Yang et al., 2022 - Google Patents
Neutralizing antibodies induced in immunized macaques recognize the CD4-binding site on an occluded-open HIV-1 envelope trimerYang et al., 2022
View HTML- Document ID
- 9636039852934313368
- Author
- Yang Z
- Dam K
- Bridges M
- Hoffmann M
- DeLaitsch A
- Gristick H
- Escolano A
- Gautam R
- Martin M
- Nussenzweig M
- Hubbell W
- Bjorkman P
- Publication year
- Publication venue
- Nature communications
External Links
Snippet
Broadly-neutralizing antibodies (bNAbs) against HIV-1 Env can protect from infection. We characterize Ab1303 and Ab1573, heterologously-neutralizing CD4-binding site (CD4bs) antibodies, isolated from sequentially-immunized macaques. Ab1303/Ab1573 binding is …
- 102100013077 CD4 0 title abstract description 58
Classifications
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
-
- G—PHYSICS
- G06—COMPUTING; CALCULATING; COUNTING
- G06F—ELECTRICAL DIGITAL DATA PROCESSING
- G06F19/00—Digital computing or data processing equipment or methods, specially adapted for specific applications
- G06F19/10—Bioinformatics, i.e. methods or systems for genetic or protein-related data processing in computational molecular biology
- G06F19/16—Bioinformatics, i.e. methods or systems for genetic or protein-related data processing in computational molecular biology for molecular structure, e.g. structure alignment, structural or functional relations, protein folding, domain topologies, drug targeting using structure data, involving two-dimensional or three-dimensional structures
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/08—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses
- C07K16/10—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses from RNA viruses, e.g. hepatitis E virus
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Wang et al. | Partially open HIV-1 envelope structures exhibit conformational changes relevant for coreceptor binding and fusion | |
Yang et al. | Neutralizing antibodies induced in immunized macaques recognize the CD4-binding site on an occluded-open HIV-1 envelope trimer | |
Juraszek et al. | Stabilizing the closed SARS-CoV-2 spike trimer | |
Kulp et al. | Structure-based design of native-like HIV-1 envelope trimers to silence non-neutralizing epitopes and eliminate CD4 binding | |
Kong et al. | Fusion peptide of HIV-1 as a site of vulnerability to neutralizing antibody | |
He et al. | HIV-1 vaccine design through minimizing envelope metastability | |
Van Gils et al. | An HIV-1 antibody from an elite neutralizer implicates the fusion peptide as a site of vulnerability | |
Julien et al. | Broadly neutralizing antibody PGT121 allosterically modulates CD4 binding via recognition of the HIV-1 gp120 V3 base and multiple surrounding glycans | |
Liu et al. | Quaternary contact in the initial interaction of CD4 with the HIV-1 envelope trimer | |
Pancera et al. | Structure and immune recognition of trimeric pre-fusion HIV-1 Env | |
Scharf et al. | Broadly neutralizing antibody 8ANC195 recognizes closed and open states of HIV-1 Env | |
Sarkar et al. | Structure of a cleavage-independent HIV Env recapitulates the glycoprotein architecture of the native cleaved trimer | |
Wu et al. | Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing | |
Ying et al. | Junctional and allele-specific residues are critical for MERS-CoV neutralization by an exceptionally potent germline-like antibody | |
Pancera et al. | Crystal structure of PG16 and chimeric dissection with somatically related PG9: structure-function analysis of two quaternary-specific antibodies that effectively neutralize HIV-1 | |
Cormier et al. | Cryo-EM structure of the αvβ8 integrin reveals a mechanism for stabilizing integrin extension | |
Yang et al. | Asymmetric opening of HIV-1 Env bound to CD4 and a coreceptor-mimicking antibody | |
Shiakolas et al. | Efficient discovery of SARS-CoV-2-neutralizing antibodies via B cell receptor sequencing and ligand blocking | |
Barnes et al. | Structural classification of neutralizing antibodies against the SARS-CoV-2 spike receptor-binding domain suggests vaccine and therapeutic strategies | |
Gray et al. | Unravelling the molecular basis of high affinity nanobodies against HIV p24: in vitro functional, structural, and in silico insights | |
Jette et al. | Cryo-EM structures of HIV-1 trimer bound to CD4-mimetics BNM-III-170 and M48U1 adopt a CD4-bound open conformation | |
Fera et al. | HIV envelope V3 region mimic embodies key features of a broadly neutralizing antibody lineage epitope | |
Kumar et al. | Capturing the inherent structural dynamics of the HIV-1 envelope glycoprotein fusion peptide | |
Wibmer et al. | Common helical V1V2 conformations of HIV-1 Envelope expose the α4β7 binding site on intact virions | |
Yuan et al. | Structural basis of a public antibody response to SARS-CoV-2 |