HPV caught in the tetraspanin web?
Autor: | Jérôme Finke, Lisa Hitschler, Klaus Boller, Thorsten Lang, Luise Florin |
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Rok vydání: | 2020 |
Předmět: |
0301 basic medicine
Microbiology (medical) Microdomains Immunology Endocytic cycle Protein nanoclustering CD63 Papillomavirus Virusinfektion Pathogen endocytosis Actin CD151 OBSL1 Tetraspanin 24 Filamentous actin Cell membrane 03 medical and health sciences 0302 clinical medicine Tetraspanin Viral entry medicine HaCaT Cells Humans Immunology and Allergy Cytoskeleton Original Investigation Human papillomavirus 16 Microscopy Confocal Tetraspanin 30 Chemistry Papillomavirus Infections Plakins Virion Signal transducing adaptor protein Hep G2 Cells General Medicine Virus Internalization Actins Endocytosis Cell biology Cytoskeletal Proteins Microscopy Electron 030104 developmental biology medicine.anatomical_structure 030220 oncology & carcinogenesis embryonic structures HeLa Cells |
Zdroj: | Medical microbiology and immunology, 209(4):447-459 Medical Microbiology and Immunology |
ISSN: | 1432-1831 0300-8584 |
Popis: | Tetraspanins are master organizers of the cell membrane. Recent evidence suggests that tetraspanins themselves may become crowded by virus particles and that these crowds/aggregates co-internalize with the viral particles. Using microscopy, we studied human papillomavirus (HPV) type 16-dependent aggregates on the cell surface of tetraspanin overexpressing keratinocytes. We find that aggregates are (1) rich in at least two different tetraspanins, (2) three-dimensional architectures extending up to several micrometers into the cell, and (3) decorated intracellularly by filamentous actin. Moreover, in cells not overexpressing tetraspanins, we note that obscurin-like protein 1 (OBSL1), which is thought to be a cytoskeletal adaptor, associates with filamentous actin. We speculate that HPV contact with the cell membrane could trigger the formation of a large tetraspanin web. This web may couple the virus contact site to the intracellular endocytic actin machinery, possibly involving the cytoskeletal adaptor protein OBSL1. Functionally, such a tetraspanin web could serve as a virus entry platform, which is co-internalized with the virus particle. Electronic supplementary material The online version of this article (10.1007/s00430-020-00683-1) contains supplementary material, which is available to authorized users. |
Databáze: | OpenAIRE |
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