Lee Jeongmin, Kim Young Bong, Kwon Moosik
Institute of Life Science and Technology, Sungkyunkwan University, Suwon 440-746, Republic of Korea.
J Microbiol. 2007 Apr;45(2):179-84.
Pasteurella multocida, a Gram-negative facultative anaerobic bacterium, is a causative animal pathogen in porcine atrophic rhinitis and avian fowl cholera. For the development of recombinant subunit vaccine against P. multocida, we cloned and analyzed the gene for outer membrane protein H (ompH) from a native strain of Pasteurella multocida in Korea. The OmpH had significant similarity in both primary and secondary structure with those of other serotypes. The full-length, and three short fragments of ompH were expressed in E. coli and the recombinant OmpH proteins were purified, respectively. The recombinant OmpH proteins were antigenic and detectable with antisera produced by either immunization of commercial vaccine for respiratory disease or formalin-killed cell. Antibodies raised against the full-length OmpH provided strong protection against P. multocida, however, three short fragments of recombinant OmpHs, respectively, showed slightly lower protection in mice challenge. The recombinant OmpH might be a useful vaccine candidate antigen for P. multocida.
多杀性巴氏杆菌是一种革兰氏阴性兼性厌氧菌,是猪萎缩性鼻炎和禽霍乱的致病性动物病原菌。为了开发针对多杀性巴氏杆菌的重组亚单位疫苗,我们从韩国一株多杀性巴氏杆菌天然菌株中克隆并分析了外膜蛋白H(OmpH)基因。OmpH在一级和二级结构上与其他血清型的OmpH具有显著相似性。ompH的全长及三个短片段在大肠杆菌中表达,并分别纯化了重组OmpH蛋白。重组OmpH蛋白具有抗原性,可被呼吸道疾病商业疫苗免疫或福尔马林灭活细胞产生的抗血清检测到。针对全长OmpH产生的抗体对多杀性巴氏杆菌提供了强大的保护作用,然而,重组OmpH的三个短片段在小鼠攻毒实验中显示出略低的保护作用。重组OmpH可能是一种有用的多杀性巴氏杆菌疫苗候选抗原。