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Article: Editorial: HTLV-1: addressing unmet research needs, volume II.

Cunha, Marcela S / Zhang, Wei / Mansky, Louis M / Mendonça, Luiza M

2023 Volume 14, Page(s) 1306416

Language	English
Publishing date	2023-10-26
Publishing country	Switzerland
Document type	Editorial
ZDB-ID	2587354-4
ISSN	1664-302X
ISSN	1664-302X
DOI	10.3389/fmicb.2023.1306416
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Article ; Online: Structural Analysis of Retrovirus Assembly and Maturation.

Krebs, Anna-Sophia / Mendonça, Luiza M / Zhang, Peijun

Viruses

2021 Volume 14, Issue 1

Abstract: Retroviruses have a very complex and tightly controlled life cycle which has been studied intensely for decades. After a virus enters the cell, it reverse-transcribes its genome, which is then integrated into the host genome, and subsequently all ... ...

Abstract	Retroviruses have a very complex and tightly controlled life cycle which has been studied intensely for decades. After a virus enters the cell, it reverse-transcribes its genome, which is then integrated into the host genome, and subsequently all structural and regulatory proteins are transcribed and translated. The proteins, along with the viral genome, assemble into a new virion, which buds off the host cell and matures into a newly infectious virion. If any one of these steps are faulty, the virus cannot produce infectious viral progeny. Recent advances in structural and molecular techniques have made it possible to better understand this class of viruses, including details about how they regulate and coordinate the different steps of the virus life cycle. In this review we summarize the molecular analysis of the assembly and maturation steps of the life cycle by providing an overview on structural and biochemical studies to understand these processes. We also outline the differences between various retrovirus families with regards to these processes.
MeSH term(s)	Capsid/metabolism ; Cryoelectron Microscopy ; Genome, Viral ; HIV-1/genetics ; HIV-1/physiology ; HIV-1/ultrastructure ; Humans ; Models, Molecular ; Retroviridae/genetics ; Retroviridae/physiology ; Retroviridae/ultrastructure ; Virion/metabolism ; Virus Assembly/physiology
Language	English
Publishing date	2021-12-29
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v14010054
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Article: Structural Analysis of Retrovirus Assembly and Maturation

Krebs, Anna-Sophia / Mendonça, Luiza M. / Zhang, Peijun

Viruses. 2021 Dec. 29, v. 14, no. 1

2021

Abstract	Retroviruses have a very complex and tightly controlled life cycle which has been studied intensely for decades. After a virus enters the cell, it reverse-transcribes its genome, which is then integrated into the host genome, and subsequently all structural and regulatory proteins are transcribed and translated. The proteins, along with the viral genome, assemble into a new virion, which buds off the host cell and matures into a newly infectious virion. If any one of these steps are faulty, the virus cannot produce infectious viral progeny. Recent advances in structural and molecular techniques have made it possible to better understand this class of viruses, including details about how they regulate and coordinate the different steps of the virus life cycle. In this review we summarize the molecular analysis of the assembly and maturation steps of the life cycle by providing an overview on structural and biochemical studies to understand these processes. We also outline the differences between various retrovirus families with regards to these processes.
Keywords	Retroviridae ; progeny ; viral genome ; virion ; viruses
Language	English
Dates of publication	2021-1229
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
ZDB-ID	2516098-9
ISSN	1999-4915
ISSN	1999-4915
DOI	10.3390/v14010054
Database	NAL-Catalogue (AGRICOLA)

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Article: The Retrovirus Capsid Core.

Zhang, Wei / Mendonça, Luiza M / Mansky, Louis M

Sub-cellular biochemistry

2018 Volume 88, Page(s) 169–187

Abstract: The retrovirus capsid core is a metastable structure that disassembles during the early phase of viral infection after membrane fusion. The core is intact and permeable to essential nucleotides during reverse transcription, but it undergoes disassembly ... ...

Abstract	The retrovirus capsid core is a metastable structure that disassembles during the early phase of viral infection after membrane fusion. The core is intact and permeable to essential nucleotides during reverse transcription, but it undergoes disassembly for nuclear entry and genome integration. Increasing or decreasing the stability of the capsid core has a substantial negative impact on virus infectivity, which makes the core an attractive anti-viral target. The retrovirus capsid core also encounters a variety of virus- and organism-specific host cellular factors that promote or restrict viral replication. This review describes the structural elements fundamental to the formation and stability of the capsid core. The physical and chemical properties of the capsid core that are critical to its functional role in reverse transcription and interaction with host cellular factors are highlighted to emphasize areas of current research.
MeSH term(s)	Animals ; Capsid/metabolism ; Humans ; Retroviridae/pathogenicity ; Reverse Transcription/physiology ; Virus Integration/physiology ; Virus Internalization ; Virus Replication/physiology
Language	English
Publishing date	2018-05-25
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ISSN	0306-0225 ; 0096-8757
ISSN	0306-0225 ; 0096-8757
DOI	10.1007/978-981-10-8456-0_8
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Article: Correction to: The Retrovirus Capsid Core.

Zhang, Wei / Mendonça, Luiza M / Mansky, Louis M

Sub-cellular biochemistry

2018 Volume 88, Page(s) E1

Abstract: In the original publication, the names of the second and third authors were incorrectly published. ...

Abstract	In the original publication, the names of the second and third authors were incorrectly published.
Language	English
Publishing date	2018-11-27
Publishing country	United States
Document type	Journal Article ; Published Erratum
ISSN	0306-0225 ; 0096-8757
ISSN	0306-0225 ; 0096-8757
DOI	10.1007/978-981-10-8456-0_18
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Article ; Online: UVC inactivation of pathogenic samples suitable for cryo-EM analysis.

Depelteau, Jamie S / Renault, Ludovic / Althof, Nynke / Cassidy, C Keith / Mendonça, Luiza M / Jensen, Grant J / Resch, Guenter P / Briegel, Ariane

Communications biology

2022 Volume 5, Issue 1, Page(s) 29

Abstract: Cryo-electron microscopy has become an essential tool to understand structure and function of biological samples. Especially for pathogens, such as disease-causing bacteria and viruses, insights gained by cryo-EM can aid in developing cures. However, due ...

Abstract	Cryo-electron microscopy has become an essential tool to understand structure and function of biological samples. Especially for pathogens, such as disease-causing bacteria and viruses, insights gained by cryo-EM can aid in developing cures. However, due to the biosafety restrictions of pathogens, samples are often treated by chemical fixation to render the pathogen inert, affecting the ultrastructure of the sample. Alternatively, researchers use in vitro or ex vivo models, which are non-pathogenic but lack the complexity of the pathogen of interest. Here we show that ultraviolet-C (UVC) radiation applied at cryogenic temperatures can be used to eliminate or dramatically reduce the infectivity of Vibrio cholerae and the bacterial virus, the ICP1 bacteriophage. We show no discernable structural impact of this treatment of either sample using two cryo-EM methods: cryo-electron tomography followed by sub-tomogram averaging, and single particle analysis (SPA). Additionally, we applied the UVC irradiation to the protein apoferritin (ApoF), which is a widely used test sample for high-resolution SPA studies. The UVC-treated ApoF sample resulted in a 2.1 Å structure indistinguishable from an untreated published map. This research demonstrates that UVC treatment is an effective and inexpensive addition to the cryo-EM sample preparation toolbox.
MeSH term(s)	Bacteria/pathogenicity ; Bacteria/radiation effects ; Chemotaxis/radiation effects ; Cryoelectron Microscopy ; Ultraviolet Rays ; Vibrio cholerae/pathogenicity ; Vibrio cholerae/radiation effects ; Viruses/pathogenicity ; Viruses/radiation effects
Language	English
Publishing date	2022-01-11
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2399-3642
ISSN (online)	2399-3642
DOI	10.1038/s42003-021-02962-w
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Article ; Online: HIV-2 Immature Particle Morphology Provides Insights into Gag Lattice Stability and Virus Maturation.

Talledge, Nathaniel / Yang, Huixin / Shi, Ke / Coray, Raffaele / Yu, Guichuan / Arndt, William G / Meng, Shuyu / Baxter, Gloria C / Mendonça, Luiza M / Castaño-Díez, Daniel / Aihara, Hideki / Mansky, Louis M / Zhang, Wei

Journal of molecular biology

2023 Volume 435, Issue 15, Page(s) 168143

Abstract: Retrovirus immature particle morphology consists of a membrane enclosed, pleomorphic, spherical and incomplete lattice of Gag hexamers. Previously, we demonstrated that human immunodeficiency virus type 2 (HIV-2) immature particles possess a distinct and ...

Abstract	Retrovirus immature particle morphology consists of a membrane enclosed, pleomorphic, spherical and incomplete lattice of Gag hexamers. Previously, we demonstrated that human immunodeficiency virus type 2 (HIV-2) immature particles possess a distinct and extensive Gag lattice morphology. To better understand the nature of the continuously curved hexagonal Gag lattice, we have used the single particle cryo-electron microscopy method to determine the HIV-2 Gag lattice structure for immature virions. The reconstruction map at 5.5 Å resolution revealed a stable, wineglass-shaped Gag hexamer structure with structural features consistent with other lentiviral immature Gag lattice structures. Cryo-electron tomography provided evidence for nearly complete ordered Gag lattice structures in HIV-2 immature particles. We also solved a 1.98 Å resolution crystal structure of the carboxyl-terminal domain (CTD) of the HIV-2 capsid (CA) protein that identified a structured helix 12 supported via an interaction of helix 10 in the absence of the SP1 region of Gag. Residues at the helix 10-12 interface proved critical in maintaining HIV-2 particle release and infectivity. Taken together, our findings provide the first 3D organization of HIV-2 immature Gag lattice and important insights into both HIV Gag lattice stabilization and virus maturation.
MeSH term(s)	Humans ; Capsid Proteins/chemistry ; Cryoelectron Microscopy ; gag Gene Products, Human Immunodeficiency Virus/chemistry ; HIV-2/chemistry ; Virion/chemistry ; Virus Assembly
Chemical Substances	Capsid Proteins ; gag Gene Products, Human Immunodeficiency Virus
Language	English
Publishing date	2023-05-06
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2023.168143
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Article ; Online: HIV-2 Immature Particle Morphology Provides Insights into Gag Lattice Stability and Virus Maturation

Talledge, Nathaniel / Yang, Huixin / Shi, Ke / Coray, Raffaele / Yu, Guichuan / Arndt, William G. / Meng, Shuyu / Baxter, Gloria C. / Mendonça, Luiza M. / Castaño-Díez, Daniel / Aihara, Hideki / Mansky, Louis M. / Zhang, Wei

Journal of Molecular Biology. 2023 Aug., v. 435, no. 15 p.168143-

2023

Abstract	Retrovirus immature particle morphology consists of a membrane enclosed, pleomorphic, spherical and incomplete lattice of Gag hexamers. Previously, we demonstrated that human immunodeficiency virus type 2 (HIV-2) immature particles possess a distinct and extensive Gag lattice morphology. To better understand the nature of the continuously curved hexagonal Gag lattice, we have used the single particle cryo-electron microscopy method to determine the HIV-2 Gag lattice structure for immature virions. The reconstruction map at 5.5 Å resolution revealed a stable, wineglass-shaped Gag hexamer structure with structural features consistent with other lentiviral immature Gag lattice structures. Cryo-electron tomography provided evidence for nearly complete ordered Gag lattice structures in HIV-2 immature particles. We also solved a 1.98 Å resolution crystal structure of the carboxyl-terminal domain (CTD) of the HIV-2 capsid (CA) protein that identified a structured helix 12 supported via an interaction of helix 10 in the absence of the SP1 region of Gag. Residues at the helix 10–12 interface proved critical in maintaining HIV-2 particle release and infectivity. Taken together, our findings provide the first 3D organization of HIV-2 immature Gag lattice and important insights into both HIV Gag lattice stabilization and virus maturation.
Keywords	Human immunodeficiency virus 2 ; capsid ; cryo-electron microscopy ; crystal structure ; molecular biology ; pathogenicity ; tomography ; viruses ; retrovirus ; lentivirus ; morphology ; virus assembly
Language	English
Dates of publication	2023-08
Publishing place	Elsevier Ltd
Document type	Article ; Online
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2023.168143
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Article ; Online: Polymorphic Nature of Human T-Cell Leukemia Virus Type 1 Particle Cores as Revealed through Characterization of a Chronically Infected Cell Line.

Meissner, Morgan E / Mendonça, Luiza M / Zhang, Wei / Mansky, Louis M

Journal of virology

2017 Volume 91, Issue 16

Abstract: Human T-cell leukemia virus type 1 (HTLV-1) is the etiological agent of adult T-cell leukemia (ATL) and HTLV-1-associated myelopathy/tropical spastic paraparesis (HAM/TSP). HTLV-1 cell-to-cell transmission is dependent on the release of infectious virus ... ...

Abstract	Human T-cell leukemia virus type 1 (HTLV-1) is the etiological agent of adult T-cell leukemia (ATL) and HTLV-1-associated myelopathy/tropical spastic paraparesis (HAM/TSP). HTLV-1 cell-to-cell transmission is dependent on the release of infectious virus particles into the virological synapse. The HTLV-1 particle structure is still poorly understood, and previous studies analyzed viruses produced by transformed lymphocytic cell lines chronically infected with HTLV-1, particularly the MT-2 cell line, which harbors truncated proviruses and expresses aberrant forms of the Gag protein. In this study, we demonstrate that the chronically infected SP cell line harbors a relatively low number of proviruses, making it a more promising experimental system for the study of the HTLV-1 particle structure. We first identified the genomic sites of integration and characterized the genetic structure of the
MeSH term(s)	Cell Line ; Cryoelectron Microscopy ; Deltaretrovirus/genetics ; Deltaretrovirus/physiology ; Deltaretrovirus/ultrastructure ; Humans ; Proviruses/genetics ; Virion/ultrastructure ; Virus Integration
Language	English
Publishing date	2017-08-15
Publishing country	United States
Document type	Journal Article
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.00369-17
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Article ; Online: Direct visualization of vaults within intact cells by electron cryo-tomography.

Woodward, Cora L / Mendonça, Luiza M / Jensen, Grant J

Cellular and molecular life sciences : CMLS

2015 Volume 72, Issue 17, Page(s) 3401–3409

Abstract: The vault complex is the largest cellular ribonucleoprotein complex ever characterized and is present across diverse Eukarya. Despite significant information regarding the structure, composition and evolutionary conservation of the vault, little is know ... ...

Abstract	The vault complex is the largest cellular ribonucleoprotein complex ever characterized and is present across diverse Eukarya. Despite significant information regarding the structure, composition and evolutionary conservation of the vault, little is know about the complex's actual biological function. To determine if intracellular vaults are morphologically similar to previously studied purified and recombinant vaults, we have used electron cryo-tomography to characterize the vault complexes found in the thin edges of primary human cells growing in tissue culture. Our studies confirm that intracellular vaults are similar in overall size and shape to purified and recombinant vaults previously analyzed. Results from subtomogram averaging indicate that densities within the vault lumen are not ordered, but randomly distributed. We also observe that vaults located in the extreme periphery of the cytoplasm predominately associate with granule-like structures and actin. Our ultrastructure studies augment existing biochemical, structural and genetic information on the vault, and provide important intracellular context for the ongoing efforts to understand the biological function of the native cytoplasmic vault.
MeSH term(s)	Cells, Cultured ; Cryoelectron Microscopy/methods ; Electron Microscope Tomography/methods ; Humans ; Vault Ribonucleoprotein Particles/ultrastructure
Chemical Substances	Vault Ribonucleoprotein Particles
Language	English
Publishing date	2015-09
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1358415-7
ISSN	1420-9071 ; 1420-682X
ISSN (online)	1420-9071
ISSN	1420-682X
DOI	10.1007/s00018-015-1898-y
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