客运架空索道线路支架的有限元分析

客运架空索道线路支架的有限元计算是其结构设计的难点和重点，文中就线路支架的结构分析中有线元力学模型的简化，计算工况的确定以及计算方法等进行了讨论。最后给出了分析算例。

客运架空索道系统动力特性分析方法

客运架空索道系统的固有频率与模态是衡量索道系统固有动力特性的重要指标，固有频率的大小直接关系到结构在各种不同的激励条件下是否会发生动力放大效应与共振。文中首先解决索道系统分析中的有限元建模问题，包括典型柔性索道的模型状态，然后利用ANSYS程序的子空间迭代法求出结构最低各阶的特征值与特征向量，并计算出三种工况下的前40阶固有频率与振动模态，为客运架空索道系统的动力特性分析提供有效的计算方法。

客运架空索道线路支架的极限承载力分析

给出了用来分析客运架空索道线路支架极限承载力的一种有效的有限元分析方法，重点讨论使用该方法的具体分析过程，同时给出了编程框图，最后通过实例作了进一步的说明。

Identification, Characterization, and Molecular Application of a Virulence-Associated Autotransporter from a Pathogenic Pseudomonas fluorescens Strain

A gene, pfa1, encoding an autotransporter was cloned from a pathogenic Pseudomonas fluorescens strain, TSS, isolated from diseased fish. The expression of pfa1 is enhanced during infection and is regulated by growth phase and growth conditions. Mutation of pfa1 significantly attenuates the overall bacterial virulence of TSS and impairs the abilities of TSS in biofilm production, interaction with host cells, modulation of host immune responses, and dissemination in host blood. The putative protein encoded by pfa1 is 1,242 amino acids in length and characterized by the presence of three functional domains that are typical for autotransporters. The passenger domain of PfaI contains a putative serine protease (Pap) that exhibits apparent proteolytic activity when expressed in and purified from Escherichia coli as a recombinant protein. Consistent with the important role played by PfaI in bacterial virulence, purified recombinant Pap has a profound cytotoxic effect on cultured fish cells. Enzymatic analysis showed that recombinant Pap is relatively heat stable and has an optimal temperature and pH of 50 degrees C and pH 8.0. The domains of PfaI that are essential to autotransporting activity were localized, and on the basis of this, a PfaI-based autodisplay system (named AT1) was engineered to facilitate the insertion and transport of heterologous proteins. When expressed in E. coli, AT1 was able to deliver an integrated Edwardsiella tarda immunogen (Et18) onto the surface of bacterial cells. Compared to purified recombinant Et18, Et18 displayed by E. coli via AT1 induced significantly enhanced immunoprotection.