Max L. Nibert

Comparisons of the M1 genome segments and encoded μ2 proteins of different reovirus isolates (2004)

Yin, Peng, Keirstead, Natalie D, Broering, Teresa J, Arnold, Michelle M, Parker, John SL, Nibert, Max L, ...

Abstract Background The reovirus M1 genome segment encodes the μ2 protein, a structurally minor component of the viral core, which has been identified as a transcriptase cofactor, nucleoside and RNA...

Reovirus Virion-Like Particles Obtained by Recoating Infectious Subvirion Particles with Baculovirus-Expressed ς3 Protein: an Approach for Analyzing ς3 Functions during Virus Entry

Jané-Valbuena, Judit, Nibert, Max L., Spencer, Stephan M., Walker, Stephen B., Baker, Timothy S., Chen, Ya, ...

Structure-function studies with mammalian reoviruses have been limited by the lack of a reverse-genetic system for engineering mutations into the viral genome. To circumvent this limitation in a...

In Vitro Recoating of Reovirus Cores with Baculovirus-Expressed Outer-Capsid Proteins μ1 and ς3

Chandran, Kartik, Walker, Stephen B., Chen, Ya, Contreras, Carlo M., Schiff, Leslie A., Baker, Timothy S., ...

Reovirus outer-capsid proteins μ1, ς3, and ς1 are thought to be assembled onto nascent core-like particles within infected cells, leading to the production of progeny virions. Consistent with this...

Protease Cleavage of Reovirus Capsid Protein μ1/μ1C Is Blocked by Alkyl Sulfate Detergents, Yielding a New Type of Infectious Subvirion Particle

Chandran, Kartik, Nibert, Max L.

Mammalian reovirus virions undergo partial disassembly of the outer capsid upon exposure to proteases in vitro, producing infectious subvirion particles (ISVPs) that lack protein ς3 and contain...

Cleavage Susceptibility of Reovirus Attachment Protein ς1 during Proteolytic Disassembly of Virions Is Determined by a Sequence Polymorphism in the ς1 Neck

Chappell, James D., Barton, Erik S., Smith, Trent H., Baer, Geoffrey S., Duong, David T., Nibert, Max L., ...

A requisite step in reovirus infection of the murine intestine is proteolysis of outer-capsid proteins to yield infectious subvirion particles (ISVPs). When converted to ISVPs by intestinal...

Reovirus Nonstructural Protein μNS Binds to Core Particles but Does Not Inhibit Their Transcription and Capping Activities

Broering, Teresa J., McCutcheon, Aimee M., Centonze, Victoria E., Nibert, Max L.

Previous studies provided evidence that nonstructural protein μNS of mammalian reoviruses is present in particle assembly intermediates isolated from infected cells. Morgan and Zweerink (Virology...

Reovirus Protein ςNS Binds in Multiple Copies to Single-Stranded RNA and Shares Properties with Single-Stranded DNA Binding Proteins

Gillian, Anne Lynn, Schmechel, Stephen C., Livny, Jonathan, Schiff, Leslie A., Nibert, Max L.

Reovirus nonstructural protein ςNS interacts with reovirus plus-strand RNAs in infected cells, but little is known about the nature of those interactions or their roles in viral replication. In this...

Complete In Vitro Assembly of the Reovirus Outer Capsid Produces Highly Infectious Particles Suitable for Genetic Studies of the Receptor-Binding Protein

Chandran, Kartik, Zhang, Xing, Olson, Norman H., Walker, Stephen B., Chappell, James D., Dermody, Terence S., ...

Mammalian reoviruses, prototype members of the Reoviridae family of nonenveloped double-stranded RNA viruses, use at least three proteins—ς1, μ1, and ς3—to enter host cells. ς1, a major...

Thermostability of Reovirus Disassembly Intermediates (ISVPs) Correlates with Genetic, Biochemical, and Thermodynamic Properties of Major Surface Protein μ1

Middleton, Jason K., Severson, Tonya F., Chandran, Kartik, Gillian, Anne Lynn, Yin, John, Nibert, Max L.

Kinetic analyses of infectivity loss during thermal inactivation of reovirus particles revealed substantial differences between virions and infectious subvirion particles (ISVPs), as well as between...

Sites and Determinants of Early Cleavages in the Proteolytic Processing Pathway of Reovirus Surface Protein σ3†

Jané-Valbuena, Judit, Breun, Laura A., Schiff, Leslie A., Nibert, Max L.

Entry of mammalian reovirus virions into target cells requires proteolytic processing of surface protein σ3. In the virion, σ3 mostly covers the membrane-penetration protein μ1, appearing to keep...

Strategy for Nonenveloped Virus Entry: a Hydrophobic Conformer of the Reovirus Membrane Penetration Protein μ1 Mediates Membrane Disruption†

Chandran, Kartik, Farsetta, Diane L., Nibert, Max L.

The mechanisms employed by nonenveloped animal viruses to penetrate the membranes of their host cells remain enigmatic. Membrane penetration by the nonenveloped mammalian reoviruses is believed to...

The Hydrophilic Amino-Terminal Arm of Reovirus Core Shell Protein λ1 Is Dispensable for Particle Assembly

Kim, Jonghwa, Zhang, Xing, Centonze, Victoria E., Bowman, Valorie D., Noble, Simon, Baker, Timothy S., ...

The reovirus core particle is a molecular machine that mediates synthesis, capping, and export of the viral plus strand RNA transcripts. Its assembly and structure-function relationships remain to be...

Structure of the reovirus outer capsid and dsRNA-binding protein σ3 at 1.8 Å resolution

Olland, Andrea M., Jané-Valbuena, Judit, Schiff, Leslie A., Nibert, Max L., Harrison, Stephen C.

The crystallographically determined structure of the reovirus outer capsid protein σ3 reveals a two-lobed structure organized around a long central helix. The smaller of the two lobes includes a...

Reovirus σNS Protein Localizes to Inclusions through an Association Requiring the μNS Amino Terminus

Miller, Cathy L., Broering, Teresa J., Parker, John S. L., Arnold, Michelle M., Nibert, Max L.

Cells infected with mammalian reoviruses contain phase-dense inclusions, called viral factories, in which viral replication and assembly are thought to occur. The major reovirus nonstructural protein...

Disulfide Bonding among μ1 Trimers in Mammalian Reovirus Outer Capsid: a Late and Reversible Step in Virion Morphogenesis

Odegard, Amy L., Chandran, Kartik, Liemann, Susanne, Harrison, Stephen C., Nibert, Max L.

We examined how a particular type of intermolecular disulfide (ds) bond is formed in the capsid of a cytoplasmically replicating nonenveloped animal virus despite the normally reducing environment...

The Viral σ1 Protein and Glycoconjugates Containing α2-3-Linked Sialic Acid Are Involved in Type 1 Reovirus Adherence to M Cell Apical Surfaces†

Helander, Anna, Silvey, Katherine J., Mantis, Nicholas J., Hutchings, Amy B., Chandran, Kartik, Lucas, William T., ...

Type 1 reoviruses invade the intestinal mucosa of mice by adhering selectively to M cells in the follicle-associated epithelium and then exploiting M cell transport activity. The purpose of this...

The δ Region of Outer-Capsid Protein μ1 Undergoes Conformational Change and Release from Reovirus Particles during Cell Entry

Chandran, Kartik, Parker, John S. L., Ehrlich, Marcelo, Kirchhausen, Tomas, Nibert, Max L.

Cell entry by reoviruses requires a large, transcriptionally active subvirion particle to gain access to the cytoplasm. The features of this particle have been the subject of debate, but three...

Secretory Immunoglobulin A Antibodies against the σ1 Outer Capsid Protein of Reovirus Type 1 Lang Prevent Infection of Mouse Peyer's Patches†

Hutchings, Amy B., Helander, Anna, Silvey, Katherine J., Chandran, Kartik, Lucas, William T., Nibert, Max L., ...

Reovirus type 1 Lang (T1L) adheres to M cells in the follicle-associated epithelium of mouse intestine and exploits the transport activity of M cells to enter and infect the Peyer's patch mucosa....

Reovirus Nonstructural Protein μNS Recruits Viral Core Surface Proteins and Entering Core Particles to Factory-Like Inclusions

Broering, Teresa J., Kim, Jonghwa, Miller, Cathy L., Piggott, Caroline D. S., Dinoso, Jason B., Nibert, Max L., ...

Mammalian reoviruses are thought to assemble and replicate within cytoplasmic, nonmembranous structures called viral factories. The viral nonstructural protein μNS forms factory-like globular...

Putative Autocleavage of Outer Capsid Protein μ1, Allowing Release of Myristoylated Peptide μ1N during Particle Uncoating, Is Critical for Cell Entry by Reovirus

Odegard, Amy L., Chandran, Kartik, Zhang, Xing, Parker, John S. L., Baker, Timothy S., Nibert, Max L.

Several nonenveloped animal viruses possess an autolytic capsid protein that is cleaved as a maturation step during assembly to yield infectious virions. The 76-kDa major outer capsid protein μ1 of...

Increased Ubiquitination and Other Covariant Phenotypes Attributed to a Strain- and Temperature-Dependent Defect of Reovirus Core Protein μ2†

Miller, Cathy L., Parker, John S. L., Dinoso, Jason B., Piggott, Caroline D. S., Perron, Michel J., Nibert, Max L.

Reovirus replication and assembly are thought to occur within cytoplasmic inclusion bodies, which we call viral factories. A strain-dependent difference in the morphology of these structures reflects...

Protective Immunoglobulin A and G Antibodies Bind to Overlapping Intersubunit Epitopes in the Head Domain of Type 1 Reovirus Adhesin σ1

Helander, Anna, Miller, Cathy L., Myers, Kimberly S., Neutra, Marian R., Nibert, Max L.

Nonfusogenic mammalian orthoreovirus (reovirus) is an enteric pathogen of mice and a useful model for studies of how an enteric virus crosses the mucosal barrier of its host and is subject to control...

Carboxyl-Proximal Regions of Reovirus Nonstructural Protein μNS Necessary and Sufficient for Forming Factory-Like Inclusions

Broering, Teresa J., Arnold, Michelle M., Miller, Cathy L., Hurt, Jessica A., Joyce, Patricia L., Nibert, Max L.

Mammalian orthoreoviruses are believed to replicate in distinctive, cytoplasmic inclusion bodies, commonly called viral factories or viroplasms. The viral nonstructural protein μNS has been...

Reovirus Core Protein μ2 Determines the Filamentous Morphology of Viral Inclusion Bodies by Interacting with and Stabilizing Microtubules

Parker, John S. L., Broering, Teresa J., Kim, Jonghwa, Higgins, Darren E., Nibert, Max L.

Cells infected with mammalian reoviruses often contain large perinuclear inclusion bodies, or “factories,” where viral replication and assembly are thought to occur. Here, we report a viral...

Mammalian Reovirus Nonstructural Protein μNS Forms Large Inclusions and Colocalizes with Reovirus Microtubule-Associated Protein μ2 in Transfected Cells

Broering, Teresa J., Parker, John S. L., Joyce, Patricia L., Kim, Jonghwa, Nibert, Max L.

Cells infected with mammalian orthoreoviruses contain large cytoplasmic phase-dense inclusions believed to be the sites of viral replication and assembly, but the morphogenesis, structure, and...

Reovirus Virion-Like Particles Obtained by Recoating Infectious Subvirion Particles with Baculovirus-Expressed ς3 Protein: an Approach for Analyzing ς3 Functions during Virus Entry

Jané-Valbuena, Judit, Nibert, Max L., Spencer, Stephan M., Walker, Stephen B., Baker, Timothy S., Chen, Ya, ...

Structure-function studies with mammalian reoviruses have been limited by the lack of a reverse-genetic system for engineering mutations into the viral genome. To circumvent this limitation in a...

In Vitro Recoating of Reovirus Cores with Baculovirus-Expressed Outer-Capsid Proteins μ1 and ς3

Chandran, Kartik, Walker, Stephen B., Chen, Ya, Contreras, Carlo M., Schiff, Leslie A., Baker, Timothy S., ...

Reovirus outer-capsid proteins μ1, ς3, and ς1 are thought to be assembled onto nascent core-like particles within infected cells, leading to the production of progeny virions. Consistent with this...

Protease Cleavage of Reovirus Capsid Protein μ1/μ1C Is Blocked by Alkyl Sulfate Detergents, Yielding a New Type of Infectious Subvirion Particle

Chandran, Kartik, Nibert, Max L.

Mammalian reovirus virions undergo partial disassembly of the outer capsid upon exposure to proteases in vitro, producing infectious subvirion particles (ISVPs) that lack protein ς3 and contain...

Cleavage Susceptibility of Reovirus Attachment Protein ς1 during Proteolytic Disassembly of Virions Is Determined by a Sequence Polymorphism in the ς1 Neck

Chappell, James D., Barton, Erik S., Smith, Trent H., Baer, Geoffrey S., Duong, David T., Nibert, Max L., ...

A requisite step in reovirus infection of the murine intestine is proteolysis of outer-capsid proteins to yield infectious subvirion particles (ISVPs). When converted to ISVPs by intestinal...

Reovirus Nonstructural Protein μNS Binds to Core Particles but Does Not Inhibit Their Transcription and Capping Activities

Broering, Teresa J., McCutcheon, Aimee M., Centonze, Victoria E., Nibert, Max L.

Previous studies provided evidence that nonstructural protein μNS of mammalian reoviruses is present in particle assembly intermediates isolated from infected cells. Morgan and Zweerink (Virology...

Reovirus Protein ςNS Binds in Multiple Copies to Single-Stranded RNA and Shares Properties with Single-Stranded DNA Binding Proteins

Gillian, Anne Lynn, Schmechel, Stephen C., Livny, Jonathan, Schiff, Leslie A., Nibert, Max L.

Reovirus nonstructural protein ςNS interacts with reovirus plus-strand RNAs in infected cells, but little is known about the nature of those interactions or their roles in viral replication. In this...

Complete In Vitro Assembly of the Reovirus Outer Capsid Produces Highly Infectious Particles Suitable for Genetic Studies of the Receptor-Binding Protein

Chandran, Kartik, Zhang, Xing, Olson, Norman H., Walker, Stephen B., Chappell, James D., Dermody, Terence S., ...

Mammalian reoviruses, prototype members of the Reoviridae family of nonenveloped double-stranded RNA viruses, use at least three proteins—ς1, μ1, and ς3—to enter host cells. ς1, a major...

Thermostability of Reovirus Disassembly Intermediates (ISVPs) Correlates with Genetic, Biochemical, and Thermodynamic Properties of Major Surface Protein μ1

Middleton, Jason K., Severson, Tonya F., Chandran, Kartik, Gillian, Anne Lynn, Yin, John, Nibert, Max L.

Kinetic analyses of infectivity loss during thermal inactivation of reovirus particles revealed substantial differences between virions and infectious subvirion particles (ISVPs), as well as between...

Sites and Determinants of Early Cleavages in the Proteolytic Processing Pathway of Reovirus Surface Protein σ3†

Jané-Valbuena, Judit, Breun, Laura A., Schiff, Leslie A., Nibert, Max L.

Entry of mammalian reovirus virions into target cells requires proteolytic processing of surface protein σ3. In the virion, σ3 mostly covers the membrane-penetration protein μ1, appearing to keep...

Strategy for Nonenveloped Virus Entry: a Hydrophobic Conformer of the Reovirus Membrane Penetration Protein μ1 Mediates Membrane Disruption†

Chandran, Kartik, Farsetta, Diane L., Nibert, Max L.

The mechanisms employed by nonenveloped animal viruses to penetrate the membranes of their host cells remain enigmatic. Membrane penetration by the nonenveloped mammalian reoviruses is believed to...

The Hydrophilic Amino-Terminal Arm of Reovirus Core Shell Protein λ1 Is Dispensable for Particle Assembly

Kim, Jonghwa, Zhang, Xing, Centonze, Victoria E., Bowman, Valorie D., Noble, Simon, Baker, Timothy S., ...

The reovirus core particle is a molecular machine that mediates synthesis, capping, and export of the viral plus strand RNA transcripts. Its assembly and structure-function relationships remain to be...

Structure of the reovirus outer capsid and dsRNA-binding protein σ3 at 1.8 Å resolution

Olland, Andrea M., Jané-Valbuena, Judit, Schiff, Leslie A., Nibert, Max L., Harrison, Stephen C.

The crystallographically determined structure of the reovirus outer capsid protein σ3 reveals a two-lobed structure organized around a long central helix. The smaller of the two lobes includes a...

Reovirus σNS Protein Localizes to Inclusions through an Association Requiring the μNS Amino Terminus

Miller, Cathy L., Broering, Teresa J., Parker, John S. L., Arnold, Michelle M., Nibert, Max L.

Cells infected with mammalian reoviruses contain phase-dense inclusions, called viral factories, in which viral replication and assembly are thought to occur. The major reovirus nonstructural protein...

Disulfide Bonding among μ1 Trimers in Mammalian Reovirus Outer Capsid: a Late and Reversible Step in Virion Morphogenesis

Odegard, Amy L., Chandran, Kartik, Liemann, Susanne, Harrison, Stephen C., Nibert, Max L.

We examined how a particular type of intermolecular disulfide (ds) bond is formed in the capsid of a cytoplasmically replicating nonenveloped animal virus despite the normally reducing environment...

Reovirus Core Protein μ2 Determines the Filamentous Morphology of Viral Inclusion Bodies by Interacting with and Stabilizing Microtubules

Parker, John S. L., Broering, Teresa J., Kim, Jonghwa, Higgins, Darren E., Nibert, Max L.

Cells infected with mammalian reoviruses often contain large perinuclear inclusion bodies, or “factories,” where viral replication and assembly are thought to occur. Here, we report a viral...

Mammalian Reovirus Nonstructural Protein μNS Forms Large Inclusions and Colocalizes with Reovirus Microtubule-Associated Protein μ2 in Transfected Cells

Broering, Teresa J., Parker, John S. L., Joyce, Patricia L., Kim, Jonghwa, Nibert, Max L.

Cells infected with mammalian orthoreoviruses contain large cytoplasmic phase-dense inclusions believed to be the sites of viral replication and assembly, but the morphogenesis, structure, and...

The Viral σ1 Protein and Glycoconjugates Containing α2-3-Linked Sialic Acid Are Involved in Type 1 Reovirus Adherence to M Cell Apical Surfaces†

Helander, Anna, Silvey, Katherine J., Mantis, Nicholas J., Hutchings, Amy B., Chandran, Kartik, Lucas, William T., ...

Type 1 reoviruses invade the intestinal mucosa of mice by adhering selectively to M cells in the follicle-associated epithelium and then exploiting M cell transport activity. The purpose of this...

The δ Region of Outer-Capsid Protein μ1 Undergoes Conformational Change and Release from Reovirus Particles during Cell Entry

Chandran, Kartik, Parker, John S. L., Ehrlich, Marcelo, Kirchhausen, Tomas, Nibert, Max L.

Cell entry by reoviruses requires a large, transcriptionally active subvirion particle to gain access to the cytoplasm. The features of this particle have been the subject of debate, but three...

Secretory Immunoglobulin A Antibodies against the σ1 Outer Capsid Protein of Reovirus Type 1 Lang Prevent Infection of Mouse Peyer's Patches†

Hutchings, Amy B., Helander, Anna, Silvey, Katherine J., Chandran, Kartik, Lucas, William T., Nibert, Max L., ...

Reovirus type 1 Lang (T1L) adheres to M cells in the follicle-associated epithelium of mouse intestine and exploits the transport activity of M cells to enter and infect the Peyer's patch mucosa....

Reovirus Nonstructural Protein μNS Recruits Viral Core Surface Proteins and Entering Core Particles to Factory-Like Inclusions

Broering, Teresa J., Kim, Jonghwa, Miller, Cathy L., Piggott, Caroline D. S., Dinoso, Jason B., Nibert, Max L., ...

Mammalian reoviruses are thought to assemble and replicate within cytoplasmic, nonmembranous structures called viral factories. The viral nonstructural protein μNS forms factory-like globular...

Putative Autocleavage of Outer Capsid Protein μ1, Allowing Release of Myristoylated Peptide μ1N during Particle Uncoating, Is Critical for Cell Entry by Reovirus

Odegard, Amy L., Chandran, Kartik, Zhang, Xing, Parker, John S. L., Baker, Timothy S., Nibert, Max L.

Several nonenveloped animal viruses possess an autolytic capsid protein that is cleaved as a maturation step during assembly to yield infectious virions. The 76-kDa major outer capsid protein μ1 of...

Increased Ubiquitination and Other Covariant Phenotypes Attributed to a Strain- and Temperature-Dependent Defect of Reovirus Core Protein μ2†

Miller, Cathy L., Parker, John S. L., Dinoso, Jason B., Piggott, Caroline D. S., Perron, Michel J., Nibert, Max L.

Reovirus replication and assembly are thought to occur within cytoplasmic inclusion bodies, which we call viral factories. A strain-dependent difference in the morphology of these structures reflects...

Protective Immunoglobulin A and G Antibodies Bind to Overlapping Intersubunit Epitopes in the Head Domain of Type 1 Reovirus Adhesin σ1

Helander, Anna, Miller, Cathy L., Myers, Kimberly S., Neutra, Marian R., Nibert, Max L.

Nonfusogenic mammalian orthoreovirus (reovirus) is an enteric pathogen of mice and a useful model for studies of how an enteric virus crosses the mucosal barrier of its host and is subject to control...

Carboxyl-Proximal Regions of Reovirus Nonstructural Protein μNS Necessary and Sufficient for Forming Factory-Like Inclusions

Broering, Teresa J., Arnold, Michelle M., Miller, Cathy L., Hurt, Jessica A., Joyce, Patricia L., Nibert, Max L.

Mammalian orthoreoviruses are believed to replicate in distinctive, cytoplasmic inclusion bodies, commonly called viral factories or viroplasms. The viral nonstructural protein μNS has been...

Reovirus Outer Capsid Protein μ1 Induces Apoptosis and Associates with Lipid Droplets, Endoplasmic Reticulum, and Mitochondria

Coffey, Caroline M., Sheh, Alexander, Kim, Irene S., Chandran, Kartik, Nibert, Max L., Parker, John S. L.

The mechanisms by which reoviruses induce apoptosis have not been fully elucidated. Earlier studies identified the mammalian reovirus S1 and M2 genes as determinants of apoptosis induction. However,...

Reovirus μ1 Structural Rearrangements That Mediate Membrane Penetration▿

Zhang, Lan, Chandran, Kartik, Nibert, Max L., Harrison, Stephen C.

Membrane penetration by nonenveloped reoviruses is mediated by the outer-capsid protein, μ1 (76 kDa). Previous evidence has suggested that an autolytic cleavage in μ1 allows the release of its...

Mammalian reovirus, a nonfusogenic nonenveloped virus, forms size-selective pores in a model membrane

Agosto, Melina A., Ivanovic, Tijana, Nibert, Max L.

During cell entry, reovirus particles with a diameter of 70–80 nm must penetrate the cellular membrane to access the cytoplasm. The mechanism of penetration, without benefit of membrane fusion, is...

Guanidine Hydrochloride Inhibits Mammalian Orthoreovirus Growth by Reversibly Blocking the Synthesis of Double-Stranded RNA▿

Murray, Kenneth E., Nibert, Max L.

Millimolar concentrations of guanidine hydrochloride (GuHCl) are known to inhibit the replication of many plant and animal viruses having positive-sense RNA genomes. For example, GuHCl reversibly...

Thermolabilizing Pseudoreversions in Reovirus Outer-Capsid Protein μ1 Rescue the Entry Defect Conferred by a Thermostabilizing Mutation▿

Agosto, Melina A., Middleton, Jason K., Freimont, Elaine C., Yin, John, Nibert, Max L.

Heat-resistant mutants selected from infectious subvirion particles of mammalian reoviruses have determinative mutations in the major outer-capsid protein μ1. Here we report the isolation and...

Human Papillomavirus Type 16 E7 Oncoprotein Associates with the Centrosomal Component γ-Tubulin▿

Nguyen, Christine L., Eichwald, Catherine, Nibert, Max L., Münger, Karl

Expression of a high-risk human papillomavirus (HPV) E7 oncoprotein is sufficient to induce aberrant centrosome duplication in primary human cells. The resulting centrosome-associated mitotic...

A positive-feedback mechanism promotes reovirus particle conversion to the intermediate associated with membrane penetration

Agosto, Melina A., Myers, Kimberly S., Ivanovic, Tijana, Nibert, Max L.

Membrane penetration by reovirus is associated with conversion of a metastable intermediate, the ISVP, to a further-disassembled particle, the ISVP*. Factors that promote this conversion in cells are...

Peptides released from reovirus outer capsid form membrane pores that recruit virus particles

Ivanovic, Tijana, Agosto, Melina A, Zhang, Lan, Chandran, Kartik, Harrison, Stephen C, Nibert, Max L

Nonenveloped animal viruses must disrupt or perforate a cell membrane during entry. Recent work with reovirus has shown formation of size-selective pores in RBC membranes in concert with structural...

Infectious myonecrosis virus has a totivirus-like, 120-subunit capsid, but with fiber complexes at the fivefold axes

Tang, Jinghua, Ochoa, Wendy F., Sinkovits, Robert S., Poulos, Bonnie T., Ghabrial, Said A., Lightner, Donald V., ...

Infectious myonecrosis virus (IMNV) is an emerging pathogen of penaeid shrimp in global aquaculture. Tentatively assigned to family Totiviridae, it has a nonsegmented dsRNA genome of 7,560 bp and an...

Atomic structure reveals the unique capsid organization of a dsRNA virus

Pan, Junhua, Dong, Liping, Lin, Li, Ochoa, Wendy F., Sinkovits, Robert S., Havens, Wendy M., ...

For most dsRNA viruses, the genome-enclosing capsid comprises 120 copies of a single capsid protein (CP) organized into 60 icosahedrally equivalent dimers, generally identified as 2...