HIV-1 rational vaccine design: Molecular details of b12-gp120 complex structure Article uri icon


MeSH Major

  • Eye Diseases
  • Neuronal Ceroid-Lipofuscinoses


  • One of the great challenges for the design of an effective HIV-1 vaccine is the design of an immunogen that will evoke neutralizing antibody responses to a broad spectrum of the different HIV isolates now circulating. Unlike the current vaccines that were invented mostly by trial and error, HIV-1, to date, has resisted all such empirical efforts and, thus, a rational vaccine design approach is necessary. To evoke an effective virus-neutralizing immune response to HIV-1, one logical target to consider is the site of viral attachment to the cellular receptor. The paper under evaluation has advanced the feasibility of this approach by solving the high resolution crystal structure of the envelope protein, gp120, bound to a broadly neutralizing monoclonal antibody, b12, that recognizes the CD4-binding site. Zhou and colleagues' work provides a 'molecular map' of this domain to accelerate a rational immunogen-design effort with the potential to offer a host of novel vaccine candidates for evaluation. © 2007 Future Drugs Ltd.

publication date

  • June 2007



  • Article


Digital Object Identifier (DOI)

  • 10.1586/14760584.6.3.319

Additional Document Info

start page

  • 319

end page

  • 21


  • 6


  • 3