Abstract
The changes in climate and exposure to heat stress are major concerns for agricultural communities as it affects pollinators like bees. Bees from different taxa play a crucial role in plant pollination, and their exposure to heat stress induces the expression of heat shock proteins (HSPs) to protect their cells. Several studies have analyzed the variations in HSPs expression levels and amino acid sequences. Databases for sequences of HSPs with different molecular weights are currently available. Variations in HSPs expression levels have been noted among individuals belonging to the same or different bee taxa exposed to heat stress. The properties of HSPs could help in understanding these variations. This study utilized bioinformatics and protein analysis tools to investigate the variations in sequences of heat shock proteins 60 (HSP60) and 83 (HSP83) in 18 bee taxa (15 from Family Apidae, 2 from Family Halictidae, and one from Megachilidae). The analysis showed some identical values to bees from genus Apis and Bombus. For HSP60, all bee taxa had high G content (587-602), followed by A (438-444), then C (389-404), and finally T (282-291). For HSP83, all bee taxa had high A content (730-759), followed by G (572-592), then C (406-419), and finally T (415-429). The conserved domains were highly identical in case of HSP60 versus HSP83. The motifs were from one or more protein families with variation among taxa. All proteins showed hydrophilic properties with variable isoelectric points. The study suggested an identical 3-D structure for proteins in all bee taxa. The role of the detected variations in affecting the response of HSPs to stress was discussed. This study paves the way for more investigations on HSPs and encourages the use of bioinformatics and protein analysis tools to explain any observable variations.