Evolutionary glycomics: characterization of milk oligosaccharides in primates.

Bibliographic Collection: 
MOCA Reference, APE
Publication Type: Journal Article
Authors: Tao, Nannan; Wu, Shuai; Kim, Jaehan; An, Hyun Joo; Hinde, Katie; Power, Michael L; Gagneux, Pascal; German, J Bruce; Lebrilla, Carlito B
Year of Publication: 2011
Journal: J Proteome Res
Volume: 10
Issue: 4
Pagination: 1548-57
Date Published: 04/2011
Publication Language: eng
ISSN: 1535-3907
Keywords: Animals, Biological Evolution, Carbohydrate Conformation, Carbohydrate Sequence, Chromatography, Liquid, Cluster Analysis, Glycomics, Humans, Milk, Molecular Sequence Data, Oligosaccharides, Phylogeny, Primates, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Abstract:

Free oligosaccharides are abundant components of mammalian milk and have primary roles as prebiotic compounds, in immune defense, and in brain development. A mass spectrometry-based technique is applied to profile milk oligosaccharides from apes (chimpanzee, gorilla, and siamang), new world monkeys (golden lion tamarin and common marmoset), and an old world monkey (rhesus). The purpose of this study is to evaluate the patterns of primate milk oligosaccharide composition from a phylogenetic perspective to assess the extent to which the compositions of HMOs derives from ancestral primate patterns as opposed to more recent evolutionary events. Milk oligosaccharides were quantitated by nanoflow liquid chromatography on chip-based devices. The relative abundances of fucosylated and sialylated milk oligosaccharides in primates were also determined. For a systematic and comprehensive study of evolutionary patterns of milk oligosaccharides, cluster analysis of primate milk was performed using the chromatographic profile. In general, the oligosaccharides in primate milk, including humans, are more complex and exhibit greater diversity compared to the ones in nonprimate milk. A detailed comparison of the oligosaccharides across evolution revealed nonsequential developmental pattern, that is, that primate milk oligosaccharides do not necessarily cluster according to the primate phylogeny. This report represents the first comprehensive and quantitative effort to profile and elucidate the structures of free milk oligosaccharides so that they can be related to glycan function in different primates.

DOI: 10.1021/pr1009367
Alternate Journal: J. Proteome Res.
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