Prokaryotic expression and immune analysis of Septin-3 in Haemaphysalis longicornis(Acari:Ixodidae)
To investigate the structure,biological function and immunological properties of Septin-3 protein of Haemaphysalis longicornis,molecular structure of Septin-3 protein was resolved by gene cloning and prokaryotic protein expression,the immune properties were analyzed using the preparation of polyclonal antibodies,ELISA for antibody potency and Western-blot detection,and Septin-3 protein function was validated in conjunction with animal infection experiment.The results showed that the target fragment size of Septin-3 gene was 1 017 bp,and the Septin-3 gene can encode about 338 amino acid residues,and it can express a protein of 38 ku,the antibody potency of the Septin-3 protein was as high as 1∶256 000.The study conducted tick attack experiments on New Zealand white rabbits,compared with the control group,the results showed that H.longicornis,its days of saturation increased by 1.34 d,its weight after saturation decreased by 20.03-24.75 mg,and its saturation rate decreased by 11.04%.The research results suggest that the recombinant Septin-3 protein has excellent immunogenicity and reactivity,and has a certain inhibitory effect on the growth and development of H.longicornis.