Anti-respiratory syncytial virus antibodies, methods of their generation and use
Inventors
Interested in licensing this patent?
MTEC can help explore whether this patent might be available for licensing for your application.
Assignees
Member
Mapp Biopharmaceutical, Inc.Mapp Biopharmaceutical, Inc. is a US-based biotechnology company focused on developing monoclonal antibody therapeutics for the prevention and treatment of infectious diseases with an emphasis on addressing unmet needs in global health and biodefense. Founded in 2003 by Drs. Kevin Whaley and Larry Zeitlin, the company pursues treatments for high-priority pathogens, including ebolaviruses, Marburg virus, Nipah virus, and other threats such as hantavirus and ricin. Mapp advances candidates through preclinical and clinical evaluation, often in partnership with government and academic entities.
Mapp Biopharmaceutical, Inc. is a US-based biotechnology company focused on developing monoclonal antibody therapeutics for the prevention and treatment of infectious diseases with an emphasis on addressing unmet needs in global health and biodefense. Founded in 2003 by Drs. Kevin Whaley and Larry Zeitlin, the company pursues treatments for high-priority pathogens, including ebolaviruses, Marburg virus, Nipah virus, and other threats such as hantavirus and ricin. Mapp advances candidates through preclinical and clinical evaluation, often in partnership with government and academic entities.
Publication Number
US-12630611-B2
Publication Date
2026-05-19
Expiration Date
Abstract
Provided are antibodies or antigen binding polypeptides characterized by the ability to neutralize respiratory syncytial virus (RSV). Specifically, the antibodies or antigen binding polypeptides are characterized by high affinity binding to RSV fusion glycoprotein (RSVF). Further provided are methods for their identification, isolation, generation, preparation, and use, as well as the heavy chain and light chain sequences of the antibodies provided.
Core Innovation
The invention relates to an antibody component for a composition, where the antibody component consists of a first antibody, or antigen binding fragment thereof, and a second antibody, or antigen binding fragment thereof. The first antibody has heavy and light chain CDRs found in antibody number 554, and the second antibody has heavy and light chain CDRs found in an antibody selected from a specified group of antibody numbers. Both the first and second antibodies specifically bind to and neutralize RSV F, and the composition does not include any antibodies other than the antibody component.
The disclosed subject matter provides amino-acid sequence information for multiple anti-RSV F antibodies, with heavy and light chain variable-region sequence segments and associated SEQ ID NOs. The sequence information is presented to define antibody variable-region sequences directed to RSV F and supports the antibody set associated with anti-RSV F targeting.
The document further characterizes RSV-neutralizing IgGs using binding kinetics, affinity determination, and polyreactivity analyses. Association and dissociation kinetics are determined using BLI-based measurement, Kd values are calculated using a 1:1 model, and polyreactivity is evaluated using a flow-cytometry-based assay with biotinylated soluble membrane protein fractions and biotinylated soluble cytosolic protein fractions.
The document also reports functional neutralization characterization of antibodies using plasma or adenoid tissue neutralization assays. Neutralization is assessed using an rA2-Rluc recombinant RSV luciferase reporter virus, with IC50 and neutralization expressed as reciprocal dilution at 50% reduction based on luciferase readouts.
Claims Coverage
The provided material includes one independent claim, centered on a two-antibody component defined by CDR identity to antibody number 554 and to a selected antibody from a specified list, with an express exclusion of any antibodies other than the antibody component. Dependent claims add framework-region sequence identity constraints, IgG Fc heavy-chain variant features, neutralization potency and binding affinity thresholds, and a treatment method for RSV infection in a mammal.
Two-antibody component defined by specified RSV F cdrs
A composition comprising an antibody component consisting of a first antibody, or antigen binding fragment thereof, with heavy and light chain CDRs found in antibody number 554, and a second antibody, or antigen binding fragment thereof, with heavy and light chain CDRs found in an antibody selected from the group consisting of antibody numbers 843, 466, 2, 71, 112, 217, 227, 228, 249, 467, 469, 470, 832, 471, 516, 527, 532, 543, 544, 551, 571, 578, 581, 592, 615, 641, 868, and 870, wherein each specifically binds to and neutralizes RSV F.
Antibody component excludes any additional antibodies
The composition does not include any antibodies other than the antibody component.
Framework regions with at least 90% sequence identity
The composition is characterized by antibody framework regions having at least 90% sequence identity to specific reference framework regions.
IgG Fc heavy-chain region variant for serum half-life, stability, and/or effector function
The composition includes an IgG Fc heavy-chain region variant designed to increase antibody serum half-life, improve stability, and/or modify effector function.
IC50 below 300 pM for RSV neutralization
Either the first antibody and/or the second antibody has an IC50 below 300 pM for neutralizing RSV.
kd less than 10 nM for binding to pre-F
The first and second antibodies bind to pre-F with a dissociation constant, kD, of less than 10 nM.
Method for treating RSV infection in a mammal
A method for treating an RSV infection in a mammal by administering the composition.
Overall claim coverage centers on a composition with exactly two RSV F-neutralizing antibodies or fragments defined by heavy and light chain CDRs corresponding to antibody number 554 and to one antibody from a specified list, with no additional antibodies included. The dependent claims further constrain framework sequence identity, introduce an IgG Fc heavy-chain variant, and recite IC50 and kD thresholds and a treatment method by administration.
Stated Advantages
Increases antibody serum half-life, improves stability, and/or modifies effector function.
Higher binding affinities and higher neutralization potency for adenoid-derived antibodies than PBMC-derived antibodies.
Neutralization predominantly targeting prefusion RSV F (preF) epitopes.
An atypical IgM+/IgD+ memory B cell population in adenoid tissue contributes substantially to neutralizing antibodies.
Provides RSV neutralization with defined potency and binding affinity to pre-F.
Enables treating an RSV infection in a mammal by administering the composition.
Documented Applications
Treating an RSV infection in a mammal by administering the claimed antibody composition.
Treating RSV infection in humans.
Interested in licensing this patent?