Antibody 2G12 recognizes di-mannose equivalently in domain- and nondomain-exchanged forms but only binds the HIV-1 glycan shield if domain exchanged.

@article{Doores2010Antibody2R,
  title={Antibody 2G12 recognizes di-mannose equivalently in domain- and nondomain-exchanged forms but only binds the HIV-1 glycan shield if domain exchanged.},
  author={Katie J. Doores and Zara Fulton and Michael M. Huber and Ian A. Wilson and Dennis R. Burton},
  journal={Journal of virology},
  year={2010},
  volume={84 20},
  pages={
          10690-9
        }
}
The broadly neutralizing anti-human immunodeficiency virus type 1 (HIV-1) antibody 2G12 targets the high-mannose cluster on the glycan shield of HIV-1. 2G12 has a unique V(H) domain-exchanged structure, with a multivalent binding surface that includes two primary glycan binding sites. The high-mannose cluster is an attractive target for HIV-1 vaccine design, but so far, no carbohydrate immunogen has elicited 2G12-like antibodies. Important questions remain as to how this domain exchange arose… CONTINUE READING

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HIV glycans in infection and immunity

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