Abstract
Sialic acid is a nutrient of bacteria important in host-pathogen interactions. The mechanism of transport of sialic acid from outer membrane to periplasmic space of Escherichia coli is not known. N-acetylneuraminic acid (Neu5Ac) - the most abundant form of sialic acid - induces a specific porin NanC (N-acetylneuraminic acid Channel) in the outer membrane of E. coli. Recently, a high resolution structure of NanC (Wirth et al., J.Mol.Biol., (2009) 394:718) revealed unique structural features that support Neu5Ac transport.
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