| 华东地区部分猪源大肠杆菌K88黏附素的生物学特性 |
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| 引用本文： | 陈祥,高崧,王雷,李文杰,曹传闺,焦新安,刘秀梵.华东地区部分猪源大肠杆菌K88黏附素的生物学特性[J].中国兽医学报,2005,25(5):474-477. |
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| 作者姓名： | 陈祥 高崧 王雷 李文杰 曹传闺 焦新安 刘秀梵 |
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| 作者单位： | 扬州大学,农业部畜禽传染病学重点开放实验室,江苏,扬州,225009 |
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| 基金项目： | 国家“863计划”资助项目（2003AA222141）;江苏省自然科学基金资助项目（BK2001148） |
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| 摘 要： | 近年来，从华东地区患腹泻仔猪中分离到一些表达K88菌毛的大肠杆菌，这些菌株只与K88a因子单抗反应，而不与b、c、d因子单抗反应。通过K88常规血清交叉吸收试验、SDS-PAGE、Western印迹，表明这些菌株不仅与K88ac参考菌株C83907制备的c因子血清反应，而且与以分离株SEC586制备且经K88ab、K88ac、K88ad参考菌株吸收后的血清也反应。对分离株SEC586、SEC464的K88主要亚单位结构基因faeG的克隆、测序，发现该基因由846对核苷酸组成，编码菌毛主要亚单位的262个氨基酸及21个氨基酸的信号肽，比国外报道的K88ac FaeG亚单位（263个氨基酸）少了1个氨基酸，比K88ab、K88ad（265个氨基酸）少了3个氨基酸。SEC586、SEC464菌株的FaeG亚单位氨基酸序列的同源性为97．7％，它们与K88ac的同源性为94．7％和96．2％；与K88ab的同源性为90．1％和91．2％；与K88ad的同源性为87．0％和88，6％。结果表明，新分离的K88ac大肠杆菌黏附素主要亚单位已发生了部分变异。
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| 关 键 词： | 大肠杆菌 K88黏附素 单克隆抗体 faeG |
| 文章编号： | 1005-4545(2005)05-0474-04 |
| 收稿时间： | 2004-04-29 |
| 修稿时间： | 2004年4月29日 |
Identification of K88ac Fimbrial Antigen of Enterotoxigenic Escherichia coli Isolated from Diarrhoeal Piglets in Eastern of China |
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| CHEN Xiang,GAO Song,WANG Lei,LI Wen-jie,CAO Chuan-gui,JIAO Xin-an,LIU Xiu-fan.Identification of K88ac Fimbrial Antigen of Enterotoxigenic Escherichia coli Isolated from Diarrhoeal Piglets in Eastern of China[J].Chinese Journal of Veterinary Science,2005,25(5):474-477. |
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| Authors: | CHEN Xiang GAO Song WANG Lei LI Wen-jie CAO Chuan-gui JIAO Xin-an LIU Xiu-fan |
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| Institution: | CHEN Xiang,GAO Song*,WANG Lei,LI Wen-jie,CAO Chuan-gui,JIAO Xin-an,LIU Xiu-fan |
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| Abstract: | Some E. coli strains from newborn piglets with diarrhoea were isolated in the eastern regions of China during 2000 to 2003. They reacted with K88-a specific monoclonal antibody while not with K88-b,c,d specific monoclonal antibodies in the slide agglutination test. These isolates were identified with K88ac variant by cross-absorbed rabbit antisera to K88ac fimbria. The apparent molecular weight of K88ac antigens purified from these isolates was about 26 000 in SDS-PAGE, and experienced a positive reaction with the rabbit antisera absorbed with K88ac reference strain in Western blot. The faeG genes were amplified from the genomic DNA of these isolates by PCR. The PCR product of faeG was cloned into pGEM-T vector. Alignment analysis of major FaeG subunits of the K88ac fimbria of these isolates showed some differences in amino acid composition as compared with those of K88ac reference strains, implying that the antigenic differences between these isolates and reference strains may be owing to the mutation of major subunits of the fimbria. Comparison of the sequences of amino acids of the major units showed that the percent identity was 97.7 % between isolate SEC586 and isolate SEC464 in amino acid sequences of major subunit FaeG, and 90. 1% and 91. 2% comparing with K88ab reference strains, 94. 7% and 96. 2% with K88ac reference strains, 87.0% and 88.6% with K88ad reference strains, respectively. These results revealed that K88ac fimbrial antigens of these ETEC isolates experienced some variations as compared with those of K88ac reference strains. |
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| Keywords: | Escherichia coil K88ac fimbria monoclonal antibody faeG |
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