Lectins - carbohydrate-binding proteins involved in a variety of recognitio
n processes - exhibit considerable structural diversity. Three new:lectin f
olds and further elaborations of known folds have been described recently L
arge variability in quaternary association resulting from small alterations
in essentially the same tertiary structure is a properly exhibited special
ly by legume:lectins, The strategies used by lectins to generate carbohydra
te specificity include the extensive use of water bridges, post-translation
al modification and oligomerisation. Recent results pertaining to influenza
and foot-and-mouth viruses further elaborate the role of lectins in infect
ion.