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  1. AU="Hatas, Andrew"
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  1. Article ; Online: Generation of bispecific antibodies by structure-guided redesign of IgG constant regions.

    Iwasaki, Yordkhwan W / Tharakaraman, Kannan / Subramanian, Vidya / Khongmanee, Amnart / Hatas, Andrew / Fleischer, Eduardo / Rurak, Troy T / Ngok-Ngam, Patchara / Tit-Oon, Phanthakarn / Ruchirawat, Mathuros / Satayavivad, Jutamaad / Fuangthong, Mayuree / Sasisekharan, Ram

    Frontiers in immunology

    2023  Volume 13, Page(s) 1063002

    Abstract: Bispecific antibodies (BsAbs) form an exciting class of bio-therapeutics owing to their multispecificity. Although numerous formats have been developed, generation of hetero-tetrameric IgG1-like BsAbs having acceptable safety and pharmacokinetics ... ...

    Abstract Bispecific antibodies (BsAbs) form an exciting class of bio-therapeutics owing to their multispecificity. Although numerous formats have been developed, generation of hetero-tetrameric IgG1-like BsAbs having acceptable safety and pharmacokinetics profiles from a single cell culture system remains challenging due to the heterogeneous pairing between the four chains. Herein, we employed a structure-guided approach to engineer mutations in the constant domain interfaces (C
    MeSH term(s) Animals ; Antibodies, Bispecific ; Immunoglobulin kappa-Chains/genetics ; Transfection ; Immunoglobulin G ; Mammals
    Chemical Substances Antibodies, Bispecific ; Immunoglobulin kappa-Chains ; Immunoglobulin G
    Language English
    Publishing date 2023-01-10
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2606827-8
    ISSN 1664-3224 ; 1664-3224
    ISSN (online) 1664-3224
    ISSN 1664-3224
    DOI 10.3389/fimmu.2022.1063002
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Redesign of a cross-reactive antibody to dengue virus with broad-spectrum activity and increased in vivo potency.

    Tharakaraman, Kannan / Robinson, Luke N / Hatas, Andrew / Chen, Yi-Ling / Siyue, Liu / Raguram, S / Sasisekharan, V / Wogan, Gerald N / Sasisekharan, Ram

    Proceedings of the National Academy of Sciences of the United States of America

    2013  Volume 110, Issue 17, Page(s) E1555–64

    Abstract: Affinity improvement of proteins, including antibodies, by computational chemistry broadly relies on physics-based energy functions coupled with refinement. However, achieving significant enhancement of binding affinity (>10-fold) remains a challenging ... ...

    Abstract Affinity improvement of proteins, including antibodies, by computational chemistry broadly relies on physics-based energy functions coupled with refinement. However, achieving significant enhancement of binding affinity (>10-fold) remains a challenging exercise, particularly for cross-reactive antibodies. We describe here an empirical approach that captures key physicochemical features common to antigen-antibody interfaces to predict protein-protein interaction and mutations that confer increased affinity. We apply this approach to the design of affinity-enhancing mutations in 4E11, a potent cross-reactive neutralizing antibody to dengue virus (DV), without a crystal structure. Combination of predicted mutations led to a 450-fold improvement in affinity to serotype 4 of DV while preserving, or modestly increasing, affinity to serotypes 1-3 of DV. We show that increased affinity resulted in strong in vitro neutralizing activity to all four serotypes, and that the redesigned antibody has potent antiviral activity in a mouse model of DV challenge. Our findings demonstrate an empirical computational chemistry approach for improving protein-protein docking and engineering antibody affinity, which will help accelerate the development of clinically relevant antibodies.
    MeSH term(s) Animals ; Antibodies, Neutralizing/biosynthesis ; Antibodies, Viral/biosynthesis ; Antibody Affinity/genetics ; Binding Sites, Antibody/genetics ; Cross Reactions/immunology ; Dengue Virus/immunology ; Enzyme-Linked Immunosorbent Assay ; Epitopes/genetics ; Mice ; Models, Immunological ; Protein Binding ; Protein Engineering/methods ; Real-Time Polymerase Chain Reaction ; Surface Plasmon Resonance
    Chemical Substances Antibodies, Neutralizing ; Antibodies, Viral ; Epitopes
    Language English
    Publishing date 2013-04-08
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.1303645110
    Database MEDical Literature Analysis and Retrieval System OnLINE

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