Immunotypes of a quaternary site of HIV-1 vulnerability and their recognition by antibodies

J Virol. 2011 May;85(9):4578-85. doi: 10.1128/JVI.02585-10. Epub 2011 Feb 16.


HIV-1 is neutralized by a class of antibodies that preferentially recognize a site formed on the assembled viral spike. Such quaternary structure-specific antibodies have diverse neutralization breadths, with antibodies PG16 and PG9 able to neutralize 70 to 80% of circulating HIV-1 isolates while antibody 2909 is specific for strain SF162. We show that alteration between a rare lysine and a common N-linked glycan at position 160 of HIV-1 gp120 is primarily responsible for toggling between 2909 and PG16/PG9 neutralization sensitivity. Quaternary structure-specific antibodies appear to target antigenic variants of the same epitope, with neutralization breadth determined by the prevalence of recognized variants among circulating isolates.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, N.I.H., Intramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Antibodies, Neutralizing / immunology*
  • Epitopes / genetics
  • Epitopes / immunology
  • Glycosylation
  • HIV Antibodies / immunology*
  • HIV Envelope Protein gp120 / immunology*
  • HIV-1 / immunology*
  • Lysine / metabolism


  • Antibodies, Neutralizing
  • Epitopes
  • HIV Antibodies
  • HIV Envelope Protein gp120
  • gp120 protein, Human immunodeficiency virus 1
  • Lysine