1,721,194 research outputs found

    Structure of a cleavage-independent HIV Env recapitulates the glycoprotein architecture of the native cleaved trimer

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    Furin cleavage of the HIV envelope glycoprotein is an essential step for cell entry that enables formation of well-folded, native-like glycosylated trimers, releases constraints on the fusion peptide, and limits enzymatic processing of the N-glycan shield. Here, we show that a cleavage-independent, stabilized, soluble Env trimer mimic (BG505 NFL.664) exhibits a "closed-form", native-like, prefusion conformation akin to furin-cleaved Env trimers. The crystal structure of BG505 NFL.664 at 3.39 Å resolution with two potent bNAbs also identifies the full epitopes of PGV19 and PGT122 that target the receptor binding site and N332 supersite, respectively. Quantitative site-specific analysis of the glycan shield reveals that native-like glycan processing is maintained despite furin-independent maturation in the secretory pathway. Thus, cleavage-independent NFL Env trimers exhibit quaternary protein and carbohydrate structures similar to the native viral spike that further validate their potential as vaccine immunogen candidates

    MassIVE MSV000086998 -site-specific glycosylation analysis of the ChAdOx1 nCoV-19 derived Spike protein

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    Site-specific glycosylation analysis of the ChAdOx1 nCoV-19 derived Spike protein. Raw files for both the cleaved (S1/S2) and uncleaved (S0) protein are included. [doi:10.25345/C55N6W] [dataset license: CC0 1.0 Universal (CC0 1.0)] </span

    MassIVE MSV000084993: Site specific glycosylation analysis of coronavirus spike proteins

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    Site specific N-linked glycosylation analysis of coronavirus spike proteins</span

    MassIVE MSV000085202 - SARS-CoV-2 Spike site-specific N-linked glycan analysis

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    Glycopeptide analysis of trypsin, chymotrypsin and alpha-lytic protease digests from SARS-CoV-2 Spike expressed in HEK 293F cells. https://www.biorxiv.org/content/10.1101/2020.03.26.010322v1 [doi:10.25345/C54X4K] [dataset license: CC0 1.0 Universal (CC0 1.0)] </span

    MassIVE MSV000091004 - Variations within the glycan shield of SARS-CoV-2 impact viral spike dynamics,Raw mass spectrometry files associated with the LC-MS analysis detailed in: Variations within the glycan shield of SARS-CoV-2 impact viral spike dynamics. This work was performed to determine the site-specific N-linked glycosylation on a number of recombinant SARS-CoV-2 variant spike glycoproteins.

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    Raw mass spectrometry files associated with the LC-MS analysis detailed in: Variations within the glycan shield of SARS-CoV-2 impact viral spike dynamics. This work was performed to determine the site-specific N-linked glycosylation on a number of recombinant SARS-CoV-2 variant spike glycoproteins</span

    MassIVE MSV000085152: N-linked glycans from recombinant SARS, MERS and HKU1 S proteins

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    PNGase F released N-linked glycans from recombinant SARS MERS and HKU1 coronavirus S protein trimers</span

    MassIVE MSV000087279 - SARS-CoV-2 Spike site-specific N-linked glycan analysis 3 Biological Replicates

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    Glycopeptide analysis of trypsin, chymotrypsin and alpha-lytic protease digests from SARS-CoV-2 Spike expressed in HEK 293F cells. Contains three biological replicates expressed separately https://science.sciencemag.org/content/369/6501/330 [doi:10.25345/C5822F] [dataset license: CC0 1.0 Universal (CC0 1.0)] </span

    Contrasting IgG structures reveal extreme asymmetry and flexibility

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    The crystal structure of IgG1 b12 represents the first visualization of an intact human IgG with a full-length hinge that has all domains ordered and visible. In comparison to intact murine antibodies and hinge-deletant human antibodies, b12 reveals extreme asymmetry, indicative of the extraordinary interdomain flexibility within an antibody. In addition, the structure provides an illustration of the human IgG1 hinge in its entirety and of asymmetry in the composition of the carbohydrate attached to each C(H)2 domain of the Fc. The two separate hinges assume different conformations in order to accommodate the vastly different placements of the two Fab domains relative to the Fc domain. Interestingly, only one of two possible intra-hinge disulfides is formed
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