Log in

Relevant bibliographies by topics / Virus particle assembly / Journal articles

To see the other types of publications on this topic, follow the link: Virus particle assembly.

Journal articles on the topic 'Virus particle assembly'

Author: Grafiati

Published: 4 June 2021

Last updated: 14 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'Virus particle assembly.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

Crist, Rachael M., Siddhartha A. K. Datta, Andrew G. Stephen, et al. "Assembly Properties of Human Immunodeficiency Virus Type 1 Gag-Leucine Zipper Chimeras: Implications for Retrovirus Assembly." Journal of Virology 83, no. 5 (2008): 2216–25. http://dx.doi.org/10.1128/jvi.02031-08.

Full text

Abstract:

ABSTRACT Expression of the retroviral Gag protein leads to formation of virus-like particles in mammalian cells. In vitro and in vivo experiments show that nucleic acid is also required for particle assembly. However, several studies have demonstrated that chimeric proteins in which the nucleocapsid domain of Gag is replaced by a leucine zipper motif can also assemble efficiently in mammalian cells. We have now analyzed assembly by chimeric proteins in which nucleocapsid of human immunodeficiency virus type 1 (HIV-1) Gag is replaced by either a dimerizing or a trimerizing zipper. Both proteins

APA, Harvard, Vancouver, ISO, and other styles

2

Wang, Shainn-Wei, and Anna Aldovini. "RNA Incorporation Is Critical for Retroviral Particle Integrity after Cell Membrane Assembly of Gag Complexes." Journal of Virology 76, no. 23 (2002): 11853–65. http://dx.doi.org/10.1128/jvi.76.23.11853-11865.2002.

Full text

Abstract:

ABSTRACT The nucleocapsid (NC) domain of retroviruses plays a critical role in specific viral RNA packaging and virus assembly. RNA is thought to facilitate viral particle assembly, but the results described here with NC mutants indicate that it also plays a critical role in particle integrity. We investigated the assembly and integrity of particles produced by the human immunodeficiency virus type 1 M1-2/BR mutant virus, in which 10 of the 13 positive residues of NC have been replaced with alanines and incorporation of viral genomic RNA is virtually abolished. We found that the mutations in t

APA, Harvard, Vancouver, ISO, and other styles

3

Chlanda, Petr, Oliver Schraidt, Susann Kummer, et al. "Structural Analysis of the Roles of Influenza A Virus Membrane-Associated Proteins in Assembly and Morphology." Journal of Virology 89, no. 17 (2015): 8957–66. http://dx.doi.org/10.1128/jvi.00592-15.

Full text

Abstract:

ABSTRACTThe assembly of influenza A virus at the plasma membrane of infected cells leads to release of enveloped virions that are typically round in tissue culture-adapted strains but filamentous in strains isolated from patients. The viral proteins hemagglutinin (HA), neuraminidase (NA), matrix protein 1 (M1), and M2 ion channel all contribute to virus assembly. When expressed individually or in combination in cells, they can all, under certain conditions, mediate release of membrane-enveloped particles, but their relative roles in virus assembly, release, and morphology remain unclear. To in

APA, Harvard, Vancouver, ISO, and other styles

4

Wang, Chin-Tien, Hsiu-Yu Lai, and Jue-Jyh Li. "Analysis of Minimal Human Immunodeficiency Virus Type 1 gag Coding Sequences Capable of Virus-Like Particle Assembly and Release." Journal of Virology 72, no. 10 (1998): 7950–59. http://dx.doi.org/10.1128/jvi.72.10.7950-7959.1998.

Full text

Abstract:

ABSTRACT We have constructed a series of human immunodeficiency virus (HIV)gag mutants by progressive truncation of thegag coding sequence from the C terminus and have combined these mutants with an assembly-competent matrix domain deletion mutation (ΔMA). By using several methods, the particle-producing capabilities of each mutant were examined. Our analysis indicated that truncated Gag precursors lacking most of C-terminal gaggene products assembled and were released from 293T cells. Additionally, a mutant with a combined deletion of the MA (ΔMA) and p6 domains even produced particles at lev

APA, Harvard, Vancouver, ISO, and other styles

5

Joshi, Swati M., and Volker M. Vogt. "Role of the Rous Sarcoma Virus p10 Domain in Shape Determination of Gag Virus-Like Particles Assembled In Vitro and within Escherichia coli." Journal of Virology 74, no. 21 (2000): 10260–68. http://dx.doi.org/10.1128/jvi.74.21.10260-10268.2000.

Full text

Abstract:

ABSTRACT Purified retrovirus Gag proteins can assemble in vitro into virus-like particles (VLPs) in the presence of RNA. It was shown previously that a Rous sarcoma virus Gag protein missing only the protease domain forms spherical particles resembling immature virions lacking a membrane but that a similar protein missing the p10 domain forms tubular particles. Thus, p10 plays a role in spherical particle formation. To further study this shape-determining function, we dissected the p10 domain by mutagenesis and examined VLPs assembled within Escherichia coli or assembled in vitro from purified

APA, Harvard, Vancouver, ISO, and other styles

6

Gómez-Puertas, Paulino, Carmen Albo, Esperanza Pérez-Pastrana, Amparo Vivo, and Agustı́n Portela. "Influenza Virus Matrix Protein Is the Major Driving Force in Virus Budding." Journal of Virology 74, no. 24 (2000): 11538–47. http://dx.doi.org/10.1128/jvi.74.24.11538-11547.2000.

Full text

Abstract:

ABSTRACT To get insights into the role played by each of the influenza A virus polypeptides in morphogenesis and virus particle assembly, the generation of virus-like particles (VLPs) has been examined in COS-1 cell cultures expressing, from recombinant plasmids, different combinations of the viral structural proteins. The presence of VLPs was examined biochemically, following centrifugation of the supernatants collected from transfected cells through sucrose cushions and immunoblotting, and by electron-microscopic analysis. It is demonstrated that the matrix (M1) protein is the only viral com

APA, Harvard, Vancouver, ISO, and other styles

7

Tellinghuisen, Timothy L., and Richard J. Kuhn. "Nucleic Acid-Dependent Cross-Linking of the Nucleocapsid Protein of Sindbis Virus." Journal of Virology 74, no. 9 (2000): 4302–9. http://dx.doi.org/10.1128/jvi.74.9.4302-4309.2000.

Full text

Abstract:

ABSTRACT The assembly of the alphavirus nucleocapsid core is a multistep event requiring the association of the nucleocapsid protein with nucleic acid and the subsequent oligomerization of capsid proteins into an assembled core particle. Although the mechanism of assembly has been investigated extensively both in vivo and in vitro, no intermediates in the core assembly pathway have been identified. Through the use of both truncated and mutant Sindbis virus nucleocapsid proteins and a variety of cross-linking reagents, a possible nucleic acid-protein assembly intermediate has been detected. The

APA, Harvard, Vancouver, ISO, and other styles

8

Yuste-Calvo, Carmen, Pablo Ibort, Flora Sánchez, and Fernando Ponz. "Turnip Mosaic Virus Coat Protein Deletion Mutants Allow Defining Dispensable Protein Domains for ‘in Planta’ eVLP Formation." Viruses 12, no. 6 (2020): 661. http://dx.doi.org/10.3390/v12060661.

Full text

Abstract:

The involvement of different structural domains of the coat protein (CP) of turnip mosaic virus, a potyvirus, in establishing and/or maintaining particle assembly was analyzed through deletion mutants of the protein. In order to identify exclusively those domains involved in protein–protein interactions within the particle, the analysis was performed by agroinfiltration “in planta”, followed by the assessment of CP accumulation in leaves and the assembly of virus-like particles lacking nucleic acids, also known as empty virus-like particles (eVLP). Thus, the interactions involving viral RNA co

APA, Harvard, Vancouver, ISO, and other styles

9

Campbell, Stephen, and Alan Rein. "In Vitro Assembly Properties of Human Immunodeficiency Virus Type 1 Gag Protein Lacking the p6 Domain." Journal of Virology 73, no. 3 (1999): 2270–79. http://dx.doi.org/10.1128/jvi.73.3.2270-2279.1999.

Full text

Abstract:

ABSTRACT Human immunodeficiency virus type 1 (HIV-1) normally assembles into particles of 100 to 120 nm in diameter by budding through the plasma membrane of the cell. The Gag polyprotein is the only viral protein that is required for the formation of these particles. We have used an in vitro assembly system to examine the assembly properties of purified, recombinant HIV-1 Gag protein and of Gag missing the C-terminal p6 domain (Gag Δp6). This system was used previously to show that the CA-NC fragment of HIV-1 Gag assembled into cylindrical particles. We now report that both HIV-1 Gag and Gag

APA, Harvard, Vancouver, ISO, and other styles

10

Moraleda, Gloria, Steven Seeholzer, Vadim Bichko, Roland Dunbrack, James Otto, and John Taylor. "Unique Properties of the Large Antigen of Hepatitis Delta Virus." Journal of Virology 73, no. 9 (1999): 7147–52. http://dx.doi.org/10.1128/jvi.73.9.7147-7152.1999.

Full text

Abstract:

ABSTRACT The large form of the hepatitis delta virus (HDV) protein (L) can be isoprenylated near its C terminus, and this modification is considered essential for particle assembly. Using gel electrophoresis, we separated L into two species of similar mobilities. The slower species could be labeled by the incorporation of [14C]mevalonolactone and is interpreted to be isoprenylated L (Li). In serum particles, infected liver, transfected cells, and assembled particles, 25 to 85% of L was isoprenylated. Isoprenylation was also demonstrated by 14C incorporation in vitro with a rabbit reticulocyte

APA, Harvard, Vancouver, ISO, and other styles

11

de Haan, Cornelis A. M., Lili Kuo, Paul S. Masters, Harry Vennema, and Peter J. M. Rottier. "Coronavirus Particle Assembly: Primary Structure Requirements of the Membrane Protein." Journal of Virology 72, no. 8 (1998): 6838–50. http://dx.doi.org/10.1128/jvi.72.8.6838-6850.1998.

Full text

Abstract:

ABSTRACT Coronavirus-like particles morphologically similar to normal virions are assembled when genes encoding the viral membrane proteins M and E are coexpressed in eukaryotic cells. Using this envelope assembly assay, we have studied the primary sequence requirements for particle formation of the mouse hepatitis virus (MHV) M protein, the major protein of the coronavirion membrane. Our results show that each of the different domains of the protein is important. Mutations (deletions, insertions, point mutations) in the luminal domain, the transmembrane domains, the amphiphilic domain, or the

APA, Harvard, Vancouver, ISO, and other styles

12

Oshima, Masamichi, Delphine Muriaux, Jane Mirro, et al. "Effects of Blocking Individual Maturation Cleavages in Murine Leukemia Virus Gag." Journal of Virology 78, no. 3 (2004): 1411–20. http://dx.doi.org/10.1128/jvi.78.3.1411-1420.2004.

Full text

Abstract:

ABSTRACT A single protein, termed Gag, is responsible for retrovirus particle assembly. After the assembled virion is released from the cell, Gag is cleaved at several sites by the viral protease (PR). The cleavages catalyzed by PR bring about a wide variety of physical changes in the particle, collectively termed maturation, and convert the particle into an infectious virion. In murine leukemia virus (MLV) maturation, Gag is cleaved at three sites, resulting in formation of the matrix (MA), p12, capsid (CA), and nucleocapsid (NC) proteins. We introduced mutations into MLV that inhibited cleav

APA, Harvard, Vancouver, ISO, and other styles

13

Bednarska, Joanna, Annegret Pelchen-Matthews, Pavel Novak, et al. "Rapid formation of human immunodeficiency virus-like particles." Proceedings of the National Academy of Sciences 117, no. 35 (2020): 21637–46. http://dx.doi.org/10.1073/pnas.2008156117.

Full text

Abstract:

Understanding the molecular mechanisms involved in the assembly of viruses is essential for discerning how viruses transmit from cell to cell and host to host. Although molecular aspects of assembly have been studied for many viruses, we still have little information about these events in real time. Enveloped viruses such as HIV that assemble at, and bud from, the plasma membrane have been studied in some detail using live cell fluorescence imaging techniques; however, these approaches provide little information about the real-time morphological changes that take place as viral components come

APA, Harvard, Vancouver, ISO, and other styles

14

Villanueva, Rodrigo A., José L. Galaz, Juan A. Valdés, Matilde M. Jashés, and Ana María Sandino. "Genome Assembly and Particle Maturation of the Birnavirus Infectious Pancreatic Necrosis Virus." Journal of Virology 78, no. 24 (2004): 13829–38. http://dx.doi.org/10.1128/jvi.78.24.13829-13838.2004.

Full text

Abstract:

ABSTRACT In this study, we have analyzed the morphogenesis of the birnavirus infectious pancreatic necrosis virus throughout the infective cycle in CHSE-214 cells by using a native agarose electrophoresis system. Two types of viral particles (designated A and B) were identified, isolated, and characterized both molecularly and biologically. Together, our results are consistent with a model of morphogenesis in which the genomic double-stranded RNA is immediately assembled, after synthesis, into a large (66-nm diameter) and uninfectious particle A, where the capsid is composed of both mature and

APA, Harvard, Vancouver, ISO, and other styles

15

Zhang, Yaqiang, Haoyu Qian, Zachary Love, and Eric Barklis. "Analysis of the Assembly Function of the Human Immunodeficiency Virus Type 1 Gag Protein Nucleocapsid Domain." Journal of Virology 72, no. 3 (1998): 1782–89. http://dx.doi.org/10.1128/jvi.72.3.1782-1789.1998.

Full text

Abstract:

ABSTRACT Previous studies have shown that in addition to its function in specific RNA encapsidation, the human immunodeficiency virus type 1 (HIV-1) nucleocapsid (NC) is required for efficient virus particle assembly. However, the mechanism by which NC facilitates the assembly process is not clearly established. Formally, NC could act by constraining the Pr55 gag polyprotein into an assembly-competent conformation or by masking residues which block the assembly process. Alternatively, the capacity of NC to bind RNA or make interprotein contacts might affect particle assembly. To examine its ro

APA, Harvard, Vancouver, ISO, and other styles

16

Sakalian, Michael, and Eric Hunter. "Separate Assembly and Transport Domains within the Gag Precursor of Mason-Pfizer Monkey Virus." Journal of Virology 73, no. 10 (1999): 8073–82. http://dx.doi.org/10.1128/jvi.73.10.8073-8082.1999.

Full text

Abstract:

ABSTRACT Mason-Pfizer monkey virus (M-PMV), the prototypical type D retrovirus, assembles immature capsids within the cytoplasm of the cell prior to plasma membrane interaction. Several mutants of M-PMV Gag have been described which display altered transport, assembly, or both. In this report, we describe the use of an in vitro synthesis and assembly system to distinguish between defects in intracellular transport and the process of assembly itself for two previously describedgag gene mutants. Matrix domain mutant R55W converts the type D morphogenesis of M-PMV particles into type C and has be

APA, Harvard, Vancouver, ISO, and other styles

17

Sakalian, Michael, Stephanie S. Dittmer, A. Dustin Gandy, Nathan D. Rapp, Aleš Zábranský, and Eric Hunter. "The Mason-Pfizer Monkey Virus Internal Scaffold Domain Enables In Vitro Assembly of Human Immunodeficiency Virus Type 1 Gag." Journal of Virology 76, no. 21 (2002): 10811–20. http://dx.doi.org/10.1128/jvi.76.21.10811-10820.2002.

Full text

Abstract:

ABSTRACT The Mason-Pfizer monkey virus (M-PMV) Gag protein possesses the ability to assemble into an immature capsid when synthesized in a reticulocyte lysate translation system. In contrast, the human immunodeficiency virus (HIV) Gag protein is incapable of assembly in parallel assays. To enable the assembly of HIV Gag, we have combined or inserted regions of M-PMV Gag into HIV Gag. By both biochemical and morphological criteria, several of these chimeric Gag molecules are capable of assembly into immature capsid-like structures in this in vitro system. Chimeric species containing large regio

APA, Harvard, Vancouver, ISO, and other styles

18

von Schwedler, Uta K., Kirsten M. Stray, Jennifer E. Garrus, and Wesley I. Sundquist. "Functional Surfaces of the Human Immunodeficiency Virus Type 1 Capsid Protein." Journal of Virology 77, no. 9 (2003): 5439–50. http://dx.doi.org/10.1128/jvi.77.9.5439-5450.2003.

Full text

Abstract:

ABSTRACT The human immunodeficiency virus type 1 initially assembles and buds as an immature particle that is organized by the viral Gag polyprotein. Gag is then proteolyzed to produce the smaller capsid protein CA, which forms the central conical capsid that surrounds the RNA genome in the mature, infectious virus. To define CA surfaces that function at different stages of the viral life cycle, a total of 48 different alanine-scanning surface mutations in CA were tested for their effects on Gag protein expression, processing, particle production and morphology, capsid assembly, and infectivit

APA, Harvard, Vancouver, ISO, and other styles

19

Klug, A. "The tobacco mosaic virus particle: structure and assembly." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 354, no. 1383 (1999): 531–35. http://dx.doi.org/10.1098/rstb.1999.0404.

Full text

Abstract:

A short account is given of the physical and chemical studies that have led to an understanding of the structure of the tobacco mosaic virus particle and how it is assembled from its constituent coat protein and RNA. The assembly is a much more complex process than might have been expected from the simplicity of the helical design of the particle. The protein forms an obligatory intermediate (a cylindrical disk composed of two layers of protein units), which recognizes a specific RNA hairpin sequence. This extraordinary mechanism simultaneously fulfils the physical requirement for nucleating t

APA, Harvard, Vancouver, ISO, and other styles

20

Muriaux, Delphine, Sylvain Costes, Kunio Nagashima, et al. "Role of Murine Leukemia Virus Nucleocapsid Protein in Virus Assembly." Journal of Virology 78, no. 22 (2004): 12378–85. http://dx.doi.org/10.1128/jvi.78.22.12378-12385.2004.

Full text

Abstract:

ABSTRACT The retroviral nucleocapsid protein (NC) originates by cleavage of the Gag polyprotein. It is highly basic and contains one or two zinc fingers. Mutations in either the basic residues or the zinc fingers can affect several events of the virus life cycle. They frequently prevent the specific packaging of the viral RNA, affect reverse transcription, and impair virion assembly. In this work, we explore the role of NC in murine leukemia virus (MLV) particle assembly and release. A panel of NC mutants, including mutants of the zinc finger and of a basic region, as well as truncations of th

APA, Harvard, Vancouver, ISO, and other styles

21

Baumert, Thomas F., Susumu Ito, David T. Wong, and T. Jake Liang. "Hepatitis C Virus Structural Proteins Assemble into Viruslike Particles in Insect Cells." Journal of Virology 72, no. 5 (1998): 3827–36. http://dx.doi.org/10.1128/jvi.72.5.3827-3836.1998.

Full text

Abstract:

ABSTRACT Hepatitis C virus (HCV) is a leading cause of chronic hepatitis in the world. The study of HCV has been hampered by the low level of viral particles in infected individuals, the inability to propagate efficiently the virus in cultured cells, and the lack of a convenient animal model. Due to these obstacles, neither the structure of the virus nor the prerequisites for its assembly have been clearly defined. In this report, we describe a model for the production and purification of HCV-like particles in insect cells using a recombinant baculovirus containing the cDNA of the HCV structur

APA, Harvard, Vancouver, ISO, and other styles

22

Füzik, Tibor, Růžena Píchalová, Florian K. M. Schur, et al. "Nucleic Acid Binding by Mason-Pfizer Monkey Virus CA Promotes Virus Assembly and Genome Packaging." Journal of Virology 90, no. 9 (2016): 4593–603. http://dx.doi.org/10.1128/jvi.03197-15.

Full text

Abstract:

ABSTRACTThe Gag polyprotein of retroviruses drives immature virus assembly by forming hexameric protein lattices. The assembly is primarily mediated by protein-protein interactions between capsid (CA) domains and by interactions between nucleocapsid (NC) domains and RNA. Specific interactions between NC and the viral RNA are required for genome packaging. Previously reported cryoelectron microscopy analysis of immature Mason-Pfizer monkey virus (M-PMV) particles suggested that a basic region (residues RKK) in CA may serve as an additional binding site for nucleic acids. Here, we have introduce

APA, Harvard, Vancouver, ISO, and other styles

23

Schmidt, Uli, Rainer Rudolph, and Gerald Böhm. "Mechanism of Assembly of Recombinant Murine Polyomavirus-Like Particles." Journal of Virology 74, no. 4 (2000): 1658–62. http://dx.doi.org/10.1128/jvi.74.4.1658-1662.2000.

Full text

Abstract:

ABSTRACT VP1 is the major viral coat protein of murine polyomavirus and can be used for the generation of virus-like particles in vitro. Here, we demonstrate that capsid assembly is an equilibrium reaction followed by oxidation of intracapsomere disulfide bonds, which are not essential for the formation of virus-like particles but enable complete particle assembly and prevent capsid dissembly.

APA, Harvard, Vancouver, ISO, and other styles

24

Ong, Swee Tin, Khatijah Yusoff, Chiew Ling Kho, Janna Ong Abdullah, and Wen Siang Tan. "Mutagenesis of the nucleocapsid protein of Nipah virus involved in capsid assembly." Journal of General Virology 90, no. 2 (2009): 392–97. http://dx.doi.org/10.1099/vir.0.005710-0.

Full text

Abstract:

The nucleocapsid protein of Nipah virus produced in Escherichia coli assembled into herringbone-like particles. The amino- and carboxy-termini of the N protein were shortened progressively to define the minimum contiguous sequence involved in capsid assembly. The first 29 aa residues of the N protein are dispensable for capsid formation. The 128 carboxy-terminal residues do not play a role in the assembly of the herringbone-like particles. A region with amino acid residues 30–32 plays a crucial role in the formation of the capsid particle. Deletion of any of the four conserved hydrophobic regi

APA, Harvard, Vancouver, ISO, and other styles

25

Tritel, Marc, and Marilyn D. Resh. "Kinetic Analysis of Human Immunodeficiency Virus Type 1 Assembly Reveals the Presence of Sequential Intermediates." Journal of Virology 74, no. 13 (2000): 5845–55. http://dx.doi.org/10.1128/jvi.74.13.5845-5855.2000.

Full text

Abstract:

ABSTRACT The assembly and budding of lentiviruses, such as human immunodeficiency virus type 1 (HIV-1), are mediated by the Gag protein precursor, but the molecular details of these processes remain poorly defined. In this study, we have combined pulse-chase techniques with density gradient centrifugation to identify, isolate, and characterize sequential kinetic intermediates in the lentivirus assembly process. We show that newly synthesized HIV-1 Gag rapidly forms cytoplasmic protein complexes that are resistant to detergent treatment, sensitive to protease digestion, and degraded intracellul

APA, Harvard, Vancouver, ISO, and other styles

26

Bennett, Robert P., and John W. Wills. "Conditions for Copackaging Rous Sarcoma Virus and Murine Leukemia Virus Gag Proteins during Retroviral Budding." Journal of Virology 73, no. 3 (1999): 2045–51. http://dx.doi.org/10.1128/jvi.73.3.2045-2051.1999.

Full text

Abstract:

ABSTRACT Rous sarcoma virus (RSV) and murine leukemia virus (MLV) are examples of distantly related retroviruses that normally do not encounter one another in nature. Their Gag proteins direct particle assembly at the plasma membrane but possess very little sequence similarity. As expected, coexpression of these two Gag proteins did not result in particles that contain both. However, when the N-terminal membrane-binding domain of each molecule was replaced with that of the Src oncoprotein, which is also targeted to the cytoplasmic face of the plasma membrane, efficient copackaging was observed

APA, Harvard, Vancouver, ISO, and other styles

27

Wieringa, Roeland, Antoine A. F. de Vries, Jannes van der Meulen, et al. "Structural Protein Requirements in Equine Arteritis Virus Assembly." Journal of Virology 78, no. 23 (2004): 13019–27. http://dx.doi.org/10.1128/jvi.78.23.13019-13027.2004.

Full text

Abstract:

ABSTRACT Equine arteritis virus (EAV) is an enveloped, positive-stranded RNA virus belonging to the family Arteriviridae of the order Nidovirales. EAV particles contain seven structural proteins: the nucleocapsid protein N, the unglycosylated envelope proteins M and E, and the N-glycosylated membrane proteins GP2b (previously named GS), GP3, GP4, and GP5 (previously named GL). Proteins N, M, and GP5 are major virion components, E occurs in virus particles in intermediate amounts, and GP4, GP3, and GP2b are minor structural proteins. The M and GP5 proteins occur in virus particles as disulfide-

APA, Harvard, Vancouver, ISO, and other styles

28

Blanchard, Emmanuelle, Denys Brand, Sylvie Trassard, Alain Goudeau, and Philippe Roingeard. "Hepatitis C Virus-Like Particle Morphogenesis." Journal of Virology 76, no. 8 (2002): 4073–79. http://dx.doi.org/10.1128/jvi.76.8.4073-4079.2002.

Full text

Abstract:

ABSTRACT Although much is known about the hepatitis C virus (HCV) genome, first cloned in 1989, little is known about HCV structure and assembly due to the lack of an efficient in vitro culture system for HCV. Using a recombinant Semliki forest virus replicon expressing genes encoding HCV structural proteins, we observed for the first time the assembly of these proteins into HCV-like particles in mammalian cells. This system opens up new possibilities for the investigation of viral morphogenesis and virus-host cell interactions.

APA, Harvard, Vancouver, ISO, and other styles

29

Kim, Gyoung Nyoun, and C. Yong Kang. "Utilization of Homotypic and Heterotypic Proteins of Vesicular Stomatitis Virus by Defective Interfering Particle Genomes for RNA Replication and Virion Assembly: Implications for the Mechanism of Homologous Viral Interference." Journal of Virology 79, no. 15 (2005): 9588–96. http://dx.doi.org/10.1128/jvi.79.15.9588-9596.2005.

Full text

Abstract:

ABSTRACT Defective interfering (DI) particles of Indiana serotype of vesicular stomatitis virus (VSVInd) are capable of interfering with the replication of both homotypic VSVInd and heterotypic New Jersey serotype (VSVNJ) standard virus. In contrast, DI particles from VSVNJ do not interfere with the replication of VSVInd standard virus but do interfere with VSVNJ replication. The differences in the interfering activities of VSVInd DI particles and VSVNJ DI particles against heterotypic standard virus were investigated. We examined the utilization of homotypic and heterotypic VSV proteins by DI

APA, Harvard, Vancouver, ISO, and other styles

30

Schroeder, Susan J. "Perspectives on Viral RNA Genomes and the RNA Folding Problem." Viruses 12, no. 10 (2020): 1126. http://dx.doi.org/10.3390/v12101126.

Full text

Abstract:

Viral RNA genomes change shape as virus particles disassemble, form replication complexes, attach to ribosomes for translation, evade host defense mechanisms, and assemble new virus particles. These structurally dynamic RNA shapeshifters present a challenging RNA folding problem, because the RNA sequence adopts multiple structures and may sometimes contain regions of partial disorder. Recent advances in high resolution asymmetric cryoelectron microscopy and chemical probing provide new ways to probe the degree of structure and disorder, and have identified more than one conformation in dynamic

APA, Harvard, Vancouver, ISO, and other styles

31

van Rosmalen, Mariska G. M., Douwe Kamsma, Andreas S. Biebricher, et al. "Revealing in real-time a multistep assembly mechanism for SV40 virus-like particles." Science Advances 6, no. 16 (2020): eaaz1639. http://dx.doi.org/10.1126/sciadv.aaz1639.

Full text

Abstract:

Many viruses use their genome as template for self-assembly into an infectious particle. However, this reaction remains elusive because of the transient nature of intermediate structures. To elucidate this process, optical tweezers and acoustic force spectroscopy are used to follow viral assembly in real time. Using Simian virus 40 (SV40) virus-like particles as model system, we reveal a multistep assembly mechanism. Initially, binding of VP1 pentamers to DNA leads to a significantly decreased persistence length. Moreover, the pentamers seem able to stabilize DNA loops. Next, formation of inte

APA, Harvard, Vancouver, ISO, and other styles

32

Gebhard, Leopoldo G., Néstor G. Iglesias, Laura A. Byk, Claudia V. Filomatori, Federico A. De Maio, and Andrea V. Gamarnik. "A Proline-Rich N-Terminal Region of the Dengue Virus NS3 Is Crucial for Infectious Particle Production." Journal of Virology 90, no. 11 (2016): 5451–61. http://dx.doi.org/10.1128/jvi.00206-16.

Full text

Abstract:

ABSTRACTDengue virus is currently the most important insect-borne viral human pathogen. Viral nonstructural protein 3 (NS3) is a key component of the viral replication machinery that performs multiple functions during viral replication and participates in antiviral evasion. Using dengue virus infectious clones and reporter systems to dissect each step of the viral life cycle, we examined the requirements of different domains of NS3 on viral particle assembly. A thorough site-directed mutagenesis study based on solvent-accessible surface areas of NS3 revealed that, in addition to being essentia

APA, Harvard, Vancouver, ISO, and other styles

33

Steinmann, Eike, Christiane Brohm, Stephanie Kallis, Ralf Bartenschlager, and Thomas Pietschmann. "Efficient trans-Encapsidation of Hepatitis C Virus RNAs into Infectious Virus-Like Particles." Journal of Virology 82, no. 14 (2008): 7034–46. http://dx.doi.org/10.1128/jvi.00118-08.

Full text

Abstract:

ABSTRACT Recently, complete replication of hepatitis C virus (HCV) in tissue culture was established using the JFH1 isolate. To analyze determinants of HCV genome packaging and virion assembly, we developed a system that supports particle production based on trans-packaging of subgenomic viral RNAs. Using JFH1 helper viruses, we show that subgenomic JFH1 replicons lacking the entire core to NS2 coding region are efficiently encapsidated into infectious virus-like particles. Similarly, chimeric helper viruses with heterologous structural proteins trans-package subgenomic JFH1 replicons. Like au

APA, Harvard, Vancouver, ISO, and other styles

34

Krishna, Neel K., Stephen Campbell, Volker M. Vogt, and John W. Wills. "Genetic Determinants of Rous Sarcoma Virus Particle Size." Journal of Virology 72, no. 1 (1998): 564–77. http://dx.doi.org/10.1128/jvi.72.1.564-577.1998.

Full text

Abstract:

ABSTRACT The Gag proteins of retroviruses are the only viral products required for the release of membrane-enclosed particles by budding from the host cell. Particles released when these proteins are expressed alone are identical to authentic virions in their rates of budding, proteolytic processing, and core morphology, as well as density and size. We have previously mapped three very small, modular regions of the Rous sarcoma virus (RSV) Gag protein that are necessary for budding. These assembly domains constitute only 20% of RSV Gag, and alterations within them block or severely impair part

APA, Harvard, Vancouver, ISO, and other styles

35

Jouvenet, Nolwenn, Stuart J. D. Neil, Maria Zhadina, et al. "Broad-Spectrum Inhibition of Retroviral and Filoviral Particle Release by Tetherin." Journal of Virology 83, no. 4 (2008): 1837–44. http://dx.doi.org/10.1128/jvi.02211-08.

Full text

Abstract:

ABSTRACT The expression of many putative antiviral genes is upregulated when cells encounter type I interferon (IFN), but the actual mechanisms by which many IFN-induced gene products inhibit virus replication are poorly understood. A recently identified IFN-induced antiretroviral protein, termed tetherin (previously known as BST-2 or CD317), blocks the release of nascent human immunodeficiency virus type 1 (HIV-1) particles from infected cells, and an HIV-1 accessory protein, Vpu, acts as a viral antagonist of tetherin. Here, we show that tetherin is capable of blocking not only the release o

APA, Harvard, Vancouver, ISO, and other styles

36

Feng, Ya-Xiong, Tong Li, Stephen Campbell, and Alan Rein. "Reversible Binding of Recombinant Human Immunodeficiency Virus Type 1 Gag Protein to Nucleic Acids in Virus-Like Particle Assembly In Vitro." Journal of Virology 76, no. 22 (2002): 11757–62. http://dx.doi.org/10.1128/jvi.76.22.11757-11762.2002.

Full text

Abstract:

ABSTRACT Recombinant human immunodeficiency virus type 1 (HIV-1) Gag protein can assemble into virus-like particles (VLPs) in suitable buffer conditions with nucleic acid. We have explored the role of nucleic acid in this assembly process. HIV-1 nucleocapsid protein, a domain of Gag, can bind to oligodeoxynucleotides with the sequence d(TG)n with more salt resistance than to d(A)n oligonucleotides. We found that assembly of VLPs on d(TG)n oligonucleotides was more salt resistant than assembly on d(A)n; thus, the oligonucleotides do not simply neutralize basic residues in Gag but provide a bind

APA, Harvard, Vancouver, ISO, and other styles

37

Balasubramaniam, Muthukumar, and Eric O. Freed. "New Insights into HIV Assembly and Trafficking." Physiology 26, no. 4 (2011): 236–51. http://dx.doi.org/10.1152/physiol.00051.2010.

Full text

Abstract:

Assembly and release of human immunodeficiency virus type 1 (HIV-1) particles is mediated by the viral Gag polyprotein precursor. Gag is synthesized in the cytosol and rapidly translocates to membrane to orchestrate particle production. The cell biology of HIV-1 Gag trafficking is currently one of the least understood aspects of HIV-1 replication. In this review, we highlight the current understanding of the cellular machinery involved in Gag trafficking and virus assembly.

APA, Harvard, Vancouver, ISO, and other styles

38

Kaplan, Igor B., Lawrence Lee, Daniel R. Ripoll, Peter Palukaitis, Frederick Gildow, and Stewart M. Gray. "Point mutations in the potato leafroll virus major capsid protein alter virion stability and aphid transmission." Journal of General Virology 88, no. 6 (2007): 1821–30. http://dx.doi.org/10.1099/vir.0.82837-0.

Full text

Abstract:

The coat protein (CP) of potato leafroll virus (PLRV) is the primary component of the capsid, and is a multifunctional protein known to be involved in vector transmission and virus movement within plant hosts, in addition to particle assembly. Thirteen mutations were generated in various regions of the CP and tested for their ability to affect virus–host and virus–vector interactions. Nine of the mutations prevented the assembly of stable virions. These mutants were unable to infect systemically four different host species. Furthermore, although virus replication and translation of the CP were

APA, Harvard, Vancouver, ISO, and other styles

39

DiPrimio, Nina, Aravind Asokan, Lakshmanan Govindasamy, Mavis Agbandje-McKenna, and R. Jude Samulski. "Surface Loop Dynamics in Adeno-Associated Virus Capsid Assembly." Journal of Virology 82, no. 11 (2008): 5178–89. http://dx.doi.org/10.1128/jvi.02721-07.

Full text

Abstract:

ABSTRACT The HI loop is a prominent domain on the adeno-associated virus (AAV) capsid surface that extends from each viral protein (VP) subunit overlapping the neighboring fivefold VP. Despite the highly conserved nature of the residues at the fivefold pore, the HI loops surrounding this critical region vary significantly in amino acid sequence between the AAV serotypes. In order to understand the role of this unique capsid domain, we ablated side chain interactions between the HI loop and the underlying EF loop in the neighboring VP subunit by generating a collection of deletion, insertion, a

APA, Harvard, Vancouver, ISO, and other styles

40

Thurlow, Johanna K., Frazer J. Rixon, Mary Murphy, Paul Targett-Adams, Michelle Hughes, and Valerie G. Preston. "The Herpes Simplex Virus Type 1 DNA Packaging Protein UL17 Is a Virion Protein That Is Present in Both the Capsid and the Tegument Compartments." Journal of Virology 79, no. 1 (2005): 150–58. http://dx.doi.org/10.1128/jvi.79.1.150-158.2005.

Full text

Abstract:

ABSTRACT The UL17 protein of herpes simplex virus type 1 is essential for packaging the viral genome into the procapsid, a spherical assembly intermediate, and is present in the mature virus particle. We have examined the distribution of UL17 in various assembly products and virions to determine which component of the virus particle UL17 is associated with and at what stage in capsid assembly UL17 is required. UL17 was present in the procapsid, in the DNA-containing angularized C capsid, and in two other angularized capsid forms, A and B, that lack DNA and are thought to be dead-end products.

APA, Harvard, Vancouver, ISO, and other styles

41

ZHONG, Boxiong. "An assembly model of Rice dwarf virus particle." Science in China Series C 47, no. 1 (2004): 92. http://dx.doi.org/10.1360/02yc0061.

Full text

APA, Harvard, Vancouver, ISO, and other styles

42

Tsvetkova, Irina, Chao Chen, Subinoy Rana, C. Cheng Kao, Vincent M. Rotello, and Bogdan Dragnea. "Pathway switching in templated virus-like particle assembly." Soft Matter 8, no. 17 (2012): 4571. http://dx.doi.org/10.1039/c2sm00024e.

Full text

APA, Harvard, Vancouver, ISO, and other styles

43

Scholz, Isabel, Brian Arvidson, Doug Huseby, and Eric Barklis. "Virus Particle Core Defects Caused by Mutations in the Human Immunodeficiency Virus Capsid N-Terminal Domain." Journal of Virology 79, no. 3 (2005): 1470–79. http://dx.doi.org/10.1128/jvi.79.3.1470-1479.2005.

Full text

Abstract:

ABSTRACT The N-terminal domains (NTDs) of the human immunodeficiency virus type 1 (HIV-1) capsid (CA) protein have been modeled to form hexamer rings in the mature cores of virions. In vitro, hexamer ring units organize into either tubes or spheres, in a pH-dependent fashion. To probe factors which might govern hexamer assembly preferences in vivo, we examined the effects of mutations at CA histidine residue 84 (H84), modeled at the outer edges of NTD hexamers, as well as a nearby histidine (H87) in the cyclophilin A (CypA) binding loop. Although mutations at H87 yielded infectious virions, mu

APA, Harvard, Vancouver, ISO, and other styles

44

Bertolotti-Ciarlet, Andrea, Laura J. White, Rong Chen, B. V. Venkataram Prasad, and Mary K. Estes. "Structural Requirements for the Assembly of Norwalk Virus-Like Particles." Journal of Virology 76, no. 8 (2002): 4044–55. http://dx.doi.org/10.1128/jvi.76.8.4044-4055.2002.

Full text

Abstract:

ABSTRACT Norwalk virus (NV) is the prototype strain of a group of human caliciviruses responsible for epidemic outbreaks of acute gastroenteritis. While these viruses do not grow in tissue culture cells or animal models, expression of the capsid protein in insect cells results in the self-assembly of recombinant NV virus-like particles (rNV VLPs) that are morphologically and antigenically similar to native NV. The X-ray structure of the rNV VLPs has revealed that the capsid protein folds into two principal domains: a shell (S) domain and a protruding (P) domain (B. V. V. Prasad, M. E. Hardy, T

APA, Harvard, Vancouver, ISO, and other styles

45

Counihan, Natalie A., Stephen M. Rawlinson, and Brett D. Lindenbach. "Trafficking of Hepatitis C Virus Core Protein during Virus Particle Assembly." PLoS Pathogens 7, no. 10 (2011): e1002302. http://dx.doi.org/10.1371/journal.ppat.1002302.

Full text

APA, Harvard, Vancouver, ISO, and other styles

46

Vieyres, Gabrielle, and Thomas Pietschmann. "HCV Pit Stop at the Lipid Droplet: Refuel Lipids and Put on a Lipoprotein Coat before Exit." Cells 8, no. 3 (2019): 233. http://dx.doi.org/10.3390/cells8030233.

Full text

Abstract:

The replication cycle of the liver-tropic hepatitis C virus (HCV) is tightly connected to the host lipid metabolism, during the virus entry, replication, assembly and egress stages, but also while the virus circulates in the bloodstream. This interplay coins viral particle properties, governs viral cell tropism, and facilitates immune evasion. This review summarizes our knowledge of these interactions focusing on the late steps of the virus replication cycle. It builds on our understanding of the cell biology of lipid droplets and the biosynthesis of liver lipoproteins and attempts to explain

APA, Harvard, Vancouver, ISO, and other styles

47

Venter, P. Arno, and Anette Schneemann. "Assembly of Two Independent Populations of Flock House Virus Particles with Distinct RNA Packaging Characteristics in the Same Cell." Journal of Virology 81, no. 2 (2006): 613–19. http://dx.doi.org/10.1128/jvi.01668-06.

Full text

Abstract:

ABSTRACT Flock House virus (FHV; Nodaviridae) is a positive-strand RNA virus that encapsidates a bipartite genome consisting of RNA1 and RNA2. We recently showed that specific recognition of these RNAs for packaging into progeny particles requires coat protein translated from replicating viral RNA. In the present study, we investigated whether the entire assembly pathway, i.e., the formation of the initial nucleating complex and the subsequent completion of the capsid, is restricted to the same pool of coat protein subunits. To test this, coat proteins carrying either FLAG or hemagglutinin epi

APA, Harvard, Vancouver, ISO, and other styles

48

Baker, T. S., W. W. Newcomb, F. P. Booy, J. C. Brown, and A. C. Steven. "Three-Dimensional reconstructions of ’light’ and ’intermediate’ capsids of equine herpes virus." Proceedings, annual meeting, Electron Microscopy Society of America 47 (August 6, 1989): 822–23. http://dx.doi.org/10.1017/s0424820100156080.

Full text

Abstract:

Equine herpes virus type 1 (EHV-1) belongs to an extensive family of large, genetically complex, and medically important animal viruses. The virion consists of an icosahedral nucleocapsid (T=16) separated from the viral envelope by a proteinaceous tegument layer. Assembly occurs in the nucleus of infected cells where capsids assemble, are packaged with DNA, then bud through the nuclear membrane. Two morphological species of EHV-1 capsids have been distinguished: “lights” which are abortive particles incapable of packaging DNA and “intermediates” which are precursors in the assembly of mature v

APA, Harvard, Vancouver, ISO, and other styles

49

Wang, Shainn-Wei, Kristin Noonan, and Anna Aldovini. "Nucleocapsid-RNA Interactions Are Essential to Structural Stability but Not to Assembly of Retroviruses." Journal of Virology 78, no. 2 (2004): 716–23. http://dx.doi.org/10.1128/jvi.78.2.716-723.2004.

Full text

Abstract:

ABSTRACT The process of RNA incorporation into nascent virions is thought to be critical for efficient retroviral particle assembly and production. Here we show that human immunodeficiency virus type 1 mutant particles (which are highly unstable and break down soon after release from the cell) lacking nucleocapsid (NC) core protein-mediated RNA incorporation are produced efficiently and can be recovered at the normal density when viral protease function is abolished. These results demonstrate that RNA binding by Gag is not necessary for retroviral particle assembly. Rather, the RNA interaction

APA, Harvard, Vancouver, ISO, and other styles

50

Rahman, Sheikh Abdul, Peter Koch, Julian Weichsel, et al. "Investigating the Role of F-Actin in Human Immunodeficiency Virus Assembly by Live-Cell Microscopy." Journal of Virology 88, no. 14 (2014): 7904–14. http://dx.doi.org/10.1128/jvi.00431-14.

Full text

Abstract:

ABSTRACTHuman immunodeficiency virus type 1 (HIV-1) particles assemble at the plasma membrane, which is lined by a dense network of filamentous actin (F-actin). Large amounts of actin have been detected in HIV-1 virions, proposed to be incorporated by interactions with the nucleocapsid domain of the viral polyprotein Gag. Previous studies addressing the role of F-actin in HIV-1 particle formation using F-actin-interfering drugs did not yield consistent results. Filamentous structures pointing toward nascent HIV-1 budding sites, detected by cryo-electron tomography and atomic force microscopy,

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!