Antibody Domain Exchange Is an Immunological Solution to Carbohydrate Cluster Recognition

By D. Calarese, Christopher N. Scanlan, M. Zwick, S. Deechongkit, Y. Mimura, R. Kunert, P. Zhu, M. Wormald, R. Stanfield, K. Roux and 6 more. Science, 2003

768 citations recorded by the source corpus.

Subfields: Molecular Biology, Organic Chemistry, Radiology, Nuclear Medicine and Imaging

View Paper: https://www.semanticscholar.org/paper/573ebb53cb131dd2fa2891c456feffcb1b886ba7

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In Molecular Biology

1. Ian A. Wilson
2. A. Ward
3. Beatrice H. Hahn
4. David S. Wishart
5. Markus R. Wenk

Citations in the corpus

• Human Immunodeficiency Virus Type 1 env Clones from Acute and Early Subtype B Infections for Standardized Assessments of Vaccine-Elicited Neutralizing Antibodies (2005, background): “2G12 recognizes a mannose cluster on gp120 that can involve N-linked glycans at multiple sites, including residues 295, 332, and 392, with possible contributions from residues 339 and 386 (9, 16, 97, 101).”
• Comprehensive Cross-Clade Neutralization Analysis of a Panel of Anti-Human Immunodeficiency Virus Type 1 Monoclonal Antibodies (2004, background): “2G12 is thought to recognize glycans at residues 332 and 392, with some dependence on glycans at positions 295, 339, and 386 (23, 126, 129).”
• A Next-Generation Cleaved, Soluble HIV-1 Env Trimer, BG505 SOSIP.664 gp140, Expresses Multiple Epitopes for Broadly Neutralizing but Not Non-Neutralizing Antibodies (2013, background): “All three antibodies have previously been shown to be dependent on the high-mannose glycan at position N332 for Env recognition [30,43,44,45,46].”