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

Yuan et al., 2022 - Google Patents

Rapid discovery of diverse neutralizing SARS-CoV-2 antibodies from large-scale synthetic phage libraries

Yuan et al., 2022

View PDF @Full View
Document ID
4725594965453909457
Author
Yuan T
Garg P
Wang L
Willis J
Kwan E
Hernandez A
Tuscano E
Sever E
Keane E
Soto C
Mucker E
Fouch M
Davidson E
Doranz B
Kailasan S
Aman M
Li H
Hooper J
Saphire E
Crowe J
Liu Q
Axelrod F
Sato A
Publication year
Publication venue
MAbs

External Links

Snippet

ABSTRACT Coronavirus disease 2019 (COVID-19) is an evolving global public health crisis in need of therapeutic options. Passive immunization of monoclonal antibodies (mAbs) represents a promising therapeutic strategy capable of conferring immediate protection from …
Continue reading at www.tandfonline.com (PDF) (other versions)

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
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2317/00—Immunoglobulins specific features
    • C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
    • C07K2317/33—Crossreactivity, e.g. for species or epitope, or lack of said crossreactivity
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2317/00—Immunoglobulins specific features
    • C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
    • C07K2317/76—Antagonist effect on antigen, e.g. neutralization or inhibition of binding
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
    • C07K16/12—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria
    • C07K16/1203—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-negative bacteria
    • C07K16/1228—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-negative bacteria from Enterobacteriaceae (F), e.g. Citrobacter, Serratia, Proteus, Providencia, Morganella, Yersinia
    • C07K16/1232—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-negative bacteria from Enterobacteriaceae (F), e.g. Citrobacter, Serratia, Proteus, Providencia, Morganella, Yersinia from Escherichia (G)
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2317/00—Immunoglobulins specific features
    • C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
    • C07K2317/21—Immunoglobulins specific features characterized by taxonomic origin from primates, e.g. man
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
    • C07K16/12—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria
    • C07K16/1267—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-positive bacteria
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2317/00—Immunoglobulins specific features
    • C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
    • C07K2317/92—Affinity (KD), association rate (Ka), dissociation rate (Kd) or EC50 value
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
    • C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2317/00—Immunoglobulins specific features
    • C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
    • C07K2317/55—Fab or Fab'
    • 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
    • A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies

Similar Documents

Publication Publication Date Title
Ku et al. Molecular determinants and mechanism for antibody cocktail preventing SARS-CoV-2 escape
Clark et al. SARS-CoV-2 evolution in an immunocompromised host reveals shared neutralization escape mechanisms
Yuan et al. Rapid discovery of diverse neutralizing SARS-CoV-2 antibodies from large-scale synthetic phage libraries
Shrestha et al. Broadly-neutralizing antibodies against emerging SARS-CoV-2 variants
Widjaja et al. Towards a solution to MERS: protective human monoclonal antibodies targeting different domains and functions of the MERS-coronavirus spike glycoprotein
Bertoglio et al. A SARS-CoV-2 neutralizing antibody selected from COVID-19 patients binds to the ACE2-RBD interface and is tolerant to most known RBD mutations
Corti et al. Prophylactic and postexposure efficacy of a potent human monoclonal antibody against MERS coronavirus
Bianchini et al. Human neutralizing antibodies to cold linear epitopes and subdomain 1 of the SARS-CoV-2 spike glycoprotein
Planchais et al. Potent human broadly SARS-CoV-2–neutralizing IgA and IgG antibodies effective against Omicron BA. 1 and BA. 2
Throsby et al. Isolation and characterization of human monoclonal antibodies from individuals infected with West Nile Virus
Du et al. A broadly neutralizing humanized ACE2-targeting antibody against SARS-CoV-2 variants
Olal et al. Structure of an antibody in complex with its mucin domain linear epitope that is protective against Ebola virus
Milligan et al. Asymmetric and non-stoichiometric glycoprotein recognition by two distinct antibodies results in broad protection against ebolaviruses
Hülseweh et al. Human-like antibodies neutralizing Western equine encephalitis virus
Torres et al. Structural insights of a highly potent pan-neutralizing SARS-CoV-2 human monoclonal antibody
Rani et al. Increased antibody affinity confers broad in vitro protection against escape mutants of severe acute respiratory syndrome coronavirus
Miao et al. A novel biparatopic hybrid antibody-ACE2 fusion that blocks SARS-CoV-2 infection: implications for therapy
Hong et al. Dromedary camel nanobodies broadly neutralize SARS-CoV-2 variants
Rouet et al. Potent SARS-CoV-2 binding and neutralization through maturation of iconic SARS-CoV-1 antibodies
Stefan et al. Development of potent and effective synthetic SARS-CoV-2 neutralizing nanobodies
Li et al. Uncovering a conserved vulnerability site in SARS‐CoV‐2 by a human antibody
Bullen et al. Cross-reactive SARS-CoV-2 neutralizing antibodies from deep mining of early patient responses
Piepenbrink et al. Potent universal beta-coronavirus therapeutic activity mediated by direct respiratory administration of a Spike S2 domain-specific human neutralizing monoclonal antibody
Gu et al. A human antibody of potent efficacy against SARS-CoV-2 in rhesus macaques showed strong blocking activity to B. 1.351
Weinstein et al. A potent alpaca-derived nanobody that neutralizes SARS-CoV-2 variants