Antibody Domain Exchange Is an Immunological Solution to Carbohydrate Cluster Recognition-Reference-Cited by-同舟云学术

Antibody Domain Exchange Is an Immunological Solution to Carbohydrate Cluster Recognition

Published:2003-06-27 Issue:5628 Volume:300 Page:2065-2071
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Calarese Daniel A.¹²³⁴⁵,Scanlan Christopher N.¹²³⁴⁵,Zwick Michael B.¹²³⁴⁵,Deechongkit Songpon¹²³⁴⁵,Mimura Yusuke¹²³⁴⁵,Kunert Renate¹²³⁴⁵,Zhu Ping¹²³⁴⁵,Wormald Mark R.¹²³⁴⁵,Stanfield Robyn L.¹²³⁴⁵,Roux Kenneth H.¹²³⁴⁵,Kelly Jeffery W.¹²³⁴⁵,Rudd Pauline M.¹²³⁴⁵,Dwek Raymond A.¹²³⁴⁵,Katinger Hermann¹²³⁴⁵,Burton Dennis R.¹²³⁴⁵,Wilson Ian A.¹²³⁴⁵

Affiliation:

1. Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.

2. Department of Immunology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.

3. Department of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.

4. Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.

5. The Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, UK.

Abstract

Human antibody 2G12 neutralizes a broad range of human immunodeficiency virus type 1 (HIV-1) isolates by binding an unusually dense cluster of carbohydrate moieties on the âsilentâ face of the gp120 envelope glycoprotein. Crystal structures of Fab 2G12 and its complexes with the disaccharide ManÎ±1-2Man and with the oligosaccharide Man 9 GlcNAc 2 revealed that two Fabs assemble into an interlocked V H domain-swapped dimer. Further biochemical, biophysical, and mutagenesis data strongly support a Fab-dimerized antibody as the prevalent form that recognizes gp120. The extraordinary configuration of this antibody provides an extended surface, with newly described binding sites, for multivalent interaction with a conserved cluster of oligomannose type sugars on the surface of gp120. The unique interdigitation of Fab domains within an antibody uncovers a previously unappreciated mechanism for high-affinity recognition of carbohydrate or other repeating epitopes on cell or microbial surfaces.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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