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Proline Is Not Uniquely Capable of Providing the Pivot Point for Domain Swapping in 2G12, a Broadly Neutralizing Antibody against HIV-1 |
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| Authors: | Johannes S Gach Paul G Furtm��ller Heribert Quendler Paul Messner Ralf Wagner Hermann Katinger and Renate Kunert |
| Institution: | From the Departments of ‡Biotechnology and ;¶Chemistry and ;the ‖Center for NanoBiotechnology, University of Natural Resources and Applied Life Sciences, 1190 Vienna, Austria, ;the **Institute of Medical Microbiology and Hygiene, University of Regensburg, 93053 Regensburg, Germany, and ;the §Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, California 92037 |
| Abstract: | The human monoclonal antibody 2G12 is a member of a small group of broadly neutralizing antibodies against human immunodeficiency virus type 1. 2G12 adopts a unique variable heavy domain-exchanged dimeric configuration that results in an extensive multivalent binding surface and the ability to bind with high affinity to densely clustered high mannose oligosaccharides on the “silent” face of the gp120 envelope glycoprotein. Here, we further define the amino acids responsible for this extraordinary domain-swapping event in 2G12. |
| Keywords: | Methods/Circular Dichroism CD Methods/Immunochemistry 2G12 HIV-1 Antibody Structure Domain Swapping gp120 |