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 หัวเรื่อง:ไม่มีชื่อไทย (ชื่ออังกฤษ : Humoral Antibody Responses of Rabbits Immunized with Anti-TickVaccine Using SERPIN Recombinant Protein) ผู้เขียน: ไพทูล แก้วหอม,  ดร.ธีระพล ศิรินฤมิตร, รองศาสตราจารย์ , ดร.ศิริรักษ์ จันทครุ, ผู้ช่วยศาสตราจารย์, ดร.สถาพร จิตตปาลพงศ์, ศาสตราจารย์ สื่อสิ่งพิมพ์:pdf AbstractThe objective of this study was to determine the immunogenicity of recombinant serine protease inhibitor (rSERPIN) in rabbits. The rSERPIN protein, expressed in Pichia pastoris, was used to immunize rabbits three times at two- week intervals with a dose of 100 ?g rSERPIN. Dot blot and SDS-PAGE analysis of crude supernatant showed a distinct band of approximately 45 kDa. Western blot analysis also gave a specific band approximately the same size as that of SDS-PAGE. By ELISA, all immunized rabbits generated antibodies against rSERPIN in the first week after immunization, which reached its peak at the seventh week. The antibody titers were analyzed by ANOVA and showed high significance between the immunized group and the control groups (group 1, PBS; and group 2, wild type protein) from the third week after immunization through to the end of the experiment. This result indicated that rSERPIN had a strong immunogenicity and might be the candidate antigen for an anti-tick vaccine. However, it is necessary to perform a clinical trail with targeted animals as natural hosts. |
หัวเรื่อง:ไม่มีชื่อไทย (ชื่ออังกฤษ : Cloning and Characterization of cDNA Encoding a Serine Protease Inhibitor from Salivary Glands of Thai Cattle Tick (Boophilus microplus)) ผู้เขียน:ไพทูล แก้วหอม, ดร.ธีระพล ศิรินฤมิตร, รองศาสตราจารย์, ดร.ศิริรักษ์ จันทครุ, ผู้ช่วยศาสตราจารย์, ดร.สถาพร จิตตปาลพงศ์, ศาสตราจารย์ สื่อสิ่งพิมพ์:pdf AbstractTick salivary gland (TSG) proteins have been an evidence for application as novel tick control agents. The serine protease inhibitors (serpins) secreted from TSG may be used in an anti-tick feeding. In this study, we cloned serpin cDNA from TSG of Boophilus microplus by Reverse Transcription Polymerase Chain Reaction (RT-PCR) and analyzed its nucleotide and deduced amino acid sequences. Our results showed that the 1,200 bp open reading frame of serpins could encode a protein with 399 amino acid residues. By comparison with other serpin available in the GenBank database, the aminoacid sequence, in the reactive center loop (RCL) of the cloned serpin, demonstrated a 95% and 100% identity to those of the B. microplus and Rhiphicephalus appendiculatus, respectively. This is the first report on a cloning of cDNA encoding a serpin derived from B. microplus in Thailand. Based on this result, Thai serpin genes were homologous to the other serpins gene and confirmed a potential use of recombinant Thai serpin as the candidate antigen for vaccine to immunize cattle against B. microplus infestations. |