Proteomic Analysis of the Royal Jelly and Characterization of the Functions of its Derivation Glands in the Honeybee

Abstract

To identify candidate royal jelly (RJ) proteins that might affect the physiologic status of honeybee colony members, we used shotgun proteomics to comprehensively identify the RJ proteome as well as proteomes of the hypopharyngeal gland (HpG), postcerebral gland (PcG), and thoracic gland (TG), from which RJ proteins are assumed to be derived. We identified a total of 38 nonredundant RJ proteins, including 22 putative secretory proteins and Insulin-like growth factor-binding protein complex acid labile subunit. Among them, 9 proteins were newly identified from RJ. Comparison of the RJ proteome with the HpG, PcG, and TG proteomes revealed that 17 of the 22 putative secretory RJ proteins were derived from some of these glands, suggesting that the RJ proteome is a cocktail of proteins from these three glands. Furthermore, pathway analysis suggested that the HpG proteome represents the molecular basis of the extremely high protein-synthesizing ability, whereas the PcG proteome suggests that the PcG functions as a reservoir for the volatile compounds and a primer pheromone. Finally, to further characterize the possible total RJ proteome, we identified putative secretory proteins in the proteomes of these three glands. This will be useful for predicting novel RJ protein components in future studies.

More than royal food - Major royal jelly protein genes in sexuals and workers of the honeybee Apis mellifera

“…In the recently compiled honeybee protein atlas of Chan et al [49] MRJPs were shown to occur in various organs of the abdomen but not in the thoracic muscle and the thoracic salivary gland (see also [25]). Nevertheless, various MRJPs, except for MRJP4, 6 and 8, were identified in the honeybee’s nerve chord [49] that is crossing the thorax and abdomen [3].…”

“…Already Peiren et al [50,51] showed that both proteins are not constrained to the food glands but also present in bee venom. In fact, MRJP8 has never been identified as component of RJ in A. mellifera and also MRJP9 was only identified in three out of numerous studies on the RJ proteome [20,24,25] alluding to a low amount of the protein in RJ. This is well in line with the previous notion that mrjp1-7 derived from mrjp8 and 9 during honeybee evolution [10].…”

“…All MRJPs, except for MRJP8, have been detected in RJ or the hypopharyngeal glands of A. mellifera [9,16-25]. The genes mrjp1 to 5 have been suggested to be primarily expressed in the hypopharyngeal glands of nurses but not in those of foragers [7,26-31].…”

Therapeutic Properties of Bioactive Compounds from Different Honeybee Products

“…Moreover, it is an exclusive food for adult queens throughout their life (Fujita et al, 2013). The induction of larval development into queen has been ascribed to major royal jelly proteins (MRJPs) and a 57-kDa protein known as royalactin (Kamakura, 2011; Buttstedt et al, 2013), although contrary opinions have been raised against the alleged role of this latter (Buttstedt et al, 2016).…”

Longevity extension of worker honey bees (Apis mellifera) by royal jelly: optimal dose and active ingredient

“…Royal jelly (RJ) is a yellow or pale syrup-like substance which is secreted by the hypopharyngeal and mandibular glands of young honey bees (“nurses”) mainly for feeding the queen larvae and adults (Fujita et al, 2012). Worker destined larvae (younger than 3 days old) will develop into queen if they are fed with RJ in queen cells.…”