Simón M, Mathes A, Blanch A, Engelhardt H
Department of Microbiology, University of Barcelona, Spain.
J Bacteriol. 1996 Jul;178(14):4182-8. doi: 10.1128/jb.178.14.4182-4188.1996.
The outer membranes of the 10 serovars of Vibrio anguillarum showed a common major protein with a size of around 40 kDa. Antibodies against the major outer membrane protein (MOMP) of V. anguillarum AO18 (serovar O1) cross-reacted with the MOMPs of all the other serovars but not with the outer membrane proteins of Escherichia coli. The MOMP of V. anguillarum serovar O1 was isolated, reconstituted to two-dimensional crystals, and structurally characterized by electron microscopy and image processing. The unit cell structure of the crystalline MOMP, as well as the secondary structure composition of the protein with a high amount of beta-structure, is strongly reminiscent of that of bacterial porins. The functional properties of the pores were investigated by conductance measurements with the MOMP reconstituted in planar lipid membranes. The V. anguillarum MOMP is characterized by a relatively weak cation selectivity and a moderate surface charge, and it shows voltage-dependent conductance effects. The MOMP is functionally similar to OmpF from E. coli, and it can be classified as a general diffusion porin.
鳗弧菌10个血清型的外膜显示出一种大小约为40 kDa的共同主要蛋白。针对鳗弧菌AO18（血清型O1）主要外膜蛋白（MOMP）的抗体与所有其他血清型的MOMP发生交叉反应，但不与大肠杆菌的外膜蛋白发生反应。分离出鳗弧菌血清型O1的MOMP，将其重构成二维晶体，并通过电子显微镜和图像处理对其结构进行表征。晶体MOMP的晶胞结构以及具有大量β结构的蛋白质二级结构组成，与细菌孔蛋白的结构非常相似。通过在平面脂质膜中重构MOMP进行电导测量，研究了孔的功能特性。鳗弧菌MOMP的特点是阳离子选择性相对较弱，表面电荷适中，并表现出电压依赖性电导效应。该MOMP在功能上与大肠杆菌的OmpF相似，可归类为一般扩散孔蛋白。
