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It is well known that plasma proteins regulate host-pathogen interactions. Two important mechanisms of regulatory function are molecular masking and molecular mimicry. Plasma proteins on the host cell surface are known to share a common conserved structure referred to as the structural core, which is often masked by variations of the core structure, such as N-linked oligosaccharides, glycosaminoglycans and phospholipids. As a result, most of these plasma proteins do not induce an immune response because the structural cores of a number of host molecules are sufficiently similar to those of pathogens. The presence of such a’molecular mask’ has recently been associated with the ability of Gram-negative bacteria to bind to human cells. In this study, we investigated the properties of bacterial binding by plasma proteins, focusing on the mannose-specific lectin of human milk, the N-linked oligosaccharide portion of the envelope protein of viral hepatitis A (HVA), and a bacterial N-linked oligosac
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