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PDBsum entry 6ozc
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Viral protein
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PDB id
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6ozc
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Contents |
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435 a.a.
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120 a.a.
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(+ 0 more)
105 a.a.
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(+ 0 more)
122 a.a.
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References listed in PDB file
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Key reference
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Title
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Networks of HIV-1 envelope glycans maintain antibody epitopes in the face of glycan additions and deletions.
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Authors
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G.E.Seabright,
C.A.Cottrell,
M.J.Van gils,
A.D'Addabbo,
D.J.Harvey,
A.J.Behrens,
J.D.Allen,
Y.Watanabe,
N.Scaringi,
T.M.Polveroni,
A.Maker,
S.Vasiljevic,
N.De val,
R.W.Sanders,
A.B.Ward,
M.Crispin.
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Ref.
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Structure, 2020,
28,
897.
[DOI no: ]
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PubMed id
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Abstract
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Numerous broadly neutralizing antibodies (bnAbs) have been identified that
target the glycans of the HIV-1 envelope spike. Neutralization breadth is
notable given that glycan processing can be substantially influenced by the
presence or absence of neighboring glycans. Here, using a stabilized recombinant
envelope trimer, we investigate the degree to which mutations in the glycan
network surrounding an epitope impact the fine glycan processing of antibody
targets. Using cryo-electron microscopy and site-specific glycan analysis, we
reveal the importance of glycans in the formation of the 2G12 bnAb epitope and
show that the epitope is only subtly impacted by variations in the glycan
network. In contrast, we show that the PG9 and PG16 glycan-based epitopes at the
trimer apex are dependent on the presence of the highly conserved surrounding
glycans. Glycan networks underpin the conservation of bnAb epitopes and are an
important parameter in immunogen design.
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