Abstract
Small heat shock proteins (sHSPs) are probably the most diverse in structure and function among the various super-families of stress proteins, and they play essential roles in various biological processes. The sweet potato whitefly, Bemisia tabaci (Gennadius), feeds in the phloem, transmits several plant viruses, and is an important pest on cotton, vegetables and ornamentals. In this research, we isolated and characterized three α-crystallin/sHSP family genes (Bthsp19.5, Bthsp19.2, and Bthsp21.3) from Bemisia tabaci. The three cDNAs encoded proteins of 171, 169, and 189 amino acids with calculated molecular weights of 19.5, 19.2, and 21.3 kDa and isoelectric points of 6.1, 6.2, and 6.0, respectively. The deduced amino acid sequences of the three genes showed strong similarity to sHSPs identified in Hemiptera and Thysanoptera insects species. All three sHSPs genes from Bemisia tabaci lacked introns. Quantitative real-time PCR analyses revealed that the three BtsHSPs genes were significantly up-regulated in Bemisia tabaci adults and pupae during high temperature stress (39, 41, 43, and 45 °C) but not in response to cold temperature stress (−6, −8, −10, and −12 °C). The expression levels of Bthsp19.2 and Bthsp21.3 in pupae was higher than adults in response to heat stress, while the expression level of Bthsp19.5 in adults was higher than pupae. In conclusion, this research results show that the sHSP genes of Bemisia tabaci had shown differential expression changes under thermal stress.
Highlights
Heat shock proteins (HSPs) comprise a group of highly-conserved proteins that are widely found in prokaryotes and eukaryotes
HSPs can be divided into HSP100, HSP90, HSP70, HSP60, HSP40 and small heat shock proteins according to their molecular weight and homology (Kim, Kim & Kim, 1998; Sǿrensen, Kristensen & Loeschcke, 2003). sHSPs are the least conserved family of all HSPs and were first identified as a set of low molecular proteins (15–43 kDa) induced after heat shock in Drosophila melanogaster (Tissières, Mitchell & Tracy, 1974). sHSPs exhibit more diversity in sequence, structure, size, and function compared to other types of HSPs
Since insects have a strong ability to adapt to a variety of habitats, it is important to understand the roles of sHSP in invertebrates
Summary
Heat shock proteins (HSPs) comprise a group of highly-conserved proteins that are widely found in prokaryotes and eukaryotes. SHSPs are the least conserved family of all HSPs and were first identified as a set of low molecular proteins (15–43 kDa) induced after heat shock in Drosophila melanogaster (Tissières, Mitchell & Tracy, 1974). SHSPs play important roles in adaptation to hot/cold stress, metamorphosis, normal development, diapause, and the immune response (Parsell & Lindquist, 1993; Jakob & Buchner, 1994; Feder & Hofmann, 1999; Hayward et al, 2005; Song et al, 2006; Huang & Kang, 2007; Rinehart et al, 2007; Gu et al, 2012; Lu et al, 2014; Pan et al, 2017)
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