Viruses frequently exploit the host's nucleocytoplasmic trafficking machinery to facilitate their replication and evade immune defenses. By encoding specialized proteins and other components, they strategically target host nuclear transport receptors (NTRs) and nucleoporins within the spiderweb-like inner channel of the nuclear pore complex (NPC), enabling efficient access to the host nucleus. This review explores the intricate mechanisms governing the nuclear import and export of viral components, with a focus on the interplay between viral factors and host determinants that are essential for these processes. Given the pivotal role of nucleocytoplasmic shuttling in the viral life cycle, we also examine therapeutic strategies aimed at disrupting the host's nuclear transport pathways. This includes evaluating the efficacy of pharmacological inhibitors in impairing viral replication and assessing their potential as antiviral treatments. Furthermore, we emphasize the need for continued research to develop targeted therapies that leverage vulnerabilities in nucleocytoplasmic trafficking. Emerging high-resolution techniques, such as advanced imaging and computational modeling, are transforming our understanding of the dynamic interactions between viruses and the NPC. These cutting-edge tools are driving progress in identifying novel therapeutic opportunities and uncovering deeper insights into viral pathogenesis. This review highlights the importance of these advancements in paving the way for innovative antiviral strategies.
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http://dx.doi.org/10.3390/v17020151 | DOI Listing |
Langmuir
March 2025
Hubei Nuclear Solid Physics Key Laboratory, Department of Physics, Wuhan University, Wuhan 430072, China.
In this work, a series of Ni/Co-MOFs with high specific capacitances were synthesized as anode materials using a one-step hydrothermal reaction method. NaOH in different amounts (3, 4, 5, and 6 mmol) was added during the synthesis to tune the pore structure of Ni/Co-MOFs. It was found that the Ni/Co-MOF-3 with a NaOH amount of 5 mmol exhibits the largest specific surface area and pore volume, which provides more active sites for the electrochemical reaction and facilitates ion diffusion at the interface of the electrolyte solution/active material, thus increasing the capacitance of the electrode material.
View Article and Find Full Text PDFParasit Vectors
March 2025
Plant Genetics Research Unit, United States Department of Agriculture (USDA)-Agricultural Research Service, Columbia, MO, USA.
Background: Heterorhabditis are important biological control agents in agriculture. Two Heterorhabditis populations, S8 and S10, were isolated from agricultural soils in the United States of America. Molecular analyses, based on mitochondrial and nuclear genes, showed that these populations are conspecific and represent a novel species of the "Bacteriophora" clade.
View Article and Find Full Text PDFMol Cell
March 2025
Department of Molecular Biosciences, Northwestern University, Evanston, IL 60201, USA. Electronic address:
Nuclear pore proteins (nucleoporins [Nups]) physically interact with hundreds of chromosomal sites, impacting transcription. In yeast, transcription factors mediate interactions between Nups and enhancers and promoters. To define the molecular basis of this mechanism, we exploited a separation-of-function mutation in the Gcn4 transcription factor that blocks its interaction with the nuclear pore complex (NPC).
View Article and Find Full Text PDFDevelopment
March 2025
HHMI and Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
Condensates that accumulate small RNA biogenesis factors (nuage) are common in germ cells and often associate with nuclei. In the C. elegans germline, P granules overlay large clusters of nuclear pores and this organization has been proposed to facilitate surveillance of nascent transcripts by Argonaute proteins enriched in P granules.
View Article and Find Full Text PDFFolia Parasitol (Praha)
February 2025
Laboratorio de Helmintologia, Departamento de Zoologia, Instituto de Biologia, Universidad Nacional Autonoma de Mexico, Mexico City, Mexico *Address for correspondence: Alejandro Oceguera-Figueroa, Laboratorio de Helmintologia, Departamento de Zoologia, Instituto de Biologia, Universidad Nacional Autonoma de Mexico, Ciudad de Mexico, Mexico. Avenida Universidad 3000, Ciudad Universitaria, Coyoacan, C.P. 04510. Mexico City, Mexico. E-mail.
A new species of Acanthocephala is described based on specimens found parasitising the intestine of the gafftopsail pompano Trachinotus rhodopus Gill in the State of Oaxaca, off the Pacific coast of Mexico. Rhadinorhynchus villalobosi sp. n.
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