Shivachandra Sathish Bhadravati, Yogisharadhya Revanaiah, Kumar Abhinendra, Mohanty Nihar Nalini, Nagaleekar Viswas Konasagara
Clinical Bacteriology Laboratory, Indian Veterinary Research Institute (IVRI), Mukteswar-263138, Nainital, Uttarakhand, India.
National Institute of Veterinary Epidemiology and Disease Informatics (NIVEDI), Bengaluru-560024, Karnataka, India.
Res Vet Sci. 2015 Feb;98:1-6. doi: 10.1016/j.rvsc.2014.11.013. Epub 2014 Dec 9.
Transferrin binding protein A (TbpA), an iron acquisition surface protein that also acts as virulence factor, is widely distributed among strains of Pasteurella multocida. In the present study, a total of seven clones of TbpA fragments (39D to F777; 39D to Q697; 188V to F777; 188V to Q697; 39D to P377; 188V to P377 and 39D to F187) belonging to P. multocida B:2 were constructed, over-expressed and purified as recombinant fusion proteins from Escherichia coli using affinity chromatography. Immunization of mice with rTbpA fragments resulted in a significant (p < 0.05) rise in antigen specific serum total IgG and subtypes (IgG1 and IgG2a) tires. All immunized mice challenged with 8 LD50 of P. multocida B:2 resulted in a variable protective efficacy up to 50%. The study indicated the potential possibilities to incorporate full length TbpA in subunit vaccine formulation composed of synergistic subunit antigens against haemorrhagic septicaemia (HS) in cattle and buffalo.
转铁蛋白结合蛋白A（TbpA）是一种铁摄取表面蛋白，也作为毒力因子，广泛分布于多杀性巴氏杆菌菌株中。在本研究中，构建了属于多杀性巴氏杆菌B:2型的总共7个TbpA片段克隆（39D至F777；39D至Q697；188V至F777；188V至Q697；39D至P377；188V至P377和39D至F187），并使用亲和色谱法从大肠杆菌中作为重组融合蛋白进行过表达和纯化。用重组TbpA片段免疫小鼠导致抗原特异性血清总IgG和亚型（IgG1和IgG2a）滴度显著（p < 0.05）升高。所有用8个半数致死剂量的多杀性巴氏杆菌B:2攻击的免疫小鼠产生了高达50%的不同保护效果。该研究表明在由针对牛和水牛出血性败血症（HS）的协同亚单位抗原组成的亚单位疫苗制剂中纳入全长TbpA的潜在可能性。
