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Background  The tick  Dermacentor silvarum  Olenev (Acari: Ixodidae) is a vital vector tick species mainly distributed in the north of China and overwinters in the unfed adult stage. The knowledge of the mechanism that underlies its molecular adaptation against cold is limited. In the present study, genes of  hsp70  and  hsp90  cDNA, named  Dshsp70  and  Dshsp90 , and tubulin were cloned and characterized from  D. silvarum , and their functions in cold stress were further evaluated.    Methods  The genome of the heat shock proteins and tubulin of  D. silvarum  were sequenced and analyzed using bioinformatics methods. Each group of 20 ticks were injected in triplicate with  Dshsp90 -,  Dshsp70 -, and tubulin-derived dsRNA, whereas the control group was injected with GFP dsRNA. Then, the total RNA was extracted and cDNA was synthesized and subjected to RT-qPCR. After the confirmation of knockdown, the ticks were incubated for 24 h and were exposed to − 20 °C lethal temperature (LT50), and then the mortality was calculated.    Results  Results indicated that  Dshsp70  and  Dshsp90  contained an open reading frame of 345 and 2190 nucleotides that encoded 114 and 729 amino acid residues, respectively. The transcript  Dshsp70  showed 90% similarity with that identified from  Dermacentor variabilis , whereas  Dshsp90  showed 85% similarity with that identified from  Ixodes scapularis . Multiple sequence alignment indicates that the deduced amino acid sequences of  D. silvarum  Hsp90, Hsp70, and tubulin show very high sequence identity to their corresponding sequences in other species. Hsp90 and Hsp70 display highly conserved and signature amino acid sequences with well-conserved MEEVD motif at the C-terminal in Hsp90 and a variable C-terminal region with a V/IEEVD-motif in Hsp70 that bind to numerous co-chaperones. RNA interference revealed that the mortality of  D. silvarum  was significantly increased after injection of dsRNA of  Dshsp70  ( P  = 0.0298) and tubulin ( P  = 0.0448), whereas no significant increases were observed after the interference of  Dshsp90  ( P  = 0.0709).    Conclusions  The above results suggested that  Dshsp70  and tubulin play an essential role in the low-temperature adaptation of ticks. The results of this study can contribute to the understanding of the survival and acclimatization of overwintering ticks.    Graphical abstractSupplementary Information  The online version contains supplementary material available at 10.1186/s13071-021-05056-y.

Functional implication of heat shock protein 70/90 and tubulin in cold stress of Dermacentor silvarum