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High-mannose-type oligosaccharides bind to human antibody 2G12.
2004 APR 7 - (NewsRx.com & NewsRx.net) -- High-mannose-type oligosaccharides bind to human antibody 2G12, which has implications for HIV-1 vaccine design.
According to a study from the United States, "Human antibody 2G12 broadly neutralizes human immunodeficiency virus type 1 (HIV-1) isolates and shows protective activity against viral challenge in animal models. Previous mutational analysis suggested that 2G12 recognized a novel cluster of high-mannose type oligosaccharides on HIV-1 gp120. To explore the carbohydrate antigen for HIV-1 vaccine design, we have studied the binding of 2G12 to an array of HIV-1 high-mannose type oligosaccharides by competitive ELISAs and found that Man[subscript]9GlNAc is 210- and 74-fold more effective than Man(5)GIcNAc and Man(6)GIcNAc in binding to 2G12."
"The results establish that the larger high-mannose oligosaccharide on HIV-1 is the favorable subunit for 2G12 recognition," said Lai-Xi Wang and colleagues at the University of Maryland. "To mimic the putative epitope of 21312, we have created scaffold-based multivalent Man[subscript]9 clusters and found that the galactose-scaffolded bi-, tri-, and tetra-valent Man[subscript]9 clusters are 7-, ...
- High-mannose-type oligosaccharides bind to human antibody 2G12.
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Source: HighBeam Research, High-mannose-type oligosaccharides bind to human antibody 2G12.