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About:
Structural basis of transmembrane coupling of the HIV-1 envelope glycoprotein
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wasabi.inria.fr
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Type:
Academic Article
research paper
schema:ScholarlyArticle
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type
Academic Article
research paper
schema:ScholarlyArticle
isDefinedBy
Covid-on-the-Web dataset
has title
Structural basis of transmembrane coupling of the HIV-1 envelope glycoprotein
Creator
Chen, Bing
Chen, Wen
Seaman, Michael
Chou, James
Cai, Yongfei
Peng, Hanqin
Rits-Volloch, Sophia
Xiao, Tianshu
Fu, Qingshan
Ghantous, Fadi
Piai, Alessandro
Shaik, Munan
Source
PMC
abstract
The prefusion conformation of HIV-1 envelope protein (Env) is recognized by most broadly neutralizing antibodies (bnAbs). Studies showed that alterations of its membrane-related components, including the transmembrane domain (TMD) and cytoplasmic tail (CT), can reshape the antigenic structure of the Env ectodomain. Using nuclear magnetic resonance (NMR) spectroscopy, we determine the structure of an Env segment encompassing the TMD and a large portion of the CT in bicelles. The structure reveals that the CT folds into amphipathic helices that wrap around the C-terminal end of the TMD, thereby forming a support baseplate for the rest of Env. NMR dynamics measurements provide evidences of dynamic coupling across the TMD between the ectodomain and CT. Pseudovirus-based neutralization assays suggest that CT-TMD interaction preferentially affects antigenic structure near the apex of the Env trimer. These results explain why the CT can modulate the Env antigenic properties and may facilitate HIV-1 Env-based vaccine design.
has issue date
2020-05-08
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xsd:dateTime
)
bibo:doi
10.1038/s41467-020-16165-0
bibo:pmid
32385256
has license
cc-by
sha1sum (hex)
bfc67841f3047d0cafe158091d7c06be17602db9
schema:url
https://doi.org/10.1038/s41467-020-16165-0
resource representing a document's title
Structural basis of transmembrane coupling of the HIV-1 envelope glycoprotein
has PubMed Central identifier
PMC7210310
has PubMed identifier
32385256
schema:publication
Nat Commun
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covid:bfc67841f3047d0cafe158091d7c06be17602db9#body_text
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schema:about
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named entity 'cytoplasmic'
named entity 'Env'
named entity 'Env'
named entity 'nuclear magnetic resonance (NMR) spectroscopy'
named entity 'antigenic'
named entity 'HIV-1'
named entity 'ectodomain'
named entity 'antigenic'
named entity 'Env'
named entity 'glycoprotein'
named entity 'transmembrane'
named entity 'hydrophobicity/hydrophilicity'
named entity 'Urea'
named entity 'protein structure'
named entity 'gp41'
named entity 'trimerized'
named entity 'growth medium'
named entity 'aliphatic'
named entity 'San Jose'
named entity 'biophysical properties'
named entity 'neutralizing antibodies'
named entity 'membrane fusion'
named entity 'force constant'
named entity 'gel-filtration chromatography'
named entity 'cysteine'
named entity 'MTSL'
named entity 'trimer'
named entity 'serum samples'
named entity 'neutralizing antibodies'
named entity 'trimer'
named entity 'pH 8'
named entity 'vector'
named entity 'SDS-PAGE'
named entity 'lipid bilayer'
named entity 'atom'
named entity 'RP-HPLC'
named entity 'PCR'
named entity 'EDTA'
named entity 'Antibodies'
named entity 'hydrophobic core'
named entity 'HIV-1'
named entity 'XPLOR-NIH'
named entity 'Cys'
named entity 'NMR'
named entity 'PBS'
named entity 'PRE'
named entity 'substrates'
named entity 'MTSL'
named entity 'antibody'
named entity 'NMR'
named entity 'bicelles'
named entity 'hydrophobic'
named entity 'affinity chromatography'
named entity 'protein'
named entity 'dialysis'
named entity 'DEAE-dextran'
named entity 'Protein'
named entity 'gp41'
named entity 'protomer'
named entity 'antibodies'
named entity 'PRE'
named entity 'palmitoylation'
named entity 'Alkaline phosphatase'
named entity 'centrifuged'
named entity 'kDa'
named entity 'transfection'
named entity 'ectodomain'
named entity 'West Grove'
named entity 'E. coli'
named entity 'disulfide'
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