Bijlsma Isaac G W, Dijk Linda van, Kusters Johannes G, Gaastra Wim
Department of Bacteriology, Institute of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, University of Utrecht, Yalelaan 1, PO Box 80. 165, 3508 TD Utrecht, The Netherlands.
Microbiology (Reading). 1995 Jun;141 ( Pt 6):1349-1357. doi: 10.1099/13500872-141-6-1349.
Proteus mirabilis strains were isolated from dogs with urinary tract infection (UTI) and fimbriae were prepared from two strains. The N-terminal amino acid sequences of the major fimbrial subunits were determined and both sequences appeared identical to the N-terminal amino acid sequence of a urinary cell adhesin (UCA) (Wray, S. K., Hull, S. I., Cook, R. G., Barrish, J. & Hull, R. A., 1986, Infect Immun 54, 43-49). The genes of two different major fimbrial subunits were cloned using oligonucleotide probes that were designed on the basis of the N-terminal UCA sequence. Nucleotide sequencing revealed the complete ucaA gene of 540 bp (from strain IVB247) encoding a polypeptide of 180 amino acids, including a 22 amino acid signal sequence peptide, and the pmpA (P. mirabilis P-like pili) gene of 549 bp (from strain IVB219) encoding a polypeptide of 183 amino acids, including a 23 amino acid signal sequence. Hybridization experiments gave clear indications of the presence of both kinds of fimbriae in many UTI-related canine P. mirabilis isolates. However, the presence of these fimbriae could not be demonstrated in P. vulgaris or other Proteus-related species. Database analysis of amino acid sequences of major subunit proteins revealed that the UcaA protein shares about 56% amino acid identity with the F17A and F111A major fimbrial subunits from bovine enterotoxigenic Escherichia coli. In turn, the PmpA protein more closely resembled the pyelonephritis-associated pili (Pap)-like major subunit protein from UTI-related E. coli. The evolutionary relationship of UcaA, PmpA and various other fimbrial subunit proteins is presented in a phylogenetic tree.
奇异变形杆菌菌株从患有尿路感染（UTI）的犬类中分离得到，从两株菌株制备了菌毛。测定了主要菌毛亚基的N端氨基酸序列，两个序列均与尿细胞粘附素（UCA）的N端氨基酸序列相同（Wray, S. K., Hull, S. I., Cook, R. G., Barrish, J. & Hull, R. A., 1986, Infect Immun 54, 43 - 49）。使用基于N端UCA序列设计的寡核苷酸探针克隆了两种不同主要菌毛亚基的基因。核苷酸测序揭示了540 bp的完整ucaA基因（来自IVB247菌株），编码180个氨基酸的多肽，包括一个22个氨基酸的信号序列肽，以及549 bp的pmpA（奇异变形杆菌P样菌毛）基因（来自IVB219菌株），编码183个氨基酸的多肽，包括一个23个氨基酸的信号序列。杂交实验明确表明许多与UTI相关的犬奇异变形杆菌分离株中存在这两种菌毛。然而，在普通变形杆菌或其他变形杆菌相关物种中未证实这些菌毛的存在。主要亚基蛋白氨基酸序列的数据库分析表明，UcaA蛋白与牛产肠毒素大肠杆菌的F17A和F111A主要菌毛亚基具有约56%的氨基酸同一性。反过来，PmpA蛋白更类似于与UTI相关的大肠杆菌的肾盂肾炎相关菌毛（Pap）样主要亚基蛋白。在系统发育树中展示了UcaA、PmpA和各种其他菌毛亚基蛋白的进化关系。
