Characterization of recombinant human lactoferrin N-glycans expressed in the milk of transgenic cows

Autor: Daniela Barile, Annabelle Le Parc, Elizabeth A. Maga, Camille Rouquié, Apichaya Bunyatratchata, Sercan Karav
Přispěvatelé: Karamanos, Nikos K
Rok vydání: 2017
Předmět:
Protein Structure Comparison
0301 basic medicine
Glycosylation
Glycobiology
Mannose
lcsh:Medicine
Gene Expression
Centrifugation
Biochemistry
Fats
Animals
Genetically Modified
chemistry.chemical_compound
Casein
Gene expression
Macromolecular Structure Analysis
Cluster Analysis
Post-Translational Modification
lcsh:Science
Fucosylation
Mammals
chemistry.chemical_classification
Multidisciplinary
biology
Organic Compounds
Lactoferrin
Monosaccharides
Lipids
Recombinant Proteins
Chemistry
Separation Processes
Milk
Physical Sciences
Vertebrates
Research Article
Protein Structure
Glycan
General Science & Technology
Carbohydrates
Genetically Modified
Research and Analysis Methods
Microbiology
03 medical and health sciences
Bovines
Polysaccharides
Animals
Humans
Molecular Biology
030102 biochemistry & molecular biology
Organic Chemistry
lcsh:R
Chemical Compounds
Organisms
Biology and Life Sciences
Proteins
Phosphoproteins
carbohydrates (lipids)
030104 developmental biology
chemistry
Amniotes
biology.protein
lcsh:Q
Cattle
Glycoprotein
Zdroj: PloS one, vol 12, iss 2
PLoS ONE, Vol 12, Iss 2, p e0171477 (2017)
PLoS ONE
Popis: Lactoferrin (LF) is one of the most abundant bioactive glycoproteins in human milk. Glycans attached through N-glycosidic bonds may contribute to Lactoferrin functional activities. In contrast, LF is present in trace amounts in bovine milk. Efforts to increase LF concentration in bovine milk led to alternative approaches using transgenic cows to express human lactoferrin (hLF). This study investigated and compared N-glycans in recombinant human lactoferrin (rhLF), bovine lactoferrin (bLF) and human lactoferrin by Nano-LC-Chip-Q-TOF Mass Spectrometry. The results revealed a high diversity of N-glycan structures, including fucosylated and sialylated complex glycans that may contribute additional bioactivities. rhLF, bLF and hLF had 23, 27 and 18 N-glycans respectively with 8 N-glycan in common overall. rhLF shared 16 N-glycan with bLF and 9 N-glycan with hLF while bLF shared 10 N-glycan with hLF. Based on the relative abundances of N-glycan types, rhLF and hLF appeared to contain mostly neutral complex/hybrid N-glycans (81% and 52% of the total respectively) whereas bLF was characterized by high mannose glycans (65%). Interestingly, the majority of hLF N-glycans were fucosylated (88%), whereas bLF and rhLF had only 9% and 20% fucosylation, respectively. Overall, this study suggests that rhLF N-glycans share more similarities to bLF than hLF.
Databáze: OpenAIRE
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