Volume  Number

previous article

next article

Characterization and functional analysis of small heat shock protein gene HSP19.5 in Bombyx mandarina

Jiaqi Ding^a,†, Enxi Chen^a,†, Ruonan Li^a,†, Mingjun Lin^a, Heying Qian^a,b, Guodong Zhao^a,b,*

 
ABSTRACT:      Heat shock proteins (HSPs) act as molecular chaperones and are widely distributed in all kinds of organisms. In this study, the small heat shock protein HSP19.5 gene was cloned from Bombyx mandarina (Bmm). Its open reading frame (ORF) is 504 bp in length, encoding 167 amino acids with the HSP20 characteristic domain. The relative molecular weight of the encoding protein was 19.5 kD, and the isoelectric point (pI) is 6.54. Multiple comparisons and phylogenetic analyses showed that the insect small heat shock proteins (sHSPs) are highly conservative. BmmHSP19.5 has the closest relationship with BmHSP19.5 of Bombyx mori. The results of real-time quantitative PCR showed that the BmmHSP19.5 was highly expressed in the testis and ovary of the 5th instar larvae. The expression level of BmmHSP19.5 gene was increased in all tested tissues under short-term high/low temperature stress. BmNPV can induce the expression of the BmmHSP19.5 gene in hemolymph and midgut. The expression of BmmHSP19.5 gene was up-regulated in the midgut of larvae under deltamethrin stress. Larval RNA interference of BmmHSP19.5 caused 36.1% insect mortality and reduced the oviposition amount by 34.7%; while the whole cocoon weight, cocoon shell rate, and unfertilized rate showed no significant differences. The results suggested that the BmmHSP19.5 gene might play an important role in the molecular mechanism of response to external stress and development in B. mandarina.

Download PDF

139 Downloads 3985 Views

* Corresponding author, E-mail: sdgdzhao@just.edu.cn

Received 1 Dec 2022, Accepted 24 Aug 2023