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Spike protein VP4 assembly with maturing rotavirus requires a postendoplasmic reticulum event in polarized Caco-2 cells
- Source :
- Journal of Virology, Journal of Virology, 2004, 78 (20), pp.10987-10994. ⟨10.1128/JVI.78.20.10987-10994.2004⟩, Journal of Virology, American Society for Microbiology, 2004, 78 (20), pp.10987-10994. ⟨10.1128/JVI.78.20.10987-10994.2004⟩
- Publication Year :
- 2004
- Publisher :
- HAL CCSD, 2004.
-
Abstract
- Rotavirus assembly is a multistep process that requires the successive association of four major structural proteins in three concentric layers. It has been assumed until now that VP4, the most external viral protein that forms the spikes of mature virions, associates with double-layer particles within the endoplasmic reticulum (ER) in conjunction with VP7 and with the help of a nonstructural protein, NSP4. VP7 and NSP4 are two glycosylated proteins. However, we recently described a strong association of VP4 with raft-type membrane microdomains, a result that makes the ER a highly questionable site for the final assembly of rotavirus, since rafts are thought to be absent from this compartment. In this study, we used tunicamycin (TM), a drug known to block the first step of protein N glycosylation, as a tool to dissect rotavirus assembly. We show that, as expected, TM blocks viral protein glycosylation and also decreases virus infectivity. In the meantime, viral particles were blocked as enveloped particles in the ER. Interestingly, TM does not prevent the targeting of VP4 to the cell surface nor its association with raft membranes, whereas the infectivity associated with the raft fractions strongly decreased. VP4 does not colocalize with the ER marker protein disulfide-isomerase even when viral particles were blocked by TM in this compartment. These results strongly support a primary role for raft membranes in rotavirus final assembly and the fact that VP4 assembly with the rest of the particle is an extrareticular event.
- Subjects :
- Rotavirus
Glycosylation
SURFACE
Viral protein
viruses
Immunology
ENDOPLASMIC-RETICULUM
Biology
NONSTRUCTURAL GLYCOPROTEIN
medicine.disease_cause
Endoplasmic Reticulum
Microbiology
03 medical and health sciences
chemistry.chemical_compound
Membrane Microdomains
fluids and secretions
N-linked glycosylation
Virology
medicine
Humans
INFECTIVITY
030304 developmental biology
Infectivity
0303 health sciences
030306 microbiology
Endoplasmic reticulum
Virus Assembly
Virion
Cell Polarity
virus diseases
Raft
Tunicamycin
TRANSPORT
Cell biology
Virus-Cell Interactions
LIPID RAFTS
Biochemistry
chemistry
Insect Science
INFECTED-CELLS
PLASMA-MEMBRANE
[SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology
Capsid Proteins
Caco-2 Cells
TUNICAMYCIN
Subjects
Details
- Language :
- English
- ISSN :
- 0022538X and 10985514
- Database :
- OpenAIRE
- Journal :
- Journal of Virology, Journal of Virology, 2004, 78 (20), pp.10987-10994. ⟨10.1128/JVI.78.20.10987-10994.2004⟩, Journal of Virology, American Society for Microbiology, 2004, 78 (20), pp.10987-10994. ⟨10.1128/JVI.78.20.10987-10994.2004⟩
- Accession number :
- edsair.doi.dedup.....a708bca0076080415dd1b4afaf835688
- Full Text :
- https://doi.org/10.1128/JVI.78.20.10987-10994.2004⟩