Ma et al., 2011 - Google Patents
Envelope deglycosylation enhances antigenicity of HIV-1 gp41 epitopes for both broad neutralizing antibodies and their unmutated ancestor antibodiesMa et al., 2011
View HTML- Document ID
- 13528338020947402541
- Author
- Ma B
- Alam S
- Go E
- Lu X
- Desaire H
- Tomaras G
- Bowman C
- Sutherland L
- Scearce R
- Santra S
- Letvin N
- Kepler T
- Liao H
- Haynes B
- Publication year
- Publication venue
- PLoS pathogens
External Links
Snippet
The HIV-1 gp41 envelope (Env) membrane proximal external region (MPER) is an important vaccine target that in rare subjects can elicit neutralizing antibodies. One mechanism proposed for rarity of MPER neutralizing antibody generation is lack of reverted unmutated …
- 102000004965 antibodies 0 title abstract description 66
Classifications
-
- 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
- C07K16/1036—Retroviridae, e.g. leukemia viruses
- C07K16/1045—Lentiviridae, e.g. HIV, FIV, SIV
- C07K16/1063—Lentiviridae, e.g. HIV, FIV, SIV env, e.g. gp41, gp110/120, gp160, V3, PND, CD4 binding site
-
- 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
- C07K16/1036—Retroviridae, e.g. leukemia viruses
- C07K16/1045—Lentiviridae, e.g. HIV, FIV, SIV
- C07K16/1054—Lentiviridae, e.g. HIV, FIV, SIV gag-pol, e.g. p17, p24
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2740/00—Reverse Transcribing RNA Viruses
- C12N2740/00011—Reverse Transcribing RNA Viruses
- C12N2740/10011—Retroviridae
- C12N2740/16011—Human Immunodeficiency Virus, HIV
- C12N2740/16111—Human Immunodeficiency Virus, HIV concerning HIV env
- C12N2740/16122—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2740/00—Reverse Transcribing RNA Viruses
- C12N2740/00011—Reverse Transcribing RNA Viruses
- C12N2740/10011—Retroviridae
- C12N2740/16011—Human Immunodeficiency Virus, HIV
- C12N2740/16111—Human Immunodeficiency Virus, HIV concerning HIV env
- C12N2740/16134—Use of virus or viral component as vaccine, e.g. live-attenuated or inactivated virus, VLP, viral protein
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2740/00—Reverse Transcribing RNA Viruses
- C12N2740/00011—Reverse Transcribing RNA Viruses
- C12N2740/10011—Retroviridae
- C12N2740/15011—Lentivirus, not HIV, e.g. FIV, SIV
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/12—Viral antigens
- A61K39/21—Retroviridae, e.g. equine infectious anemia virus
-
- 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
- G01N33/569—Immunoassay; Biospecific binding assay for micro-organisms, e.g. protozoa, bacteria, viruses
- G01N33/56983—Viruses
- G01N33/56988—AIDS or HTLV
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Ma et al. | Envelope deglycosylation enhances antigenicity of HIV-1 gp41 epitopes for both broad neutralizing antibodies and their unmutated ancestor antibodies | |
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 | |
Zhou et al. | Quantification of the impact of the HIV-1-glycan shield on antibody elicitation | |
Feng et al. | Thermostability of well-ordered HIV spikes correlates with the elicitation of autologous tier 2 neutralizing antibodies | |
Sanders et al. | HIV-1 neutralizing antibodies induced by native-like envelope trimers | |
Klasse et al. | Sequential and simultaneous immunization of rabbits with HIV-1 envelope glycoprotein SOSIP. 664 trimers from clades A, B and C | |
Walker et al. | A limited number of antibody specificities mediate broad and potent serum neutralization in selected HIV-1 infected individuals | |
Binley et al. | Profiling the specificity of neutralizing antibodies in a large panel of plasmas from patients chronically infected with human immunodeficiency virus type 1 subtypes B and C | |
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 | |
Hoffenberg et al. | Identification of an HIV-1 clade A envelope that exhibits broad antigenicity and neutralization sensitivity and elicits antibodies targeting three distinct epitopes | |
Sanders et al. | A next-generation cleaved, soluble HIV-1 Env trimer, BG505 SOSIP. 664 gp140, expresses multiple epitopes for broadly neutralizing but not non-neutralizing antibodies | |
Selvarajah et al. | Comparing antigenicity and immunogenicity of engineered gp120 | |
Mikell et al. | Characteristics of the earliest cross-neutralizing antibody response to HIV-1 | |
US9738688B2 (en) | HIV-1 envelope glycoprotein | |
Davenport et al. | Binding interactions between soluble HIV envelope glycoproteins and quaternary-structure-specific monoclonal antibodies PG9 and PG16 | |
Law et al. | Antigenic and immunogenic study of membrane-proximal external region-grafted gp120 antigens by a DNA prime-protein boost immunization strategy | |
Dubrovskaya et al. | Targeted N-glycan deletion at the receptor-binding site retains HIV Env NFL trimer integrity and accelerates the elicited antibody response | |
Wang et al. | HIV-1 gp41 core with exposed membrane-proximal external region inducing broad HIV-1 neutralizing antibodies | |
EP2788026A2 (en) | V1v2 immunogens | |
Schiffner et al. | Immune focusing and enhanced neutralization induced by HIV-1 gp140 chemical cross-linking | |
Schroeder et al. | Breaching peripheral tolerance promotes the production of HIV-1–neutralizing antibodies | |
Leaman et al. | In-solution virus capture assay helps deconstruct heterogeneous antibody recognition of human immunodeficiency virus type 1 | |
Qin et al. | Eliciting neutralizing antibodies with gp120 outer domain constructs based on M-group consensus sequence | |
Venditto et al. | Rational design of membrane proximal external region lipopeptides containing chemical modifications for HIV-1 vaccination | |
Carbonetti et al. | Soluble HIV-1 envelope immunogens derived from an elite neutralizer elicit cross-reactive V1V2 antibodies and low potency neutralizing antibodies |