Comprehensive identification of novel proteins and N-glycosylation sites in royal jelly
- Equal contributors
1 Institute of Apicultural Research, Chinese Academy of Agricultural Science, Beijing 100093, China
2 College of Bioengineering, Henan University of Technology, Zhengzhou 450001, China
3 Bioengineering Department, Zhengzhou University, Zhengzhou 450001, China
4 Thermo Fisher Scientific (China) Co., Ltd, Shanghai 200021, China
5 Shanghai AB Sciex Analytical Instrument Trading Co., Ltd, Shanghai 200023, China
BMC Genomics 2014, 15:135 doi:10.1186/1471-2164-15-135Published: 16 February 2014
Royal jelly (RJ) is a proteinaceous secretion produced from the hypopharyngeal and mandibular glands of nurse bees. It plays vital roles in honeybee biology and in the improvement of human health. However, some proteins remain unknown in RJ, and mapping N-glycosylation modification sites on RJ proteins demands further investigation. We used two different liquid chromatography-tandem mass spectrometry techniques, complementary N-glycopeptide enrichment strategies, and bioinformatic approaches to gain a better understanding of novel and glycosylated proteins in RJ.
A total of 25 N-glycosylated proteins, carrying 53 N-glycosylation sites, were identified in RJ proteins, of which 42 N-linked glycosylation sites were mapped as novel on RJ proteins. Most of the glycosylated proteins were related to metabolic activities and health improvement. The 13 newly identified proteins were also mainly associated with metabolic processes and health improvement activities.
Our in-depth, large-scale mapping of novel glycosylation sites represents a crucial step toward systematically revealing the functionality of N-glycosylated RJ proteins, and is potentially useful for producing a protein with desirable pharmacokinetic and biological activity using a genetic engineering approach. The newly-identified proteins significantly extend the proteome coverage of RJ. These findings contribute vital and new knowledge to our understanding of the innate biochemical nature of RJ at both the proteome and glycoproteome levels.