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

Liang et al., 2016 - Google Patents

Probing the impact of local structural dynamics of conformational epitopes on antibody recognition

Liang et al., 2016

View HTML
Document ID
10780914052011839528
Author
Liang Y
Guttman M
Davenport T
Hu S
Lee K
Publication year
Publication venue
Biochemistry

External Links

Snippet

Antibody–antigen interactions are governed by recognition of specific residues and structural complementarity between the antigen epitope and antibody paratope. While X-ray crystallography has provided detailed insights into static conformations of antibody–antigen …
Continue reading at www.ncbi.nlm.nih.gov (HTML) (other versions)

Classifications

    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/53Immunoassay; Biospecific binding assay
    • G01N33/569Immunoassay; Biospecific binding assay for micro-organisms, e.g. protozoa, bacteria, viruses
    • G01N33/56983Viruses
    • G01N33/56988AIDS or HTLV
    • 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

Similar Documents

Publication Publication Date Title
Saunders et al. Targeted selection of HIV-specific antibody mutations by engineering B cell maturation
Dubrovskaya et al. Vaccination with glycan-modified HIV NFL envelope trimer-liposomes elicits broadly neutralizing antibodies to multiple sites of vulnerability
Medina-Ramírez et al. Design and crystal structure of a native-like HIV-1 envelope trimer that engages multiple broadly neutralizing antibody precursors in vivo
Xu et al. Epitope-based vaccine design yields fusion peptide-directed antibodies that neutralize diverse strains of HIV-1
Liang et al. Probing the impact of local structural dynamics of conformational epitopes on antibody recognition
Kulp et al. Structure-based design of native-like HIV-1 envelope trimers to silence non-neutralizing epitopes and eliminate CD4 binding
He et al. HIV-1 vaccine design through minimizing envelope metastability
Gorman et al. Structures of HIV-1 Env V1V2 with broadly neutralizing antibodies reveal commonalities that enable vaccine design
Alam et al. Mimicry of an HIV broadly neutralizing antibody epitope with a synthetic glycopeptide
Dey et al. Structure-based stabilization of HIV-1 gp120 enhances humoral immune responses to the induced co-receptor binding site
Ma et al. Envelope deglycosylation enhances antigenicity of HIV-1 gp41 epitopes for both broad neutralizing antibodies and their unmutated ancestor antibodies
Cale et al. Virus-like particles identify an HIV V1V2 apex-binding neutralizing antibody that lacks a protruding loop
Wu et al. Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing
Antanasijevic et al. Polyclonal antibody responses to HIV Env immunogens resolved using cryoEM
Zwick et al. Molecular features of the broadly neutralizing immunoglobulin G1 b12 required for recognition of human immunodeficiency virus type 1 gp120
Voss et al. Elicitation of neutralizing antibodies targeting the V2 apex of the HIV envelope trimer in a wild-type animal model
Shrock et al. Germline-encoded amino acid–binding motifs drive immunodominant public antibody responses
Jiang et al. Rationally designed immunogens targeting HIV-1 gp120 V1V2 induce distinct conformation-specific antibody responses in rabbits
Nguyen et al. Oligomannose glycopeptide conjugates elicit antibodies targeting the glycan core rather than its extremities
Ray et al. Antigenic properties of the HIV envelope on virions in solution
Fera et al. HIV envelope V3 region mimic embodies key features of a broadly neutralizing antibody lineage epitope
Chuang et al. Development of a 3mut-apex-stabilized envelope trimer that expands HIV-1 neutralization breadth when used to boost fusion peptide-directed vaccine-elicited responses
Wibmer et al. Common helical V1V2 conformations of HIV-1 Envelope expose the α4β7 binding site on intact virions
Orwenyo et al. Systematic synthesis and binding study of HIV V3 glycopeptides reveal the fine epitopes of several broadly neutralizing antibodies
Kumar et al. A VH1-69 antibody lineage from an infected Chinese donor potently neutralizes HIV-1 by targeting the V3 glycan supersite