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Dynamic Temporal Variations in Bovine Lactoferrin Glycan Structures.

Rivca L Valk-Weeber¹, Talitha Eshuis-de Ruiter², Lubbert Dijkhuizen¹

¹Microbial Physiology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB) , University of Groningen , Nijenborgh 7 , 9747 AG Groningen , The Netherlands.

Journal of Agricultural and Food Chemistry

|December 13, 2019

Summary

Bovine lactoferrin glycosylation changes rapidly in early lactation but stabilizes within a month. Predry period milk lactoferrin glycosylation resembles colostrum, offering insights into its function.

Keywords:

(α2,3)-sialic acid N-glycosylation colostrum lactoferrin milk

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Area of Science:

Biochemistry
Glycobiology
Animal Science

Background:

Glycosylation of bovine lactoferrin is known to vary.
A comprehensive understanding of these glycosylation changes throughout lactation, including the predry period, is currently lacking.

Purpose of the Study:

To provide a detailed structural overview of bovine lactoferrin glycosylation changes throughout the entire lactation cycle.
To compare glycosylation profiles between colostrum, mature milk, and predry period milk.
To analyze variations across different cows and commercial samples.

Main Methods:

High-throughput analysis of glycoprofiles from lactoferrin isolated from colostrum, mature, and predry period milk.
Analysis over two lactation cycles in 8 cows of diverse genetic backgrounds.
Comparison with commercial bovine lactoferrin samples.

Main Results:

Dynamic changes in lactoferrin glycosylation were observed within the first 72 hours of lactation.
Shifts in oligomannose distribution and levels of sialylated and fucosylated glycans were noted.
Some cows exhibited (α2,3)-linked sialic acid in early colostrum samples.
Glycosylation profiles stabilized approximately one month post-delivery and were consistent across cows.
Predry period lactoferrin glycosylation profiles were similar to those in colostrum.
Commercial lactoferrin glycosylation profiles remained stable throughout the year.

Conclusions:

Bovine lactoferrin glycosylation undergoes significant dynamic changes in early lactation, stabilizing thereafter.
Predry period lactoferrin glycosylation mirrors that of colostrum.
Understanding these glycosylation variations can aid in elucidating lactoferrin's functions and regulatory mechanisms.