Abstract
Honeybee caste development is nutritionally regulated by royal jelly (RJ). Major royal jelly protein 1 (MRJP1), the most abundant glycoprotein among soluble royal jelly proteins, plays pivotal roles in honeybee nutrition and larvae development, and exhibits broad pharmacological activities in humans. However, its structure has long remained unknown. Herein, we identify and report a 16-molecule architecture of native MRJP1 oligomer containing four MRJP1, four apisimin, and eight unanticipated 24-methylenecholesterol molecules at 2.65 Å resolution. MRJP1 has a unique six-bladed β-propeller fold with three disulfide bonds, and it interacts with apisimin mainly by hydrophobic interaction. Every four 24-methylenecholesterol molecules are packaged by two MRJP1 and two apisimin molecules. This assembly dimerizes to form an H-shaped MRJP14-apisimin4-24-methylenecholesterol8 complex via apisimin in a conserved and pH-dependent fashion. Our findings offer a structural basis for understanding the pharmacological effects of MRJPs and 24-methylenecholesterol, and provide insights into their unique physiological roles in bees.
Highlights
Honeybee caste development is nutritionally regulated by royal jelly (RJ)
Our findings provide a structural basis for a better understanding of the unique physiological roles of MRJP family proteins and 24-methylenecholesterol in bees and their pharmacological effects in humans
Previous studies indicated that Major royal jelly protein 1 (MRJP1) exhibits a relatively high degree of disorder[32]
Summary
Major royal jelly protein 1 (MRJP1), the most abundant glycoprotein among soluble royal jelly proteins, plays pivotal roles in honeybee nutrition and larvae development, and exhibits broad pharmacological activities in humans. Our findings offer a structural basis for understanding the pharmacological effects of MRJPs and 24-methylenecholesterol, and provide insights into their unique physiological roles in bees. MRJP1 is the most important and abundant glycoprotein in RJ and in bee bread, accounting for 48% of water-soluble RJ proteins[1], and is the most prominent colony-specific honeybee protein[9]. Our findings provide a structural basis for a better understanding of the unique physiological roles of MRJP family proteins and 24-methylenecholesterol in bees and their pharmacological effects in humans
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