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Adenovirus interaction with its cellular receptor CAR

J Howitt1, C W Anderson, P Freimuth

  • 1Biology Department, Brookhaven National Laboratory, Upton, NY 11973, USA.

Current Topics in Microbiology and Immunology
|May 16, 2003
PubMed

Insights

Adenoviruses bind to the coxsackievirus and adenovirus receptor (CAR) using their fiber protein knob. Structural studies reveal how knob architecture balances antigenicity and CAR binding specificity, with CAR remaining non-polymorphic.

Area of Science:

  • Virology
  • Structural Biology
  • Molecular Interactions

Background:

  • Adenoviruses are common viruses infecting various human cell types.
  • Adenovirus-host cell interactions are crucial for viral entry and infection.
  • The coxsackievirus and adenovirus receptor (CAR) is a key cellular receptor for many adenoviruses.

Purpose of the Study:

  • To review structural characterizations of adenovirus knob, CAR, and their complexes.
  • To discuss the evolutionary pressures shaping adenovirus knob architecture for receptor binding and antigenicity.
  • To highlight the conserved nature of CAR despite viral surface variability.

Main Methods:

  • Review of recent structural studies (e.g., X-ray crystallography, cryo-EM) of knob-CAR complexes.
  • Analysis of existing literature on adenovirus fiber protein structure and evolution.
  • Comparative analysis of knob surface variability and CAR structure.

Main Results:

  • Adenovirus fiber knob domains interact with the CAR protein.
  • Knob architecture exhibits a conserved receptor-binding interface and a variable surface for antigenicity.
  • CAR is a non-polymorphic receptor, suggesting conserved binding interactions across adenovirus serotypes.

Conclusions:

  • Adenovirus binding to CAR is mediated by the fiber knob domain.
  • The evolution of knob structure balances the need for immune evasion with conserved CAR recognition.
  • CAR's conserved structure facilitates broad adenovirus tropism and infection.

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