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Structure-Based Modeling of Complement C4 Mediated Neutralization of Adenovirus.

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An antibody (9C12) triggers complement component C4b deposition on adenovirus (AdV) capsids. This C4b entanglement with RGD loops blocks viral uncoating and infection.

Keywords:
adenoviruscomplement C1complement C4molecular dynamicsneutralizationneutralizing antibody

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Area of Science:

  • Virology
  • Immunology
  • Structural Biology

Background:

  • Adenovirus (AdV) infection triggers immune responses, including neutralizing antibodies and complement activation.
  • The anti-hexon antibody 9C12 activates complement, leading to C4b deposition and AdV neutralization.
  • C4b-mediated neutralization blocks protein VI release, essential for viral endosomal escape.

Purpose of the Study:

  • To investigate the structural mechanisms by which C4b blocks AdV uncoating.
  • To model the complex of human adenovirus type-5 (HAdV5) with 9C12, C1, and C4b.

Main Methods:

  • Computational modeling of the HAdV5-9C12-C1-C4b complex.
  • Molecular dynamics simulations of penton base multimers with C4b.

Main Results:

  • The model positions C4b near the Arg-Gly-Asp (RGD) loops of the penton base.
  • C4b potentially binds covalently to amino acids within the RGD loops.
  • Simulations suggest stabilizing interactions between C4b and multiple RGD loops.

Conclusions:

  • C4b deposition on one RGD loop may entangle with other RGD loops on the same penton base multimer.
  • This entanglement mechanism is proposed to physically block AdV uncoating.
  • Understanding this interaction provides structural insights into complement-mediated viral neutralization.