title: Comparative Proteomics of Human and Macaque Milk Reveals Species-Specific Nutrition during Postnatal Development.
abstract: Milk has been well established as the optimal nutrition source for infants, yet there is still much to be understood about its molecular composition. Therefore, our objective was to develop and compare comprehensive milk proteomes for human and rhesus macaques to highlight differences in neonatal nutrition. We developed a milk proteomics technique that overcomes previous technical barriers including pervasive post-translational modifications and limited sample volume. We identified 1606 and 518 proteins in human and macaque milk, respectively. During analysis of detected protein orthologs, we identified 88 differentially abundant proteins. Of these, 93% exhibited increased abundance in human milk relative to macaque and include lactoferrin, polymeric immunoglobulin receptor, alpha-1 antichymotrypsin, vitamin D-binding protein, and haptocorrin. Furthermore, proteins more abundant in human milk compared with macaque are associated with development of the gastrointestinal tract, the immune system, and the brain. Overall, our novel proteomics method reveals the first comprehensive macaque milk proteome and 524 newly identified human milk proteins. The differentially abundant proteins observed are consistent with the perspective that human infants, compared with nonhuman primates, are born at a slightly earlier stage of somatic development and require additional support through higher quantities of specific proteins to nurture human infant maturation.
authors.forename: Kristen L
authors.initials: KL
authors.lastname: Beck
authors.forename: Darren
authors.initials: D
authors.lastname: Weber
authors.forename: Brett S
authors.initials: BS
authors.lastname: Phinney
authors.forename: Jennifer T
authors.initials: JT
authors.lastname: Smilowitz
authors.affiliation: ⊥Department of Human Evolutionary Biology, Harvard University, 11 Divinity Avenue, Cambridge, Massachusetts 02138, United States.
authors.forename: Katie
authors.initials: K
authors.lastname: Hinde
authors.forename: Bo
authors.initials: B
authors.lastname: Lönnerdal
authors.forename: Ian
authors.initials: I
authors.lastname: Korf
authors.forename: Danielle G
authors.initials: DG
authors.lastname: Lemay
mesh_terms: D000818:Animals; D001921:Brain / Q000254:growth & development / Q000378:metabolism; D002657:Child Development / Q000502:physiology; D002853:Chromatography, Liquid; D005260:Female; D041981:Gastrointestinal Tract / Q000254:growth & development / Q000378:metabolism; D006801:Humans; D007107:Immune System / Q000254:growth & development / Q000378:metabolism; D007223:Infant; D007774:Lactation / Q000502:physiology*; D007781:Lactoferrin / Q000302:isolation & purification / Q000378:metabolism; D008253:Macaca mulatta / Q000254:growth & development / Q000378:metabolism; D008895:Milk, Human / Q000737:chemistry* / Q000378:metabolism; D058977:Molecular Sequence Annotation; D020543:Proteome / Q000302:isolation & purification* / Q000378:metabolism; D019056:Receptors, Polymeric Immunoglobulin / Q000302:isolation & purification / Q000378:metabolism; D013045:Species Specificity; D053719:Tandem Mass Spectrometry; D014155:Transcobalamins / Q000302:isolation & purification / Q000378:metabolism; D014809:Vitamin D-Binding Protein / Q000302:isolation & purification / Q000378:metabolism; D000514:alpha 1-Antichymotrypsin / Q000302:isolation & purification / Q000378:metabolism
chemical_list: C490098:LTF protein, human; D020543:Proteome; D019056:Receptors, Polymeric Immunoglobulin; D014155:Transcobalamins; D014809:Vitamin D-Binding Protein; D000514:alpha 1-Antichymotrypsin; D007781:Lactoferrin
keywords: LC−MS/MS; comparative biology; development; human; infant; lactation; macaque; milk; nutrition; proteome