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Monitoring Beta-casein phosphorylation and O-glycosylation over lactation reveals distinct differences between the proteome and endogenous peptidome

ABSTRACT: Human milk is a vital biofluid containing a myriad of molecular components to ensure an infants best start at a healthy life. One key component of human milk is Beta-casein, a protein which is not only a structural constituent of casein micelles but also a source of bioactive, often antimicrobial, peptides contributing to milks endogenous peptidome. Importantly, post-translational modifications (PTMs) like phosphorylation and glycosylation typically affect the function of proteins and peptides, but here our understanding of Beta-casein is critically limited. To uncover the scope of proteoforms and endogenous peptidoforms we utilized mass spectrometry (LC-MSMS) to achieve in-depth longitudinal profiling of Beta-casein from human milk, studying two donors across 16 weeks of lactation. We not only observed changes in Beta-caseins known protein and endogenous peptidome phosphorylation, but also in previously unexplored O-glycosylation. This newly discovered PTM of Beta-casein may be important as it resides on known Beta-casein-derived antimicrobial peptide sequences.

INSTRUMENT(S): Orbitrap Fusion Lumos, Orbitrap Fusion

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Albert J.R. Heck

PROVIDER: MSV000087464 | MassIVE | Thu May 20 07:33:00 BST 2021

REPOSITORIES: MassIVE

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