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    Structural and molecular analysis of a protective epitope of Lyme disease antigen OspA and antibody interactions

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    Authors
    Shandilya, Shivender
    Yilmaz, Nese Kurt
    Sadowski, Andrew
    Monir, Ejemel
    Schiller, Zachary A.
    Thomas, William D. Jr.
    Klempner, Mark S.
    Schiffer, Celia A.
    Wang, Yang
    UMass Chan Affiliations
    MassBiologics
    Department of Biochemistry and Molecular Pharmacology
    Document Type
    Journal Article
    Publication Date
    2016-11-16
    Keywords
    antibody
    Lyme disease
    mutations
    protein-protein
    structural analysis
    molecular interactions
    vaccine design
    protein structure
    UMCCTS funding
    Bacterial Infections and Mycoses
    Biochemistry
    Immunoprophylaxis and Therapy
    Medicinal Chemistry and Pharmaceutics
    Medicinal-Pharmaceutical Chemistry
    Molecular Biology
    Structural Biology
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    Link to Full Text
    https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5383521/
    Abstract
    The murine monoclonal antibody LA-2 recognizes a clinically protective epitope on outer surface protein (OspA) of Borrelia burgdorferi, the causative agent of Lyme disease in North America. Human antibody equivalence to LA-2 is the best serologic correlate of protective antibody responses following OspA vaccination. Understanding the structural and functional basis of the LA-2 protective epitope is important for developing OspA-based vaccines and discovering prophylactic antibodies against Lyme disease. Here, we present a detailed structure-based analysis of the LA-2/OspA interaction interface and identification of residues mediating antibody recognition. Mutations were introduced into both OspA and LA-2 on the basis of computational predictions on the crystal structure of the complex and experimentally tested for in vitro binding and borreliacidal activity. We find that Y32 and H49 on the LA-2 light chain, N52 on the LA-2 heavy chain and residues A208, N228 and N251 on OspA were the key constituents of OspA/LA-2 interface. These results reveal specific residues that may be exploited to modulate recognition of the protective epitope of OspA and have implications for developing prophylactic passive antibodies.
    Source

    J Mol Recognit. 2016 Nov 16. doi: 10.1002/jmr.2595. Link to article on publisher's site

    DOI
    10.1002/jmr.2595
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/48867
    PubMed ID
    27859766
    Related Resources

    Link to Article in PubMed

    ae974a485f413a2113503eed53cd6c53
    10.1002/jmr.2595
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