溶血巴斯德氏菌和多杀巴斯德氏菌外膜主要蛋白的分离及部分特性鉴定
Isolation and partial characterization of the major protein of the outer membrane of Pasteurella haemolytica and Pasteurella multocida.
作者信息
Lübke A, Hartmann L, Schröder W, Hellmann E
机构信息
Institut für Mikrobiologie und Tierseuchen, Fachbereich Veterinärmedizin, Freie Universität Berlin, Berlin-Dahlem, Germany.
出版信息
Zentralbl Bakteriol. 1994 Jun;281(1):45-54. doi: 10.1016/s0934-8840(11)80636-5.
The N-terminal amino acid sequence of the 35 kDa (p35) major outer membrane protein (MOMP) of P. multocida shared a strong homology with those of homotrimeric nonspecific porins of gram-negative bacteria. The capacity of outer membrane protein (OMP) preparations of P. multocida to bind to respiratory mucosal surface preparations was inhibited significantly by using a polyclonal anti-p35 antiserum in an adhesion ELISA. Anti-p35 antiserum cross-reacted with a 44 kDa (p44) MOMP of P. haemolytica. N-terminal sequencing of MOMP p44 revealed a homology of 81% with the putative porin MOMP p35 of P. multocida.
多杀性巴氏杆菌35 kDa（p35）主要外膜蛋白（MOMP）的N端氨基酸序列与革兰氏阴性菌同三聚体非特异性孔蛋白的序列具有高度同源性。在黏附ELISA中，使用多克隆抗p35抗血清可显著抑制多杀性巴氏杆菌外膜蛋白（OMP）制剂与呼吸道黏膜表面制剂的结合能力。抗p35抗血清与溶血巴氏杆菌的44 kDa（p44）MOMP发生交叉反应。MOMP p44的N端测序显示，其与多杀性巴氏杆菌推定的孔蛋白MOMP p35的同源性为81%。
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