[go: up one dir, main page]
More Web Proxy on the site http://driver.im/

Zhou et al., 2017 - Google Patents

Quantification of the impact of the HIV-1-glycan shield on antibody elicitation

Zhou et al., 2017

View HTML @Full View
Document ID
16482980427476203090
Author
Zhou T
Doria-Rose N
Cheng C
Stewart-Jones G
Chuang G
Chambers M
Druz A
Geng H
McKee K
Do Kwon Y
O’Dell S
Sastry M
Schmidt S
Xu K
Chen L
Chen R
Louder M
Pancera M
Wanninger T
Zhang B
Zheng A
Farney S
Foulds K
Georgiev I
Joyce M
Lemmin T
Narpala S
Rawi R
Soto C
Todd J
Shen C
Tsybovsky Y
Yang Y
Zhao P
Haynes B
Stamatatos L
Tiemeyer M
Wells L
Scorpio D
Shapiro L
McDermott A
Mascola J
Kwong P
Publication year
Publication venue
Cell reports

External Links

Snippet

While the HIV-1-glycan shield is known to shelter Env from the humoral immune response, its quantitative impact on antibody elicitation has been unclear. Here, we use targeted deglycosylation to measure the impact of the glycan shield on elicitation of antibodies …
Continue reading at www.cell.com (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
    • C12N2740/16122New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes
    • 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
    • C07K16/1063Lentiviridae, e.g. HIV, FIV, SIV env, e.g. gp41, gp110/120, gp160, V3, PND, CD4 binding site
    • 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
    • C12N2740/16134Use of virus or viral component as vaccine, e.g. live-attenuated or inactivated virus, VLP, viral protein
    • 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
    • C12N2740/15011Lentivirus, not HIV, e.g. FIV, SIV
    • AHUMAN NECESSITIES
    • A61MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61KPREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K39/00Medicinal preparations containing antigens or antibodies
    • A61K39/12Viral antigens
    • A61K39/21Retroviridae, e.g. equine infectious anemia virus

Similar Documents

Publication Publication Date Title
Zhou et al. Quantification of the impact of the HIV-1-glycan shield on antibody elicitation
Sok et al. Recent progress in broadly neutralizing antibodies to HIV
McCoy et al. Holes in the glycan shield of the native HIV envelope are a target of trimer-elicited neutralizing antibodies
Ma et al. Envelope deglycosylation enhances antigenicity of HIV-1 gp41 epitopes for both broad neutralizing antibodies and their unmutated ancestor antibodies
Crooks et al. Vaccine-elicited tier 2 HIV-1 neutralizing antibodies bind to quaternary epitopes involving glycan-deficient patches proximal to the CD4 binding site
Kwong et al. HIV-1 vaccines based on antibody identification, B cell ontogeny, and epitope structure
Stamatatos et al. Germline‐targeting immunogens
Falkowska et al. Broadly neutralizing HIV antibodies define a glycan-dependent epitope on the prefusion conformation of gp41 on cleaved envelope trimers
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
Huang et al. Identification of a CD4-binding-site antibody to HIV that evolved near-pan neutralization breadth
Rudicell et al. Enhanced potency of a broadly neutralizing HIV-1 antibody in vitro improves protection against lentiviral infection in vivo
Aldon et al. Rational design of DNA-expressed stabilized native-like HIV-1 envelope trimers
Seabright et al. Networks of HIV-1 envelope glycans maintain antibody epitopes in the face of glycan additions and deletions
Saunders et al. Vaccine elicitation of high mannose-dependent neutralizing antibodies against the V3-glycan broadly neutralizing epitope in nonhuman primates
Zolla-Pazner et al. Structure–function relationships of HIV-1 envelope sequence-variable regions refocus vaccine design
Joyce et al. Soluble prefusion closed DS-SOSIP. 664-Env trimers of diverse HIV-1 strains
Selvarajah et al. Comparing antigenicity and immunogenicity of engineered gp120
Bradley et al. Structural constraints of vaccine-induced tier-2 autologous HIV neutralizing antibodies targeting the receptor-binding site
Rawi et al. Automated design by structure-based stabilization and consensus repair to achieve prefusion-closed envelope trimers in a wide variety of HIV strains
Haim et al. Modeling virus-and antibody-specific factors to predict human immunodeficiency virus neutralization efficiency
Bricault et al. A multivalent clade C HIV-1 Env trimer cocktail elicits a higher magnitude of neutralizing antibodies than any individual component
Crooks et al. Effects of partially dismantling the CD4 binding site glycan fence of HIV-1 Envelope glycoprotein trimers on neutralizing antibody induction
WO2011109511A2 (en) Novel hiv-1 envelope glycoprotein
Wieczorek et al. Comparable antigenicity and immunogenicity of oligomeric forms of a novel, acute HIV-1 subtype C gp145 envelope for use in preclinical and clinical vaccine research