Atomic structure of the human cytomegalovirus capsid with its securing tegument layer of pp150

Yu, Xuekui; Jih, Jonathan; Jiang, Junchen; Zh, Zhou

doi:10.1126/science.aam6892

Cited by 112 publications

(202 citation statements)

References 65 publications

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“…Instead, the Tri1 monomer inserts its N-terminal extension (N anchor) through the capsid floor and folds into a tri-lobed structure inside the capsid (Fig. 3, C, D, and L) (20, 28), anchoring the entire triplex. Selection pressure to mediate binding of divergent tegument proteins outside the capsid and to accommodate genomes of varying sizes inside the capsid could have also forced Tri1 to diverge on both its outer and inner sides.…”

Section: Bacteriophage-related Motif and α-Herpesvirus–specific Featumentioning

confidence: 99%

“…Selection pressure to mediate binding of divergent tegument proteins outside the capsid and to accommodate genomes of varying sizes inside the capsid could have also forced Tri1 to diverge on both its outer and inner sides. Indeed, the Tri1 insertional arm, which emanates from a topologically similar location on one of the two β barrels as that of the Tri2 embracing arm, is the most externally located and is completely missing in HCMV Tri1 (20) and KSHV Tri1 (28). Likewise, the genome-facing N anchor of HSV-1 Tri1 is substantially longer than (102 versus 44 amino acids), and not as rigid as, that of HCMV (20).…”

Section: Bacteriophage-related Motif and α-Herpesvirus–specific Featumentioning

confidence: 99%

“…Like that of HCMV or KSHV (20, 28), the HSV-1 MCP (VP5) subunit can be thought of as an extensive elaboration on a central bacteriophage HK97 gp5–like (“Johnson”) fold (amino acids 51 to 193, 232 to 298, 365 to 396, 1061 to 1113), with six additional domains, including the N lasso (1 to 50), dimerization (299 to 364), helix-hairpin (194 to 231), channel (407 to 480, 1335 to 1374), buttress (397 to 406, 1048 to 1060, 1114 to 1334) and upper (481 to 1047) domains (Fig. 4A).…”

Section: Hsv-1–specific Features In the Scp And Mcpmentioning

confidence: 99%

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Structure of the herpes simplex virus 1 capsid with associated tegument protein complexes

Dai

2018

Science

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INTRODUCTION Since Hippocrates first described the cutaneous spreading of herpes simplex lesions, many other diseases—chickenpox, infectious mononucleosis, nasopharyngeal carcinoma, and Kaposi’s sarcoma—have been found to be associated with the nine known human herpesviruses. Among them, herpes simplex virus type 1 (HSV-1, causes cold sores), type 2 (HSV-2, causes genital herpes), and varicella-zoster virus (causes chickenpox and shingles)—which all belong to the α-herpesvirus subfamily—can establish lifelong latent infection within our peripheral nervous system. RATIONALE A prominent feature of these neurotropic viruses is the long-range (up to tens of centimeters) axonal retrograde transport of the DNA-containing viral capsid from nerve endings at sites of infection (such as the lips) to neuronal cell bodies at the ganglia to establish latency or, upon reactivation, anterograde transport of the progeny viral particles from the ganglia to nerve terminals, resulting in reinfection of the dermis. Capsid-associated tegument complexes (CATCs) have been demonstrated to be involved in this cytoskeleton-dependent capsid transport. Because of the large size (~1300 Å) of HSV-1 particles, it has been difficult to obtain atomic structures of the HSV-1 capsid and CATC; consequently, the structural bases underlying α-herpesviruses’ remarkable capability of long-range neuronal transport and many other aspects of its life cycle are poorly understood. RESULTS By using cryo–electron microscopy, we obtained an atomic model of the HSV-1 capsid with CATC, comprising multiple conformers of the capsid proteins VP5, VP19c, VP23, and VP26 and tegument proteins pUL17, pUL25, and pUL36. Crowning every capsid vertex are five copies of heteropentameric CATC. The pUL17 monomer in each CATC bridges over triplexes Ta and Tc on the capsid surface and supports a coiled-coil helix bundle of a pUL25 dimer and a pUL36 dimer, thus positioning their flexible domains for potential involvement in nuclear egress and axonal transport of the capsid. The single C-terminal helix of pUL36 resolved in the CATC links the capsid to the outer tegument and envelope: As the largest tegument protein in all herpesviruses and essential for virion formation, pUL36 has been shown to interact extensively with other tegument proteins, which in turn interact with envelope glycoproteins. Architectural similarities between herpesvirus triplex proteins and auxiliary cementing protein gpD in bacteriophage λ, in addition to the bacteriophage HK97 gp5–like folds in their major capsid proteins and structural similarities in their DNA packaging and delivery apparatuses, indicate that the commonality between bacteriophages and herpes-viruses extends to their auxiliary components. Notwithstanding this broad evolutionary conservation, comparison of HSV-1 capsid proteins with those of other herpesviruses revealed extraordinary structural diversities in the forms of domain insertion and conformation polymorphism, not only for tegument interactions but also for DNA encapsulation...

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Section: Bacteriophage-related Motif and α-Herpesvirus–specific Featumentioning

confidence: 99%

Section: Bacteriophage-related Motif and α-Herpesvirus–specific Featumentioning

confidence: 99%

Section: Hsv-1–specific Features In the Scp And Mcpmentioning

confidence: 99%

See 1 more Smart Citation

Structure of the herpes simplex virus 1 capsid with associated tegument protein complexes

Dai

2018

Science

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“…In PRV, the lack of SCP on the PRV penton and the longer N-terminal region of pUL25 seem to have enabled each pUL25 to bind two penton MCPs. The PRV pUL17 binds to two hexon MCP and it bends 40 compared to KSHV pORF32, which only binds to one hexon MCP.…”

Section: Discussionmentioning

confidence: 99%

“…By contrast, bherpesviruses possess a capsid-associated tegument protein, pp150, that forms a proteinaceous net enclosing the entire capsid, presumably to buttress it against the internal pressure of their large genomes [36][37][38][39][40]. In both cases, CATCs are essential for virus propagation [32,41,42].…”

Section: Introductionmentioning

confidence: 99%

A pUL25 dimer interfaces the pseudorabies virus capsid and tegument

Liu

Jiang

Bohannon

et al. 2017

Journal of General Virology

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Inside the virions of a-herpesviruses, tegument protein pUL25 anchors the tegument to capsid vertices through direct interactions with tegument proteins pUL17 and pUL36. In addition to promoting virion assembly, both pUL25 and pUL36 are critical for intracellular microtubule-dependent capsid transport. Despite these essential roles during infection, the stoichiometry and precise organization of pUL25 and pUL36 on the capsid surface remain controversial due to the insufficient resolution of existing reconstructions from cryo-electron microscopy (cryoEM). Here, we report a threedimensional (3D) icosahedral reconstruction of pseudorabies virus (PRV), a varicellovirus of the a-herpesvirinae subfamily, obtained by electron-counting cryoEM at 4.9 Å resolution. Our reconstruction resolves a dimer of pUL25 forming a capsidassociated tegument complex with pUL36 and pUL17 through a coiled coil helix bundle, thus correcting previous misinterpretations. A comparison between reconstructions of PRV and the g-herpesvirus Kaposi's sarcoma-associated herpesvirus (KSHV) reinforces their similar architectures and establishes important subfamily differences in the capsidtegument interface.

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Strong and Tough Physical Eutectogels Regulated by the Spatiotemporal Expression of Non‐Covalent Interactions

Zhang

Tang

et al. 2022

Adv Funct Materials

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Physical eutectogels are appealing materials for technological devices due to their superior ionic conductivity, thermal and electrochemical stability, non-volatility, and low cost. Nevertheless, current physical eutectogels are suffering from weak mechanical strength and toughness. Here, taking advantage of the distribution difference of polyvinyl alcohol (PVA) in water and deep eutectic solvents (DESs), a simple and universal solvent-replacement approach is proposed to regulate the spatiotemporal expression of intra/ interpolymer interactions to prepare strong and tough physical eutectogels. The exchange of DESs with water can restrengthen the weakened interactions between PVA chains in water, enabling PVA to crystallize to construct a uniform and robust polymer network. Consequently, the resultant PVA eutectogel exhibits record-high strength (20.2 MPa), toughness (62.7 MJ m -3 ), and tear-resistance (tearing energy Σ42.4 kJ m -2 ), while possessing excellent stretchability (Σ550% strain), repairability, and adhesive performance. Furthermore, this strategy is proven to be universally applicable to various species of polymers, and even can be utilized to fabricate continuous and conductive eutectogel fibers, demonstrating potential as engineering materials and wearable sensors.

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Atomic structure of the human cytomegalovirus capsid with its securing tegument layer of pp150

Cited by 112 publications

References 65 publications

Structure of the herpes simplex virus 1 capsid with associated tegument protein complexes

Structure of the herpes simplex virus 1 capsid with associated tegument protein complexes

A pUL25 dimer interfaces the pseudorabies virus capsid and tegument

Strong and Tough Physical Eutectogels Regulated by the Spatiotemporal Expression of Non‐Covalent Interactions

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