PMC:7253482 / 3292-4197 JSONTXT

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{"project":"LitCovid-sample-sentences","denotations":[{"id":"T21","span":{"begin":0,"end":383},"obj":"Sentence"},{"id":"T22","span":{"begin":384,"end":582},"obj":"Sentence"},{"id":"T23","span":{"begin":583,"end":905},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Previous analyses of viral glycan shields have revealed the presence of underprocessed oligomannose-type glycans that seemingly arise due to steric constraints that prevent access of glycan processing enzymes to substrate glycans24,27,28, especially when the viral glycoprotein has evolved to mask immunogenic epitopes with a particularly dense array of host-derived glycans26,29–34. Restricted access to these glycan sites or interference with surrounding protein surface or neighbouring glycan residues can render glycan processing enzymes ineffective in specific regions27,28,35. Glycan processing on soluble glycoproteins has also been shown to be a strong reporter of native-like protein architecture and thus immunogen integrity36–38; and glycan processing on a successful immunogen candidate should therefore mimic, as closely as possible, the structural features observed on the native virus39,40."}

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analyses of viral glycan shields have revealed the presence of underprocessed oligomannose-type glycans that seemingly arise due to steric constraints that prevent access of glycan processing enzymes to substrate glycans24,27,28, especially when the viral glycoprotein has evolved to mask immunogenic epitopes with a particularly dense array of host-derived glycans26,29–34. Restricted access to these glycan sites or interference with surrounding protein surface or neighbouring glycan residues can render glycan processing enzymes ineffective in specific regions27,28,35. Glycan processing on soluble glycoproteins has also been shown to be a strong reporter of native-like protein architecture and thus immunogen integrity36–38; and glycan processing on a successful immunogen candidate should therefore mimic, as closely as possible, the structural features observed on the native virus39,40."}

{"project":"LitCovid-sentences","denotations":[{"id":"T21","span":{"begin":0,"end":383},"obj":"Sentence"},{"id":"T22","span":{"begin":384,"end":582},"obj":"Sentence"},{"id":"T23","span":{"begin":583,"end":905},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Previous analyses of viral glycan shields have revealed the presence of underprocessed oligomannose-type glycans that seemingly arise due to steric constraints that prevent access of glycan processing enzymes to substrate glycans24,27,28, especially when the viral glycoprotein has evolved to mask immunogenic epitopes with a particularly dense array of host-derived glycans26,29–34. Restricted access to these glycan sites or interference with surrounding protein surface or neighbouring glycan residues can render glycan processing enzymes ineffective in specific regions27,28,35. Glycan processing on soluble glycoproteins has also been shown to be a strong reporter of native-like protein architecture and thus immunogen integrity36–38; and glycan processing on a successful immunogen candidate should therefore mimic, as closely as possible, the structural features observed on the native virus39,40."}