Mouse polyomavirus enters early endosomes, requires their acidic pH for productive infection, and meets transferrin cargo in Rab11-positive endosomes
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
16611921
PubMed Central
PMC1472029
DOI
10.1128/jvi.80.9.4610-4622.2006
PII: 80/9/4610
Knihovny.cz E-zdroje
- MeSH
- buněčné linie MeSH
- časové faktory MeSH
- elektronová mikroskopie MeSH
- endozomy metabolismus virologie MeSH
- fúze membrán MeSH
- kaveolin 1 genetika metabolismus MeSH
- koncentrace vodíkových iontů MeSH
- myši MeSH
- Polyomavirus fyziologie MeSH
- Rab proteiny vázající GTP metabolismus MeSH
- Rab11 proteiny vázající GTP MeSH
- rezonanční přenos fluorescenční energie MeSH
- transferin metabolismus MeSH
- transport proteinů MeSH
- vazba proteinů MeSH
- virion metabolismus MeSH
- zvířata MeSH
- Check Tag
- myši MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- kaveolin 1 MeSH
- Rab proteiny vázající GTP MeSH
- Rab11 proteiny vázající GTP MeSH
- transferin MeSH
Mouse polyomavirus (PyV) virions enter cells by internalization into smooth monopinocytic vesicles, which fuse under the cell membrane with larger endosomes. Caveolin-1 was detected on monopinocytic vesicles carrying PyV particles in mouse fibroblasts and epithelial cells (33). Here, we show that PyV can be efficiently internalized by Jurkat cells, which do not express caveolin-1 and lack caveolae, and that overexpression of a caveolin-1 dominant-negative mutant in mouse epithelial cells does not prevent their productive infection. Strong colocalization of VP1 with early endosome antigen 1 (EEA1) and of EEA1 with caveolin-1 in mouse fibroblasts and epithelial cells suggests that the monopinocytic vesicles carrying the virus (and vesicles containing caveolin-1) fuse with EEA1-positive early endosomes. In contrast to SV40, PyV infection is dependent on the acidic pH of endosomes. Bafilomycin A1 abolished PyV infection, and an increase in endosomal pH by NH4Cl markedly reduced its efficiency when drugs were applied during virion transport towards the cell nucleus. The block of acidification resulted in the retention of a fraction of virions in early endosomes. To monitor further trafficking of PyV, we used fluorescent resonance energy transfer (FRET) to determine mutual localization of PyV VP1 with transferrin and Rab11 GTPase at a 2- to 10-nm resolution. Positive FRET between PyV VP1 and transferrin cargo and between PyV VP1 and Rab11 suggests that during later times postinfection (1.5 to 3 h), the virus meets up with transferrin in the Rab11-positive recycling endosome. These results point to a convergence of the virus and the cargo internalized by different pathways in common transitional compartments.
Zobrazit více v PubMed
None PubMed
None
None PubMed
None PubMed
None PubMed
None PubMed
None PubMed
None PubMed
None PubMed
None PubMed
None PubMed
None PubMed
None PubMed
None PubMed
None PubMed
None PubMed
None PubMed
None PubMed
Mouse polyomavirus infection induces lamin reorganisation
The Interplay between Viruses and Host DNA Sensors
Immune sensing of mouse polyomavirus DNA by p204 and cGAS DNA sensors
