Structurally and genetically, human herpesviruses are among the largest and most complex of viruses. Using cryo-electron microscopy (cryo-EM) with an optimized image reconstruction strategy, we report the herpes simplex virus type 2 (HSV-2) capsid structure at 3.1 angstroms, which is built up of about 3000 proteins organized into three types of hexons (central, peripentonal, and edge), pentons, and triplexes. Both hexons and pentons contain the major capsid protein, VP5; hexons also contain a small capsid protein, VP26; and triplexes comprise VP23 and VP19C. Acting as core organizers, VP5 proteins form extensive intermolecular networks, involving multiple disulfide bonds (about 1500 in total) and noncovalent interactions, with VP26 proteins and triplexes that underpin capsid stability and assembly. Conformational adaptations of these proteins induced by their microenvironments lead to 46 different conformers that assemble into a massive quasisymmetric shell, exemplifying the structural and functional complexity of HSV.

This review reports an overview and development of micro-gyroscope. The review first presents different types of micro-gyroscopes. Micro-gyroscopes in this review are categorized into Coriolis gyroscope, levitated rotor gyroscope, Sagnac gyroscope, nuclear magnetic resonance (NMR) gyroscope according to the working principle. Different principles, structures, materials, fabrications and control technologies of micro-gyroscopes are analyzed. This review compares different classes of gyroscopes in the aspects such as fabrication method, detection axis, materials, size and so on. Finally, the review evaluates the key technologies on how to improve the precision and anti-jamming ability and to extend the available applications of the gyroscopes in the market and patents as well.

The bisolute sorption and thermodynamic behavior of organic pollutants on low temperature biochars (LTB) at 300 °C and high temperature biochars (HTB) at 700 °C were determined to elucidate sorptive properties of biochar changed with pyrolytic temperatures. The structural characteristics and isotherms shape of the biochar were more dependent on the pyrolytic temperature than on the biomass feedstocks, which included orange peel, pine needle, and sugar cane bagasse. For LTB, the thermally altered organic matter colocalized with the carbonized matter, and the visible fine pores of the fixed carbons were plugged by the remaining volatile carbon. For HTB, most of the volatile matter was gone and the fixed matter was composed of fully carbonized adsorptive sites. Monolayer adsorption of 1-naphthol to HTB was dominant but was suppressed by phenol. In comparison, LTB displayed exceptional sorption behavior where partition and adsorption were concurrently promoted by a cosolute and elevated temperature. In addition to monolayer surface coverage, pore-filling mechanisms may contribute to the increase of adsorption fraction. Moreover, the entropy gain was a dominant force driving the partition and adsorption processes in LTB. Thus, the colocalizing partition phase and adsorptive sites in LTB are proposed to be in interencased states rather than in physical separation.

Most double-stranded RNA (dsRNA) viruses transcribe RNA plus strands within a common innermost capsid shell. This process requires coordinated efforts by RNA-dependent RNA polymerase (RdRp) together with other capsid proteins and genomic RNA. Here we report the near-atomic resolution structure of the RdRp protein VP2 in complex with its cofactor protein VP4 and genomic RNA within an aquareovirus capsid using 200-kV cryoelectron microscopy and symmetry-mismatch reconstruction. The structure of these capsid proteins enabled us to observe the elaborate nonicosahedral structure within the double-layered icosahedral capsid. Our structure shows that the RdRp complex is anchored at the inner surface of the capsid shell and interacts with genomic dsRNA and four of the five asymmetrically arranged N termini of the capsid shell proteins under the fivefold axis, implying roles for these N termini in virus assembly. The binding site of the RNA end at VP2 is different from the RNA cap binding site identified in the crystal structure of orthoreovirus RdRp λ3, although the structures of VP2 and λ3 are almost identical. A loop, which was thought to separate the RNA template and transcript, interacts with an apical domain of the capsid shell protein, suggesting a mechanism for regulating RdRp replication and transcription. A conserved nucleoside triphosphate binding site was localized in our RdRp cofactor protein VP4 structure, and interactions between the VP4 and the genomic RNA were identified.

Herpes simplex viruses (HSVs) cause human oral and genital ulcer diseases. Patients with HSV-2 have a higher risk of acquiring a human immunodeficiency virus infection. HSV-2 is a member of the α-herpesvirinae subfamily that together with the β- and γ-herpesvirinae subfamilies forms the Herpesviridae family. Here, we report the cryo-electron microscopy structure of the HSV-2 C-capsid with capsid-vertex-specific component (CVSC) that was determined at 3.75 Å using a block-based reconstruction strategy. We present atomic models of multiple conformers for the capsid proteins (VP5, VP23, VP19C, and VP26) and CVSC. Comparison of the HSV-2 homologs yields information about structural similarities and differences between the three herpesviruses sub-families and we identify α-herpesvirus-specific structural features. The hetero-pentameric CVSC, consisting of a UL17 monomer, a UL25 dimer and a UL36 dimer, is bound tightly by a five-helix bundle that forms extensive networks of subunit contacts with surrounding capsid proteins, which reinforce capsid stability.

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