Variable Lymphocyte Receptor Recognition of the Immunodominant Glycoprotein of Bacillus anthracis Spores
Variable lymphocyte receptors (VLRs) are the adaptive immune receptors of jawless fish, which evolved adaptive immunity independent of other vertebrates. In lieu of the immunoglobulin fold-based T and B cell receptors, lymphocyte-like cells of jawless fish express VLRs (VLRA, VLRB, or VLRC) composed...
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| Published in | Structure (London) Vol. 20; no. 3; pp. 479 - 486 |
|---|---|
| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
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United States
Elsevier Inc
07.03.2012
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| Subjects | |
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| Abstract | Variable lymphocyte receptors (VLRs) are the adaptive immune receptors of jawless fish, which evolved adaptive immunity independent of other vertebrates. In lieu of the immunoglobulin fold-based T and B cell receptors, lymphocyte-like cells of jawless fish express VLRs (VLRA, VLRB, or VLRC) composed of leucine-rich repeats and are similar to toll-like receptors (TLRs) in structure, but antibodies (VLRB) and T cell receptors (VLRA and VLRC) in function. Here, we present the structural and biochemical characterization of VLR4, a VLRB, in complex with BclA, the immunodominant glycoprotein of Bacillus anthracis spores. Using a combination of crystallography, mutagenesis, and binding studies, we delineate the mode of antigen recognition and binding between VLR4 and BclA, examine commonalities in VLRB recognition of antigens, and demonstrate the potential of VLR4 as a diagnostic tool for the identification of B. anthracis spores.
[Display omitted]
► VLRBs use their C-terminal LRRs and the LRRCT-loop to interact with antigen ► Sequence-related VLRBs exhibit differential recognition of their BclA epitopes ► VLR4 binds a conserved protein epitope, yet is specific for B. anthracis spores |
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| AbstractList | Variable lymphocyte receptors (VLRs) are the adaptive immune receptors of jawless fish, which evolved adaptive immunity independent of other vertebrates. In lieu of the immunoglobulin fold-based T and B cell receptors, lymphocyte-like cells of jawless fish express VLRs (VLRA, VLRB, or VLRC) composed of leucine-rich repeats and are similar to toll-like receptors (TLRs) in structure, but antibodies (VLRB) and T cell receptors (VLRA and VLRC) in function. Here, we present the structural and biochemical characterization of VLR4, a VLRB, in complex with BclA, the immunodominant glycoprotein of Bacillus anthracis spores. Using a combination of crystallography, mutagenesis, and binding studies, we delineate the mode of antigen recognition and binding between VLR4 and BclA, examine commonalities in VLRB recognition of antigens, and demonstrate the potential of VLR4 as a diagnostic tool for the identification of B. anthracis spores.Variable lymphocyte receptors (VLRs) are the adaptive immune receptors of jawless fish, which evolved adaptive immunity independent of other vertebrates. In lieu of the immunoglobulin fold-based T and B cell receptors, lymphocyte-like cells of jawless fish express VLRs (VLRA, VLRB, or VLRC) composed of leucine-rich repeats and are similar to toll-like receptors (TLRs) in structure, but antibodies (VLRB) and T cell receptors (VLRA and VLRC) in function. Here, we present the structural and biochemical characterization of VLR4, a VLRB, in complex with BclA, the immunodominant glycoprotein of Bacillus anthracis spores. Using a combination of crystallography, mutagenesis, and binding studies, we delineate the mode of antigen recognition and binding between VLR4 and BclA, examine commonalities in VLRB recognition of antigens, and demonstrate the potential of VLR4 as a diagnostic tool for the identification of B. anthracis spores. Variable Lymphocyte Receptors (VLRs) are the adaptive immune receptors of jawless fish, which evolved adaptive immunity independent of other vertebrates. In lieu of the immunoglobulin-fold based T- and B-cell receptors, lymphocyte-like cells of jawless fish express VLRs (A, B or C) composed of leucine-rich repeats and are similar to toll-like receptors (TLRs) in structure, but antibodies (VLRB) and T cell receptors (VLRA, C) in function. Here we present the structural and biochemical characterization of VLR4, a VLRB, in complex with BclA, the immunodominant glycoprotein of Bacillus anthracis spores. Using a combination of crystallography, mutagenesis and binding studies, we delineate the mode of antigen recognition and binding between VLR4 and BclA, examine commonalities in VLRB recognition of antigens, and demonstrate the potential of VLR4 as a diagnostic tool for the identification of B. anthracis spores. Variable lymphocyte receptors (VLRs) are the adaptive immune receptors of jawless fish, which evolved adaptive immunity independent of other vertebrates. In lieu of the immunoglobulin fold-based T and B cell receptors, lymphocyte-like cells of jawless fish express VLRs (VLRA, VLRB, or VLRC) composed of leucine-rich repeats and are similar to toll-like receptors (TLRs) in structure, but antibodies (VLRB) and T cell receptors (VLRA and VLRC) in function. Here, we present the structural and biochemical characterization of VLR4, a VLRB, in complex with BclA, the immunodominant glycoprotein of Bacillus anthracis spores. Using a combination of crystallography, mutagenesis, and binding studies, we delineate the mode of antigen recognition and binding between VLR4 and BclA, examine commonalities in VLRB recognition of antigens, and demonstrate the potential of VLR4 as a diagnostic tool for the identification of B. anthracis spores. [Display omitted] ► VLRBs use their C-terminal LRRs and the LRRCT-loop to interact with antigen ► Sequence-related VLRBs exhibit differential recognition of their BclA epitopes ► VLR4 binds a conserved protein epitope, yet is specific for B. anthracis spores Variable lymphocyte receptors (VLRs) are the adaptive immune receptors of jawless fish, which evolved adaptive immunity independent of other vertebrates. In lieu of the immunoglobulin fold-based T and B cell receptors, lymphocyte-like cells of jawless fish express VLRs (VLRA, VLRB, or VLRC) composed of leucine-rich repeats and are similar to toll-like receptors (TLRs) in structure, but antibodies (VLRB) and T cell receptors (VLRA and VLRC) in function. Here, we present the structural and biochemical characterization of VLR4, a VLRB, in complex with BclA, the immunodominant glycoprotein of Bacillus anthracis spores. Using a combination of crystallography, mutagenesis, and binding studies, we delineate the mode of antigen recognition and binding between VLR4 and BclA, examine commonalities in VLRB recognition of antigens, and demonstrate the potential of VLR4 as a diagnostic tool for the identification of B. anthracis spores. Variable lymphocyte receptors (VLRs) are the adaptive immune receptors of jawless fish, which evolved adaptive immunity independent of other vertebrates. In lieu of the immunoglobulin fold-based T and B cell receptors, lymphocyte-like cells of jawless fish express VLRs (VLRA, VLRB, or VLRC) composed of leucine-rich repeats and are similar to toll-like receptors (TLRs) in structure, but antibodies (VLRB) and T cell receptors (VLRA and VLRC) in function. Here, we present the structural and biochemical characterization of VLR4, a VLRB, in complex with BclA, the immunodominant glycoprotein of Bacillus anthracis spores. Using a combination of crystallography, mutagenesis, and binding studies, we delineate the mode of antigen recognition and binding between VLR4 and BclA, examine commonalities in VLRB recognition of antigens, and demonstrate the potential of VLR4 as a diagnostic tool for the identification of B. anthracis spores. |
| Author | Wilson, Ian A. Kirchdoerfer, Robert N. Han, Byung Woo Herrin, Brantley R. Turnbough, Charles L. Cooper, Max D. |
| AuthorAffiliation | 2 The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, United States 1 Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, United States 4 Department of Pathology and Laboratory Medicine, Emory University, Atlanta, Georgia 30322, United States 3 Emory Vaccine Center, Atlanta Georgia 30329, United States 5 Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul 151-742, Korea 6 University of Alabama at Birmingham, Department of Microbiology, Birmingham, AL 35294-2170, United States |
| AuthorAffiliation_xml | – name: 4 Department of Pathology and Laboratory Medicine, Emory University, Atlanta, Georgia 30322, United States – name: 3 Emory Vaccine Center, Atlanta Georgia 30329, United States – name: 1 Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, United States – name: 2 The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, United States – name: 6 University of Alabama at Birmingham, Department of Microbiology, Birmingham, AL 35294-2170, United States – name: 5 Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul 151-742, Korea |
| Author_xml | – sequence: 1 givenname: Robert N. surname: Kirchdoerfer fullname: Kirchdoerfer, Robert N. organization: Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA – sequence: 2 givenname: Brantley R. surname: Herrin fullname: Herrin, Brantley R. organization: Emory Vaccine Center, Atlanta, GA 30329, USA – sequence: 3 givenname: Byung Woo surname: Han fullname: Han, Byung Woo organization: Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul 151-742, Korea – sequence: 4 givenname: Charles L. surname: Turnbough fullname: Turnbough, Charles L. organization: Department of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294-2170, USA – sequence: 5 givenname: Max D. surname: Cooper fullname: Cooper, Max D. organization: Emory Vaccine Center, Atlanta, GA 30329, USA – sequence: 6 givenname: Ian A. surname: Wilson fullname: Wilson, Ian A. email: wilson@scripps.edu organization: Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA |
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| Snippet | Variable lymphocyte receptors (VLRs) are the adaptive immune receptors of jawless fish, which evolved adaptive immunity independent of other vertebrates. In... Variable Lymphocyte Receptors (VLRs) are the adaptive immune receptors of jawless fish, which evolved adaptive immunity independent of other vertebrates. In... |
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| SubjectTerms | Animals Bacillus anthracis Bacillus anthracis - chemistry Cloning, Molecular Crystallography Glycoproteins - chemistry Glycoproteins - metabolism Immunodominant Epitopes - chemistry Immunodominant Epitopes - metabolism Lampreys - immunology Models, Molecular Mutagenesis Protein Binding Receptors, Immunologic - chemistry Spores, Bacterial - chemistry |
| Title | Variable Lymphocyte Receptor Recognition of the Immunodominant Glycoprotein of Bacillus anthracis Spores |
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