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?:abstract
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Dense surface glycosylation on the HIV-1 envelope (Env) protein acts as a shield from the adaptive immune system. However, the molecular complexity and flexibility of glycans make experimental studies a challenge. Here we have integrated high-throughput atomistic modeling of fully glycosylated HIV-1 Env with graph theory to capture immunologically important features of the shield topology. This is the first complete all-atom model of HIV-1 Env SOSIP glycan shield that includes both oligomannose and complex glycans, providing physiologically relevant insights of the glycan shield. This integrated approach including quantitative comparison with cryo-electron microscopy data provides hitherto unexplored details of the native shield architecture and its difference from the high-mannose glycoform. We have also derived a measure to quantify the shielding effect over the antigenic protein surface that defines regions of relative vulnerability and resilience of the shield and can be harnessed for rational immunogen design.
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?:doi
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10.1016/j.isci.2020.101836
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document_parses/pdf_json/f679717f5c550e84a9ec3789a58d488935b68f43.json; document_parses/pdf_json/2c9fc3331920dbcdfd788e402027df64e93680c2.json
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document_parses/pmc_json/PMC7724196.xml.json
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?:title
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Quantification of the Resilience and Vulnerability of HIV-1 Native Glycan Shield at Atomistic Detail
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