McNamara P J, Cuevas W A, Songer J G
Department of Veterinary Science, University of Arizona, Tucson 85721, USA.
Gene. 1995 Apr 14;156(1):113-8. doi: 10.1016/0378-1119(95)00002-n.
The genes encoding toxic phospholipases D (PLD) from Corynebacterium pseudotuberculosis (Cp)biovar equi and C. ulcerans (Cu) have been cloned and sequenced. The deduced proteins are 307 amino acids (aa) in length and include a putative signal sequences of 26-aa. A molecular mass of 31.2 and 31.0 kDa and pI values of 8.84 and 6.73 are predicted for the secreted (mature) proteins from Cp and Cu, respectively. Comparison of the deduced primary structure of the two proteins to those of the PLD produced by Cp biovar ovis and Arcanobacterium haemolyticum (Ah) revealed that the four enzymes share 64-97% identity. The aa sequences of this group of proteins were unique when compared to the sequences of other phospholipases in GenBank and were found to share only small regions of homology with other proteins, including two conserved domains of glyceraldehyde-3-phosphate dehydrogenase (G3PD). The similarity of PLD from Cp biovar equi, Cu and Ah to the PLD of Cp biovar ovis suggests that these enzymes may act as virulence determinants.
来自马伪结核棒状杆菌（Cp）生物变种马型和溃疡棒状杆菌（Cu）的编码毒性磷脂酶D（PLD）的基因已被克隆和测序。推导的蛋白质长度为307个氨基酸（aa），并包括一个26个氨基酸的假定信号序列。预测来自Cp和Cu的分泌型（成熟）蛋白质的分子量分别为31.2和31.0 kDa，pI值分别为8.84和6.73。将这两种蛋白质推导的一级结构与Cp生物变种绵羊型和溶血隐秘杆菌（Ah）产生的PLD的一级结构进行比较，发现这四种酶具有64 - 97%的同一性。与GenBank中其他磷脂酶的序列相比，这组蛋白质的氨基酸序列是独特的，并且发现它们与其他蛋白质仅共享小的同源区域，包括甘油醛-3-磷酸脱氢酶（G3PD）的两个保守结构域。来自Cp生物变种马型、Cu和Ah的PLD与Cp生物变种绵羊型的PLD的相似性表明这些酶可能作为毒力决定因素。
