Structural and functional aspects of three major glycoproteins of the human milk fat globule membrane.

The MUC1 mucin, lactadherin, and butyrophilin are 3 major components of the human milk fat globule membrane. The mucin inhibits binding of S-fimbriated Escherichia coli to buccal epithelial cells, and lactadherin prevents symptomatic rotavirus infection in breast-fed infants. Butyrophilin has been suggested to be a structural component of the human milk fat globule (HMFG) membrane and to have receptor functions, but has no known anti-infective activity.

Glycoproteins of the human milk fat globule in the protection of the breast-fed infant against infections.

Nonimmunological components in human milk can protect breast-fed infants against infection by microorganisms. The structural and functional characteristics of four such components are discussed. The mucin inhibits binding of S-fimbriated Escherichia coli to bucal epithelial cells; lactadherin prevents symptomatic rotavirus-induced infection; glycoaminoglycans inhibit binding of human immunodeficiency virus gp120 to its host cell CD4 receptor, and oligosaccharides provide protection against several pathogens and their toxins.