Construction and identification of the recombinant plasmid p. ET3. 0a- Eg. A3. 1- Eg. Echinococcus.. The total RNA was extracted from the protoscoleces of Echinococcus granulosus (E. The complementary DNA (c. DNA) encoding the Eg. A3. 1 antigen was amplified via quantitative real- time polymerase chain reaction (q. PCR). The recombinant plasmid p. ET3. 0a- Eg. A3. 1 was used as a carrier and was connected with the Eg. The recombinant plasmid p. ET3. 0a- Eg. A3. 1- Eg. The pET-27b(+) vector (Cat. 69863-3) carries an N-terminal pelB signal sequence for poten-tial periplasmic localization. Unique sites are shown on the circle map. Vector: Map: Genbank file: PDF: Linear map: pMCentr2: pMCentr2.gb: pMCentr2.pdf: pMCentr3: pMCentr3.gb: pMCentr3.pdf. The cloning/expression region of the coding strand transcribed by T7 RNA poly-. Plasmid pET28a-LIC from Dr. Generated by Addgene from full sequence supplied by. SGC Oxford seeks to generate high quality reagents to accelerate the discovery of new medicines and place them into the public domain without restriction. Initiation of translation in bacteria by a structured eukaryotic IRES RNA. Eg. A3. 1- Eg. 95 was detected using sodium dodecyl sulfate- polyacrylamide gel electrophoresis (SDS- PAGE). The positive clone was the empty recombinant vector. The recombinant protein p. ET3. 0a- Eg. A3. 1- Eg. Da, and the expressed product accounted for approximately 2. We successfully constructed the recombinant plasmid p. ET3. 0a- Eg. A3. 1- Eg. Eg. A3. 1- Eg. 95. The results may be the foundation of research on its immunogenicity in the future. Keywords: Echinococcus granulosus, Eg. A3. 1- Eg. 95 antigen gene, prokaryotic expression plasmid. Introduction. Echinococcus granulosus (E. China is one of the countries with a high rate of E. The main treatment of hydatid disease is surgery supplemented by drug treatment (4). However, the surgery is harmful to the human body, whereas a molecular vaccine is an ideal method to prevent alveolar echinococcosis (5,6). If the rostellum of the protoscolex entering the host intestine is not removed or absorbed by the intestinal mucosa, the worms are excreted out of the host (7). Fraize et al(8) built a model in vitro to evaluate the T cell response of the final host to the protoscolex and Eg antigen. The study observed that the protoscolex did not cause changes in cytokine production, which was consistent with the Eg metacestode showing no or little immunogenicity within the final host (9). This was consistent with Vuitton’s (1. Eg. A3. 1 antigen may increase interleukin- 1. IL- 1. 0) and IL- 1. IL- 1. 2 may promote the production of interferon- . The Eg. 95 recombinant protein vaccine immunized the intermediate host (sheep), and 8. Furthermore, Ding et al(1. Liu et al(1. 3) demonstrated that the pc. DNA3- Eg. 95 gene vaccine and the Eg. Alvite and Esteves (1. Eg. A3. 1 antigen may be correlated with the sucking function of the scolex in each growth stage of the adult. This antigen is located at multiple sites on the parasite protoscolex and adult worms. Saboulard et al(1. Eg. A3. 1 protein exhibited a high level of antigenicity and immunogenicity. Eg. A3. 1 was also demonstrated to show the strongest immunoreactivity in a different study (1. It is possible to develop a protein composition vaccine; thus, the Eg. Eg. A3. 1 antigens were selected as vaccine candidates and recombinant antigens, and were predicted to enhance the immune response and play a significant role in immunogenicity. The aim was to provide further experimental foundation for a multivalent Eg. A3. 1- Eg. 95 vaccine. Materials and methods. E. The mice infected with Echinococcus granulosus were supplied by Animal Center of Xinjiang Medical University. The cloning plasmid p. UCm- T was purchased from MBI, Inc. The prokaryotic expression plasmid p. ET3. 0a and the recombinant plasmids p. ET2. 8a- Eg. 95 and p. ET3. 0a- Eg. A3. 1 were obtained from Xinjiang Laboratory of Hydatid Fundamental Medicine, First Affiliated Hospital of Xinjiang Medical University (Urumqi, China), while the Escherichia coli (E. All patients and healthy controls signed the informed consent, the experimental design was approved by the ethical committee (Approval Number: 2. All experiments using mice were performed in accordance with protocols approved by Xinjiang Medical University Animal Ethics Committee according to China Guidelines on Animals Care (No. A- 2. 01. 00. 92. Main reagents and formula. TRIzol. A c. DNA synthesis kit (MBI, Inc.) was used to amplify the AMV reverse transcriptase, while Taq DNA polymerase and p. UCm- T (MBI, Inc.) were used to amplify the genes. Prestained protein marker and a Bicinchoninic acid (BCA) Protein Quantitation kit from Bio. Teke Corp. Goat anti- rabbit immunoglobulin G (Ig. G)- horseradish peroxidase (HRP) and goat anti- human Ig. G- HRP were obtained from Sigma (St. In addition, a UNIQ- 1. Column Mini Plasmid kit and UNIQ- 1. Column DNA Gel Extraction kit (Bio- Rad Laboratories (Shanghai) Co., Ltd., Shanghai, China) were used. Primer design and synthesis. According to the Echinococcus Eg. A3. 1 gene sequence (Gen. Bank Accession: AF0. Eg. 95 gene sequence (Gen. Bank Accession: X9. Prokaryotic expression plasmid p. ET3. 0a restriction map, we designed two pairs of primers with the software. Two pairs of primers were designed with the DNAman software (Lynnon Corp., Pointe- Claire, QC, Canada), and synthesized by Sangon (Shanghai, China). The primers were as follows: Eg. A3. 1 forward primer P1, 5. A transcription kit was used to amplify all m. RNA into complementary DNA (c. DNA). Cloning and identification of the Eg. A3. 1- and Eg. 95- encoding genes. The c. DNA in adult specimens was used as a template to clone the Eg. A3. 1 target fragment using reverse transcription- polymerase chain reaction (RT- PCR). The c. DNA in the protoscolex specimens was used as a template for the Eg. Eg. 95 target fragment with an RT- PCR kit, according to the manufacturer’s instructions (Invitrogen Life Technologies). Construction of the prokaryotic expression plasmid p. ET3. 0a- Eg. A3. 1- Eg. Plasmid construction is shown schematically in Fig. Genetic engineering and cloning were used to channel the Eg. ET3. 0a- Eg. A3. 1 to build the recombinant plasmid p. ET3. 0a- Eg. A3. 1- Eg. The recombinant plasmids p. ET3. 0a- Eg. A3. 1 and p. UCm- T/Eg. 95 were extracted. The double digestion of the recombinant plasmid p. ET3. 0a- Eg. A3. 1 consisted of a total reaction volume of 1. The double digestion of the recombinant plasmid p. UCm- T/Eg. 95 consisted of a total reaction volume of 2. The digestions were performed at 3. Following separation by 1. Eg. 95 and a large fragment of linear p. ET3. 0a were recycled by a DNA gel extraction kit. The DNA was then dissolved in dd. H2. O. Diagram of the constructed recombinant plasmid p. ET3. 0a- Eg. A3. 1- Eg. The two digested plasmids were linked. Subsequently, the recombinant plasmid p. ET3. 0a- Eg. A3. 1- Eg. P1 and P4 were amplified (annealing temperature 5. The restriction enzyme digestion was used to confirm the amplified DNA and affirm that the sites were correct (Bam. HI, Not. I digestion). The recombinant plasmid p. ET3. 0a- Eg. A3. 1- Eg. The measurement analysis was performed with a kit purchased from Sangon. Expression and purification of the recombinant protein. Recombinant Eg. 95 protein The prokaryotic expression plasmid p. ET2. 8a- Eg. 95 was transformed into E. The A6. 00 absorbance value was ~0. Protein expression was induced with the final concentration of 0. The samples were collected at different induction times (0, 1, 2, 3, 4, 5 and 6 h) and bacteria were obtained. The samples were then placed into a boiling water bath for 5 min and 1. SDS- PAGE) was performed to assess expression. Recombinant Eg. A3. Eg. A3. 1- Eg. 95 protein The recombinant plasmid p. ET3. 0a- Eg. A3. 1- Eg. Cultured and expression- induced thalli were collected at 0, 2, 4 and 6 h using SDS- PAGE (p. ET3. 0a- Eg. A3. 1- Eg. SDS- PAGE Mini Protein IH using a miniature protein electrophoresis system). The recombinant protein was purified by a His column using chromatographic purification of the target protein. Protease inhibitor (Ben 1. The cells were lysed by ice bath sonication and centrifugation, and the purified recombinant p. ET2. 8a- Eg. 95 protein was obtained by His- Bind Resin, SDS- PAGE electrophoresis analysis. Recombinant protein detection The separation gel was retained for transformation to a membrane, with a constant current of 1. A at 4. The gel was sealed and agitated at 3. The primary antibody was added and incubated at 3. The nitrocellulose membrane was placed in the diluted secondary antibody, with stable shaking at 3. Dog serum infected with E. The density of the RNA bands was measured by the absorption at wavelengths of 2. Nano. Drop 2. 00. Thermo Scientific, Waltham, MA, USA). The A2. 60/A2. 80 ratio for protoscolex RNA was 1. The total RNA extraction was successful and the purity and concentration of RNA were high. Agarose gel electrophoresis result of the E. The m. RNA levels were high. The PCR products were analyzed using 1. Fig. 3), which were consistent with the expected results. The negative control without template showed no specific band, demonstrating that the amplification of the Eg. A3. 1 and Eg. 95 gene fragments was successful. Quantitative real- time polymerase chain reaction (q. PCR) products of Eg. A3. 1and Eg. 95 gene. M, DL2. 00. 0.. Eg. A3. 1 and Eg. 95 antigen gene sequences. A comparison between the recorded or registered Eg. A3. 1 antigen gene sequence in Gen. Bank (accession no. AF0. 67. 80. 7) and the cloning Eg. A3. 1 antigen- specific sequence showed that the two sequences were identical. The cloned Eg. 95 antigen gene sequence was also consistent with the Eg. Gen. Bank (accession no. X9. 09. 28). Construction of the prokaryotic expression plasmid p. ET3. 0a- Eg. A3. 1- Eg. Identification of enzyme digestion and amplification Eg. ET3. 0a- Eg. A3. 1 fragment at 5. Eg. 95 fragment and p. ET3. 0a- Eg. A3. 1 fragment were recycled by electrophoresis and connected by T4 DNA ligase, directionally cloned p. ET3. 0a- Eg. A3. 1- Eg. The 1. 03. 8 bp Eg. A3. 1- Eg. 95 DNA fragment was obtained by either PCR method or recombinant plasmid p. ET3. 0a- Eg. A3. 1- Eg. Bam. HI and Not. I, consistent with expected products (Fig. Identification of p. ET3. 0a- Eg. A3. 1- Eg. PCR) and digestion with restriction enzymes. M1: DL2. 00. 0 DNA Marker; Lanes 1 and 2: PCR products of Eg. A3. 1- Eg. 95; Lanes 3 and 4: recombinant plasmid digested by Bam. HI/.. Sequencing analysis The digested identified recombinant plasmid broth (1 ml) was sent to Sangon for sequencing. Due to the connected fragment length of 1,0. The cloned Eg. A3. Eg. 95 antigen gene was identical to the Eg.
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