The Broadly Neutralizing Anti-Human Immunodeficiency Virus Type 1 Antibody 2G12 Recognizes a Cluster of α1→2 Mannose Residues on the Outer Face of gp120

By Christopher N. Scanlan, R. Pantophlet, M. Wormald, Erica Ollmann Saphire, R. Stanfield, Ian A. Wilson, H. Katinger, R. Dwek, P. Rudd, D. Burton. Journal of Virology, 2002

701 citations recorded by the source corpus.

Subfields: Molecular Biology, Radiology, Nuclear Medicine and Imaging, Virology

View Paper: https://www.semanticscholar.org/paper/f61120917ca258faa0816d353735588de4b73475

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In Molecular Biology

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

In Virology

1. Beatrice H. Hahn

Citations in the corpus

• 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].”
• 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).”
• Antibody neutralization and escape by HIV-1 (2003, background): “Previously, it has been shown that the monosaccharide d -mannose can specifically compete with HIV-1 gp120 for binding of the glycan-dependent 2G12 monoclonal antibod”