Structural and mutational analysis of human Ad37 and canine adenovirus 2 fiber heads in complex with the D1 domain of coxsackie and adenovirus receptor.

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  • Author(s): Seiradake E;Seiradake E; Lortat-Jacob H; Billet O; Kremer EJ; Cusack S
  • Source:
    The Journal of biological chemistry [J Biol Chem] 2006 Nov 03; Vol. 281 (44), pp. 33704-16. Date of Electronic Publication: 2006 Aug 21.
  • Publication Type:
    Journal Article; Research Support, Non-U.S. Gov't
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print-Electronic Cited Medium: Print ISSN: 0021-9258 (Print) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE
    • Publication Information:
      Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology
      Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology
    • Subject Terms:
      Adenoviridae/*chemistry ; Adenoviridae/*metabolism ; Receptors, Virus/*chemistry ; Receptors, Virus/*metabolism; Adenoviridae/classification ; Adenoviridae/genetics ; Amino Acid Sequence ; Animals ; Conserved Sequence ; Coxsackie and Adenovirus Receptor-Like Membrane Protein ; Crystallography, X-Ray ; Dogs ; Humans ; Models, Molecular ; Molecular Sequence Data ; Mutation/genetics ; Protein Binding ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Sequence Alignment ; Surface Plasmon Resonance ; Water/chemistry
    • Abstract:
      Adenovirus fibers from most serotypes bind the D1 domain of coxsackie and adenovirus receptor (CAR), although the binding residues are not strictly conserved. To understand this further, we determined the crystal structures of canine adenovirus serotype 2 (CAV-2) and the human adenovirus serotype 37 (HAd37) in complex with human CAR D1 at 2.3 and 1.5A resolution, respectively. Structure comparison with the HAd12 fiber head-CAR D1 complex showed that the overall topology of the interaction is conserved but that the interfaces differ in number and identity of interacting residues, shape complementarity, and degree of conformational adaptation. Using surface plasmon resonance, we characterized the binding affinity to CAR D1 of wild type and mutant CAV-2 and HAd37 fiber heads. We found that CAV-2 has the highest affinity but fewest direct interactions, with the reverse being true for HAd37. Moreover, we found that conserved interactions can have a minor contribution, whereas serotype-specific interactions can be essential. These results are discussed in the light of virus evolution and design of adenovirus vectors for gene transfer.
    • Molecular Sequence:
      PDB 2J12; 2J1K; 2J2J
    • Accession Number:
      0 (CLMP protein, human)
      0 (Coxsackie and Adenovirus Receptor-Like Membrane Protein)
      0 (Receptors, Virus)
      059QF0KO0R (Water)
    • Publication Date:
      Date Created: 20060823 Date Completed: 20061211 Latest Revision: 20210209
    • Publication Date:
      20221213
    • Accession Number:
      10.1074/jbc.M605316200
    • Accession Number:
      16923808