期刊
MEDICAL MICROBIOLOGY AND IMMUNOLOGY
卷 209, 期 4, 页码 447-459出版社
SPRINGER
DOI: 10.1007/s00430-020-00683-1
关键词
CD151; CD63; Actin; OBSL1; Papillomavirus; Pathogen endocytosis; Microdomains; Protein nanoclustering
资金
- Projekt DEAL
- German Research Foundation (Deutsche Forschungsgemeinschaft, DFG) [FL 696/3-1, LA 1272/8-1]
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.
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