Mark R. Wormald

TL;DR: New molecular models of all the immunoglobulins are included to provide a basis for informed and critical discussion and to optimize the properties of therapeutic antibodies.

TL;DR: 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, finding a previously unappreciated mechanism for high-affinity recognition of carbohydrate or other repeating epitopes on cell or microbial surfaces.

TL;DR: It is demonstrated here that the alteration in glycosylation associated with rheumatoid arthritis can create a new mode for the interaction of IgG with complement through binding to the collagenous lectin mannose-binding protein (MBP).

TL;DR: Consideration of all the data, together with inspection of a molecular model of gp120, suggests that the most likely epitope for 2G12 is formed from mannose residues contributed by the glycans attached to N295 and N332, with the other glycans playing an indirect role in maintaining epitope conformation.

TL;DR: It is shown that antibodies binding cell-surface PrPC inhibit PrPSc formation in a dose-dependent manner, and this observations support the use of antibodies in the prevention and treatment of prion diseases and identify a region of PrPC for drug targeting.