Abstract
Venoms of invertebrates contain an enormous diversity of proteins, peptides, and other classes of substances. Insect venoms are characterized by a large interspecific variation resulting in extended lists of venom compounds. The venom composition of several hymenopterans also shows different intraspecific variation. For instance, venom from different honeybee castes, more specifically queens and workers, shows quantitative and qualitative variation, while the environment, like seasonal changes, also proves to be an important factor. The present study aimed at an in-depth analysis of the intraspecific variation in the honeybee venom proteome. In summer workers, the recent list of venom proteins resulted from merging combinatorial peptide ligand library sample pretreatment and targeted tandem mass spectrometry realized with a Fourier transform ion cyclotron resonance mass spectrometer (FT-ICR MS/MS). Now, the same technique was used to determine the venom proteome of queens and winter bees, enabling us to compare it with that of summer bees. In total, 34 putative venom toxins were found, of which two were never described in honeybee venoms before. Venom from winter workers did not contain toxins that were not present in queens or summer workers, while winter worker venom lacked the allergen Api m 12, also known as vitellogenin. Venom from queen bees, on the other hand, was lacking six of the 34 venom toxins compared to worker bees, while it contained two new venom toxins, in particularly serine proteinase stubble and antithrombin-III. Although people are hardly stung by honeybees during winter or by queen bees, these newly identified toxins should be taken into account in the characterization of a putative allergic response against Apis mellifera stings.
Highlights
Hymenopteran venoms are a complex mixture of substances, mainly composed of proteins and peptides, and containing alkaloids, amines, and other small molecules [1]
While this in-depth analysis was performed on venom from worker bees collected during the summer, the present study aimed to examine possible caste and/or seasonal variation in the venom composition of A. mellifera carnica
The combination of the combinatorial peptide ligand library (CPLL) approach with FT-ICR MS/MS used on three different venom samples from honeybees resulted in 35 putative venom toxins, of which three had never been described in honeybee venoms before
Summary
Hymenopteran venoms are a complex mixture of substances, mainly composed of proteins and peptides, and containing alkaloids, amines, and other small molecules [1]. During winter in the temperate zone, the workers face different predators and intruders than during the summer: for example, mice often try to take shelter in a honeybee hive during the winter months, while wasps are not active during winter months This means that the function together with the composition of the venom possibly differs from summer worker venom. The venom proteome of the honeybee A. mellifera was recently investigated by integrating a combinatorial peptide ligand library approach with nanoLC FT-ICR MS/MS [18], resulting in 102 venom proteins and peptides, of which 33 were categorized as putative venom toxins While this in-depth analysis was performed on venom from worker bees collected during the summer, the present study aimed to examine possible caste and/or seasonal variation in the venom composition of A. mellifera carnica. We used similar techniques on venom collected from queens and winter workers and compared the data to previous results
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