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

Behrens et al., 2017 - Google Patents

Structural principles controlling HIV envelope glycosylation

Behrens et al., 2017

View HTML
Document ID
17033545115454501997
Author
Behrens A
Crispin M
Publication year
Publication venue
Current opinion in structural biology

External Links

Snippet

Highlights•The HIV-1 glycan shield is a conserved target for broadly neutralizing antibodies.•Mass spectrometry analyses have revealed fine structural details of HIV-1 envelope glycosylation.•Dense glycan packing, trimerization and potentially membrane …
Continue reading at www.ncbi.nlm.nih.gov (HTML) (other versions)

Classifications

    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N2740/00Reverse Transcribing RNA Viruses
    • C12N2740/00011Reverse Transcribing RNA Viruses
    • C12N2740/10011Retroviridae
    • C12N2740/16011Human Immunodeficiency Virus, HIV
    • C12N2740/16111Human Immunodeficiency Virus, HIV concerning HIV env
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K16/00Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
    • C07K16/08Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses
    • C07K16/10Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses from RNA viruses, e.g. hepatitis E virus
    • C07K16/1036Retroviridae, e.g. leukemia viruses
    • C07K16/1045Lentiviridae, e.g. HIV, FIV, SIV

Similar Documents

Publication Publication Date Title
Behrens et al. Structural principles controlling HIV envelope glycosylation
Doores The HIV glycan shield as a target for broadly neutralizing antibodies
Struwe et al. Site-specific glycosylation of virion-derived HIV-1 Env is mimicked by a soluble trimeric immunogen
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
Crispin et al. Structure and immune recognition of the HIV glycan shield
Behrens et al. Composition and antigenic effects of individual glycan sites of a trimeric HIV-1 envelope glycoprotein
Bonomelli et al. The glycan shield of HIV is predominantly oligomannose independently of production system or viral clade
Cao et al. Global site-specific N-glycosylation analysis of HIV envelope glycoprotein
Seabright et al. Protein and glycan mimicry in HIV vaccine design
Go et al. Glycosylation site-specific analysis of clade C HIV-1 envelope proteins
Zhu et al. Mass spectrometric characterization of the glycosylation pattern of HIV-gp120 expressed in CHO cells
Doores et al. Variable loop glycan dependency of the broad and potent HIV-1-neutralizing antibodies PG9 and PG16
Go et al. Glycosylation benchmark profile for HIV-1 envelope glycoprotein production based on eleven Env trimers
Behrens et al. Molecular architecture of the cleavage-dependent mannose patch on a soluble HIV-1 envelope glycoprotein trimer
Go et al. Comparative analysis of the glycosylation profiles of membrane-anchored HIV-1 envelope glycoprotein trimers and soluble gp140
Stewart-Jones et al. Trimeric HIV-1-Env structures define glycan shields from clades A, B, and G
Ringe et al. Closing and opening holes in the glycan shield of HIV-1 envelope glycoprotein SOSIP trimers can redirect the neutralizing antibody response to the newly unmasked epitopes
Binley et al. Role of complex carbohydrates in human immunodeficiency virus type 1 infection and resistance to antibody neutralization
Pritchard et al. Cell-and protein-directed glycosylation of native cleaved HIV-1 envelope
Crispin et al. Targeting host-derived glycans on enveloped viruses for antibody-based vaccine design
Pritchard et al. Glycan clustering stabilizes the mannose patch of HIV-1 and preserves vulnerability to broadly neutralizing antibodies
Raska et al. Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition
Scanlan et al. Inhibition of mammalian glycan biosynthesis produces non-self antigens for a broadly neutralising, HIV-1 specific antibody
Yang et al. Glycoform analysis of recombinant and human immunodeficiency virus envelope protein gp120 via higher energy collisional dissociation and spectral-aligning strategy
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