Nothing Special   »   [go: up one dir, main page]

Shivatare et al., 2018 - Google Patents

Unprecedented role of hybrid N-glycans as ligands for HIV-1 broadly neutralizing antibodies

Shivatare et al., 2018

Document ID
4157362029890391496
Author
Shivatare V
Shivatare S
Lee C
Liang C
Liao K
Cheng Y
Saidachary G
Wu C
Lin N
Kwong P
Burton D
Wu C
Wong C
Publication year
Publication venue
Journal of the American Chemical Society

External Links

Snippet

The development of an HIV vaccine has been hampered by the extraordinary mutability and genetic diversity of the virus, particularly the substantial sequence diversity of gp120 and gp 41 envelope glycoproteins existing in more than 2000 HIV variants. The highly diverse …
Continue reading at pubs.acs.org (other versions)

Classifications

    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K16/00Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies

Similar Documents

Publication Publication Date Title
Shivatare et al. Unprecedented role of hybrid N-glycans as ligands for HIV-1 broadly neutralizing antibodies
Crispin et al. Structure and immune recognition of the HIV glycan shield
Casalino et al. Beyond shielding: the roles of glycans in the SARS-CoV-2 spike protein
Seabright et al. Protein and glycan mimicry in HIV vaccine design
Go et al. Glycosylation site-specific analysis of hiv envelope proteins (jr-fl and con-s) reveals major differences in glycosylation site occupancy, glycoform profiles, and antigenic epitopesʼ accessibility
Pancera et al. Structural basis for diverse N-glycan recognition by HIV-1–neutralizing V1–V2–directed antibody PG16
Stewart-Jones et al. Trimeric HIV-1-Env structures define glycan shields from clades A, B, and G
Sterner et al. Perspectives on anti-glycan antibodies gleaned from development of a community resource database
Scanlan et al. Exploiting the defensive sugars of HIV-1 for drug and vaccine design
Zhu et al. Mass spectrometric characterization of the glycosylation pattern of HIV-gp120 expressed in CHO cells
Wang Synthetic carbohydrate antigens for HIV vaccine design
Dwek Glycobiology: toward understanding the function of sugars
Barb et al. NMR characterization of immunoglobulin G Fc glycan motion on enzymatic sialylation
Fernandez-Tejada et al. Designing synthetic vaccines for HIV
Go et al. Glycosylation and disulfide bond analysis of transiently and stably expressed clade C HIV-1 gp140 trimers in 293T cells identifies disulfide heterogeneity present in both proteins and differences in O-linked glycosylation
Thépaut et al. Structural studies of langerin and Birbeck granule: a macromolecular organization model
Pantophlet et al. Bacterially derived synthetic mimetics of mammalian oligomannose prime antibody responses that neutralize HIV infectivity
Yang et al. Glycoform analysis of recombinant and human immunodeficiency virus envelope protein gp120 via higher energy collisional dissociation and spectral-aligning strategy
Dunlop et al. Polysaccharide mimicry of the epitope of the broadly neutralizing anti-HIV antibody, 2G12, induces enhanced antibody responses to self oligomannose glycans
Orwenyo et al. Systematic synthesis and binding study of HIV V3 glycopeptides reveal the fine epitopes of several broadly neutralizing antibodies
Echeverria et al. Chemoenzymatic synthesis of N-glycan positional isomers and evidence for branch selective binding by monoclonal antibodies and human C-type lectin receptors
Toonstra et al. Top-down chemoenzymatic approach to synthesizing diverse high-mannose N-glycans and related neoglycoproteins for carbohydrate microarray analysis
Toonstra et al. Site-selective chemoenzymatic glycosylation of an HIV-1 polypeptide antigen with two distinct N-glycans via an orthogonal protecting group strategy
Struwe et al. Global N-glycan site occupancy of HIV-1 gp120 by metabolic engineering and high-resolution intact mass spectrometry
Nordén et al. Recombinant glycoprotein E of varicella zoster virus contains glycan-peptide motifs that modulate B cell epitopes into discrete immunological signatures