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Review
. 2013 Aug;8(4):354-62.
doi: 10.1089/bfm.2013.0016. Epub 2013 May 22.

Human milk glycoproteins protect infants against human pathogens

Bo Liu  1 , David S Newburg
Affiliations
Review

Human milk glycoproteins protect infants against human pathogens

Bo Liu et al. Breastfeed Med. 2013 Aug.

Abstract

Breastfeeding protects the neonate against pathogen infection. Major mechanisms of protection include human milk glycoconjugates functioning as soluble receptor mimetics that inhibit pathogen binding to the mucosal cell surface, prebiotic stimulation of gut colonization by favorable microbiota, immunomodulation, and as a substrate for bacterial fermentation products in the gut. Human milk proteins are predominantly glycosylated, and some biological functions of these human milk glycoproteins (HMGPs) have been reported. HMGPs range in size from 14 kDa to 2,000 kDa and include mucins, secretory immunoglobulin A, bile salt-stimulated lipase, lactoferrin, butyrophilin, lactadherin, leptin, and adiponectin. This review summarizes known biological roles of HMGPs that may contribute to the ability of human milk to protect neonates from disease.

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Figures

FIG. 1.
FIG. 1.
Sodium dodecyl sulfate–polyacrylamide gel electrophoresis analysis of human milk mucins from a pool of 20 human milk donors. The 4–12% gradient sodium dodecyl sulfate–polyacrylamide gel–electrophoresed gel was stained with periodic acid–Schiff reagent. Mucin 1 and mucin 4 were identified by western blot. The arrows indicate mucin 1, mucin 4, and an unknown band.
FIG. 2.
FIG. 2.
Structural motifs of mucin 1 and mucin 4. Key domains include the following: a variable number of tandem repeats (VNTR); sperm protein, exterokinase, and agrin (SEA) modules; transmembrane (TM) domains; cytoplasmic tail (CT); nidogen homology sequence (NIDO); adhesion-associated domain in mucin 4 and other proteins (AMOP); von Willebrand factor D sequence (VWD); and epidermal growth factor (EGF)-like regions. aa, amino acids.
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