Abstract
We compared the surface envelope glycoprotein distribution and the budding polarity of four RNA viruses in Fischer rat thyroid (FRT) cells and in CaCo-2 cells derived from a human colon carcinoma. Whereas both FRT and CaCo-2 cells sort similarly influenza hemagglutinin and vesicular stomatitis virus (VSV) G protein, respectively, to apical and basolateral membrane domains, they differ in their handling of two togaviruses, Sindbis and Semliki Forest virus (SFV). By conventional EM Sindbis virus and SFV were shown to bud apically in FRT cells and basolaterally in CaCo-2 cells. Consistent with this finding, the distribution of the p62/E2 envelope glycoprotein of SFV, assayed by immunoelectronmicroscopy and by domain-selective surface biotinylation was predominantly apical on FRT cells and basolateral on CaCo-2 cells. We conclude that a given virus and its envelope glycoprotein can be delivered to opposite membrane domains in epithelial cells derived from different tissues. The tissue specificity in the polarity of virus budding and viral envelope glycoprotein distribution indicate that the sorting machinery varies considerably between different epithelial cell types.
| Original language | English |
|---|---|
| Pages (from-to) | 551-564 |
| Number of pages | 14 |
| Journal | Journal of Cell Biology |
| Volume | 117 |
| Issue number | 3 |
| Publication status | Published - May 1992 |
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- Cell Biology
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Opposite polarity of virus budding and of viral envelope glycoprotein distribution in epithelial cells derived from different tissues. / Zurzolo, Chiara; Polistina, Claudio; Saini, Marco; Gentile, Raffaele; Aloj, Luigi; Migliaccio, Giovanni; Bonatti, Stefano; Nitsch, Lucio.
In: Journal of Cell Biology, Vol. 117, No. 3, 05.1992, p. 551-564.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Opposite polarity of virus budding and of viral envelope glycoprotein distribution in epithelial cells derived from different tissues
AU - Zurzolo, Chiara
AU - Polistina, Claudio
AU - Saini, Marco
AU - Gentile, Raffaele
AU - Aloj, Luigi
AU - Migliaccio, Giovanni
AU - Bonatti, Stefano
AU - Nitsch, Lucio
PY - 1992/5
Y1 - 1992/5
N2 - We compared the surface envelope glycoprotein distribution and the budding polarity of four RNA viruses in Fischer rat thyroid (FRT) cells and in CaCo-2 cells derived from a human colon carcinoma. Whereas both FRT and CaCo-2 cells sort similarly influenza hemagglutinin and vesicular stomatitis virus (VSV) G protein, respectively, to apical and basolateral membrane domains, they differ in their handling of two togaviruses, Sindbis and Semliki Forest virus (SFV). By conventional EM Sindbis virus and SFV were shown to bud apically in FRT cells and basolaterally in CaCo-2 cells. Consistent with this finding, the distribution of the p62/E2 envelope glycoprotein of SFV, assayed by immunoelectronmicroscopy and by domain-selective surface biotinylation was predominantly apical on FRT cells and basolateral on CaCo-2 cells. We conclude that a given virus and its envelope glycoprotein can be delivered to opposite membrane domains in epithelial cells derived from different tissues. The tissue specificity in the polarity of virus budding and viral envelope glycoprotein distribution indicate that the sorting machinery varies considerably between different epithelial cell types.
AB - We compared the surface envelope glycoprotein distribution and the budding polarity of four RNA viruses in Fischer rat thyroid (FRT) cells and in CaCo-2 cells derived from a human colon carcinoma. Whereas both FRT and CaCo-2 cells sort similarly influenza hemagglutinin and vesicular stomatitis virus (VSV) G protein, respectively, to apical and basolateral membrane domains, they differ in their handling of two togaviruses, Sindbis and Semliki Forest virus (SFV). By conventional EM Sindbis virus and SFV were shown to bud apically in FRT cells and basolaterally in CaCo-2 cells. Consistent with this finding, the distribution of the p62/E2 envelope glycoprotein of SFV, assayed by immunoelectronmicroscopy and by domain-selective surface biotinylation was predominantly apical on FRT cells and basolateral on CaCo-2 cells. We conclude that a given virus and its envelope glycoprotein can be delivered to opposite membrane domains in epithelial cells derived from different tissues. The tissue specificity in the polarity of virus budding and viral envelope glycoprotein distribution indicate that the sorting machinery varies considerably between different epithelial cell types.
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UR - http://www.scopus.com/inward/citedby.url?scp=0026557513&partnerID=8YFLogxK
M3 - Article
C2 - 1572895
AN - SCOPUS:0026557513
VL - 117
SP - 551
EP - 564
JO - Journal of Cell Biology
JF - Journal of Cell Biology
SN - 0021-9525
IS - 3
ER -