As intracellular parasites, viruses depend heavily on host cell structures and their functions to complete their life cycle and produce new viral particles. Viruses utilize or modulate cellular translational machinery to achieve efficient replication; the role of ribosome biogenesis and protein synthesis in viral replication particularly highlights the importance of the ribosome quantity and/or quality in controlling viral protein synthesis. Recently reported studies have demonstrated that ribosome biogenesis factors (RBFs) and ribosomal proteins (RPs) act as multifaceted regulators in selective translation of viral transcripts. Here we summarize the recent literature on RBFs and RPs and their association with subcellular redistribution, post-translational modification, enzyme catalysis, and direct interaction with viral proteins. The advances described in this literature establish a rationale for targeting ribosome production and function in the design of the next generation of antiviral agents.

The transmission of most respiratory pathogens, including SARS-CoV-2, occurs via virus-containing respiratory droplets, and thus, factors that affect virus viability in droplet residues on surfaces are of critical medical and public health importance. Relative humidity (RH) is known to play a role in virus survival, with a U-shaped relationship between RH and virus viability. The mechanisms affecting virus viability in droplet residues, however, are unclear. This study examines the structure and evaporation dynamics of virus-containing saliva droplets on fomites and their impact on virus viability using four model viruses: vesicular stomatitis virus, herpes simplex virus 1, Newcastle disease virus, and coronavirus HCoV-OC43. The results support the hypothesis that the direct contact of antiviral proteins and virions within the "coffee ring" region of the droplet residue gives rise to the observed U-shaped relationship between virus viability and RH. Viruses survive much better at low and high RH, and their viability is substantially reduced at intermediate RH. A phenomenological theory explaining this phenomenon and a quantitative model analyzing and correlating the experimentally measured virus survivability are developed on the basis of the observations. The mechanisms by which RH affects virus viability are explored. At intermediate RH, antiviral proteins have optimal influence on virions because of their largest contact time and overlap area, which leads to the lowest level of virus activity.

Toxoplasma gondii, a protozoan intracellular parasite, is present in a wide range of hosts, including virtually all species of warm-blooded vertebrates. Toxoplasmosis spreads to humans through a variety of pathways, including contaminated food or water, and close contact with various types of domestic animals. It poses a severe threat to human health, and contributes to important economic losses, not only in cost-of-illness but also in surveillance programs. It is thus necessary to develop a rapid point-of-care field diagnostic technology to control or prevent pathogen transmission to economically important livestock animals, domestic animals, and human beings. In this study, we develop a real-time isothermal amplification method capable of detecting the T. gondii genome in swine and feline blood samples. This method can detect toxoplasma genome with a lowest detection limit of 10(2) copies of per reaction under optimal reaction conditions of 36 degrees C for 25 min. The assay displayed advantages in sensitivity and specificity in comparison to traditional real-time PCR, and can be performed in a portable instrument.

基于解析细胞—病毒互作机理研究抗病毒制剂，是病毒学领域重要研究方向之一。本课题发现高三尖杉酯碱HHT—作为p-eIF4E抑制子，具有高效的抗感染活性，以及广谱的抗病毒效果，动物实验效果显著。我们还将HHT与氯喹等联合用药，效果更加明显。病毒感染过程中会激活ERK/p38-eIF4E细胞通路，提高p-eIF4E水平;p-eIF4E有利于病毒自身蛋白的产生，因此是抗病毒制剂的有效靶位。此外，我们还研究了p-4E抑制剂RAF265的作用机理及抑制效果，以及基于p-eIF4E进行TMT定量蛋白质组筛选，这些结果为进一步了解p-eIF4E在病毒复制中的意义提供进一步资料。本项目为开发仔猪病毒性腹泻药物提供依据。

Presentation of viral epitopes by swine MHC I (termed leukocyte antigen class I, SLA I) to cytotoxic T lymphocytes (CTLs) is crucial for swine immunity. The SLA-2 structure, however, remains largely unknown. To illustrate the structural basis of swine CTL epitope presentation, the crystal structure of SLA-2*04:02:02 complexed with one peptide, derived from foot-and-mouth disease virus (FMDV), was analyzed in this study. SLA2*04:02:02 and swine beta 2-microglobulin (s beta 2m) were refolded in vitro in the presence of peptides. X-ray diffraction data of SLA-2*04:02:02-peptide-432m (referred to as p/SLA-2*04:02:02) were collected. The diffraction dataset was 2.3 A in resolution and the space group was P3(2)21. Relevant data included a = 101.8 angstrom, b = 101.8 angstrom, c = 73.455 angstrom, alpha = 90.00 degrees, beta = 90.00 degrees, gamma = 120.00 degrees. The structure of p/SLA-2*04:02:02 was analyzed. The results revealed that Glu24, Met68, Gly76, and Gln173 in PBG of SLA-2*04:02:02 are different from other MHC I. Furthermore, Asn63 is different from other SLA I. Gln57, Met174 and Gln180 in PBG of SLA I are different from other species' MHC I. All of these features are different from known mammalian peptide-MHC class I complexes (referred to as p/MHC I). In addition, P4-His, P6-Val, and P8-Pro in the peptide were exposed, and these residues as epitopes can be presented by SLA-2*4:02:02. This study not only provides a structural basis for peptide presentation by SLA-2, but also screens one potential FMDV CTL epitope. The results may be of interest in future vaccine development.