despite extensive research, effective vaccines or antiviral strategies are still lacking and relevant gaps in knowledge of the fundamental biology of the viral infection cycle exist. In this study, we identified pE199L, a protein of the inner viral membrane that is required for virus entry. More specifically, pE199L is necessary for the fusion event that leads to the penetration of the genome-containing core in the host cell. Our results significantly increase our knowledge of the process of internalization of African swine fever virus, which may instruct future research on antiviral strategies.

Assembly of the enveloped bacteriophage ϕ6 in environments which perturb the host cell membranes

1975 ◽  
Vol 21 (8) ◽  
pp. 1287-1290 ◽  
Author(s):  
J. A. Sands ◽  
R. A. Lowlicht ◽  
S. C. Cadden ◽  
J. Haneman
Keyword(s):  
Host Cell ◽  
Cell Membranes ◽  
Virus Assembly ◽  
Phospholipid Composition ◽  
Chemical Properties ◽  
Cell System ◽  
Cellular Growth ◽  
Cellular Membranes ◽  
Hydrophobic Molecule ◽  
Host Cell Membranes

The effects of known membrane-perturbing agents (pH, Na+, Ca2+, and a small lipid-soluble molecule) on the enveloped bacteriophage ϕ6 host cell system were investigated at the levels of cellular growth, virus assembly and stability, and the physical and chemical properties of host cell membranes. Spin-label probes of cellular membranes indicate that growth in high levels of Na+ or the small spherical hydrophobic molecule adamantanone results in membranes having increased "fluidity," while growth in high levels of Ca2+ results in slightly greater rigidity of the membranes. In addition, the phospholipid composition of the cellular membranes is dependent on the NaCl concentration in the growth medium. None of these membrane alterations, however, prevent the production of infectious ϕ6 virus particles.

Virus Assembly Pathways: Straying Away but Not Too Far

Small ◽  
2020 ◽  
Vol 16 (51) ◽  
pp. 2004475
Author(s):  
Kevin Bond ◽  
Irina B. Tsvetkova ◽  
Joseph Che‐Yen Wang ◽  
Martin F. Jarrold ◽  
Bogdan Dragnea
Keyword(s):  
Virus Assembly ◽  
Assembly Pathways

scholarly journals Lipid–protein interactions in virus assembly and budding from the host cell plasma membrane

2021 ◽  
Author(s):  
Balindile B. Motsa ◽  
Robert V. Stahelin
Keyword(s):  
Plasma Membrane ◽  
Host Cell ◽  
Lipid Bilayer ◽  
Protein Interactions ◽  
Current Knowledge ◽  
Virus Assembly ◽  
Cell Plasma Membrane ◽  
New Host ◽  
Cell Plasma ◽  
Lipid Protein Interactions

Lipid enveloped viruses contain a lipid bilayer coat that protects their genome to help facilitate entry into the new host cell. This lipid bilayer comes from the host cell which they infect. After viral replication, the mature virion hijacks the host cell plasma membrane where it is then released to infect new cells. This process is facilitated by the interaction between phospholipids that make up the plasma membrane and specialized viral matrix proteins. This step in the viral lifecycle may represent a viable therapeutic strategy for small molecules that aim to block enveloped virus spread. In this review, we summarize the current knowledge on the role of plasma membrane lipid–protein interactions on viral assembly and budding.

Chapter 2a: Virology

2020 ◽  
Keyword(s):  
Host Cell ◽  
Secretory Pathway ◽  
Virus Assembly ◽  
Close Association ◽  
Spherical Particles ◽  
Structural Proteins ◽  
Membrane Structures ◽  
Vesicle Membrane ◽  
Reading Frame ◽  
Tbe Virus

TBEV is the most medically important member of the tick-borne serocomplex group within the genus Flavivirus, family Flaviviridae. Three antigenic subtypes of TBEV correspond to the 3 recognized genotypes: European (TBEV-EU), also known as Western, Far Eastern (TBEV-FE), and Siberian (TBEV-SIB). An additional 2 genotypes have been identified in the Irkutsk region of Russia, currently named TBE virus Baikalian subtype (TBEV-BKL) and TBE virus Himalayan subtype (Himalayan and “178-79” group; TBEV-HIM). TBEV virions are small enveloped spherical particles about 50 nm in diameter. The TBEV genome consists of a single-stranded positive sense RNA molecule. The genome encodes one open reading frame (ORF), which is flanked by untranslated (non-coding) regions (UTRs). The 5′-UTR end has a methylated nucleotide cap for canonical cellular translation. The 3′-UTR is not polyadenylated and is characterized by extensive length and sequence heterogeneity. The ORF encodes one large polyprotein, which is co- and post-translationally cleaved into 3 structural proteins (C, prM, and E) and 7 non-structural proteins (NS1, NS2A, NS2B, NS3, NS4A, NS4B, and NS5). TBEV replicates in the cytoplasm of the host cell in close association with virus-induced intracellular membrane structures. Virus assembly occurs in the endoplasmic reticulum. The immature virions are transported to the Golgi complex, and mature virions pass through the host secretory pathway and are finally released from the host cell by fusion of the transport vesicle membrane with the plasma membrane.

Chapter 2a: Virology

2019 ◽  
Author(s):  
Daniel Růžek ◽  
Kentaro Yoshii ◽  
Marshall E. Bloom ◽  
Ernest A. Gould
Keyword(s):  
Host Cell ◽  
Secretory Pathway ◽  
Virus Assembly ◽  
Close Association ◽  
Spherical Particles ◽  
Structural Proteins ◽  
Membrane Structures ◽  
Vesicle Membrane ◽  
Reading Frame ◽  
Tbe Virus

• TBEV is the most medically important member of the tick-borne serocomplex group within the genus Flavivirus, family Flaviviridae. • Three antigenic subtypes of TBEV correspond to the 3 recognized genotypes: European (TBEV-EU), also known as Western, Far Eastern (TBEV-FE), and Siberian (TBEV-SIB). Additional 2 genotypes have been identified in the Irkutsk region of Russia, currently named TBE virus Baikalian subtype (TBEV-BKL) and TBE virus Himalaya subtype (Himalayan and “178-79” group; TBEV-HIM). • TBEV virions are small enveloped spherical particles about 50 nm in diameter. • The TBEV genome consists of a single-stranded positive sense RNA molecule. • The genome encodes one open reading frame (ORF), which is flanked by untranslated (non-coding) regions (UTRs). • The 5′-UTR end has a methylated nucleotide cap for canonical cellular translation. The 3′-UTR is not polyadenylated and is characterized by extensive length and sequence heterogeneity. • The ORF encodes one large polyprotein, which is co- and post-translationally cleaved into 3 structural proteins (C, prM, and E) and 7 non-structural proteins (NS1, NS2A, NS2B, NS3, NS4A, NS4B, and NS5). • TBEV replicates in the cytoplasm of the host cell in close association with virus-induced intracellular membrane structures. Virus assembly occurs in the endoplasmic reticulum. The immature virions are transported to the Golgi complex, and mature virions pass through the host secretory pathway and are finally released from the host cell by fusion of the transport vesicle membrane with the plasma membrane.

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