3 results match your criteria: "Lanzhou Veterinary Research Institute-Chinese Academy of Agricultural Science[Affiliation]"

Theileria annulata SVSP455 interacts with host HSP60.

Parasit Vectors

August 2022

State Key Laboratory of Veterinary Etiological Biology, Key Laboratory of Veterinary Parasitology of Gansu Province, Lanzhou Veterinary Research Institute-Chinese Academy of Agricultural Science, Xujiaping 1, Lanzhou, Gansu, 730046, People's Republic of China.

Background: Theileria annulata, a transforming parasite, invades bovine B cells, dendritic cells and macrophages, promoting the uncontrolled proliferation of these cells. This protozoan evolved intricate strategies to subvert host cell signaling pathways related to antiapoptotic signaling to enable survival and proliferation within the host cells. However, the molecular mechanisms of the cell transformation induced by T.

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[Establishment of indirect ELISA diagnose based on the VP1 structural protein of foot-and-mouth disease virus (FMDV) in pigs].

Sheng Wu Gong Cheng Xue Bao

September 2007

Key Laboratory of Animal Virology of Ministry of Agriculture, National FMD Reference Laboratory, State Key Laboratory of Veterinary Etiological Biology, Lanzhou Veterinary Research Institute Chinese Academy of Agricultural Science, Lanzhou 730046, China.

The complete gene encoding the structural protein of FMDV(VP1) was subcloned into expression vector pPROex-HT, resulting in the fusion expression plasmid pPROexHT-VP1. After transformed into E. coli BL21(DE3) and induced by IPTG, the fusion protein was expressed in high level.

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[Secreted expression of nonstructural protein gene 3ABC of foot-and-mouth disease virus in Sf9 cells and activity analysis].

Sheng Wu Gong Cheng Xue Bao

May 2007

State Key Laboratory of Veterinary Etiological Biology, Key Laboratory of Animal Virology of Ministry of Agriculture, Lanzhou Veterinary Research Institute Chinese Academy of Agricultural Science, Lanzhou 730046, China.

Entire 3ABC sequence of FMDV containing a 6 x his tag coding sequence at the N-terminal was obtained through PCR amplification using a pair of specific primers, subcloned into shuttle plasmid of pMelBac-B with a melittin secretion signal sequence and finally constructed recombinant plasmid of pMel-3ABC. After co-transfected the recombinant plasmid and linearized Bac-N-Blue DNA into Sf9 insect cell under intermediary agent of the Cellfectin, the result showed that we have already acquired recombinant baculovirus by screen of plaque assay and identification of PCR. Though the recombinant baculovirus infecting the Sf9 cells again, experiments indicated that 3ABC gene could express in insect cells and the expressed protein was secreted in the supernatant of Sf9 cell culture possessing favourable biological activities detected by adopting two methods of SDS-PAGE and Western blot.

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