Differential glycosylation of envelope gp120 is associated with differential recognition of HIV-1 by virus-specific antibodies and cell infection

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11110%2F14%3A10285841" target="_blank" >RIV/00216208:11110/14:10285841 - isvavai.cz</a>
Alternative codes found
RIV/61989592:15110/14:33149997
Result on the web
<a href="http://dx.doi.org/10.1186/1742-6405-11-23" target="_blank" >http://dx.doi.org/10.1186/1742-6405-11-23</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1186/1742-6405-11-23" target="_blank" >10.1186/1742-6405-11-23</a>

Result language
angličtina
Original language name
Differential glycosylation of envelope gp120 is associated with differential recognition of HIV-1 by virus-specific antibodies and cell infection
Original language description
Conclusion: Our data support the hypothesis that the glycosylation machinery of different cells shapes gp120 glycosylation and, consequently, impacts envelope recognition by specific antibodies as well as the interaction of HIV-1 gp120 with cellular receptors. These findings underscore the importance of selection of appropriately glycosylated HIV-1 envelope as a vaccine antigen.
Czech name
—
Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
EC - Immunology
OECD FORD branch
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Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
V - Vyzkumna aktivita podporovana z jinych verejnych zdroju

Publication year
2014
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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