跳到主要內容

臺灣博碩士論文加值系統

(3.239.4.127) 您好!臺灣時間:2022/08/20 08:05
字體大小: 字級放大   字級縮小   預設字形  
回查詢結果 :::

詳目顯示

: 
twitterline
研究生:陳欣欣
論文名稱:D型巴氏桿菌毒素與大腸桿菌忌熱性腸毒素之基因融合及其分子選殖之研究
論文名稱(外文):Studies on the molecular cloning of type D pasteurella multocida toxin (PMT) fused to heat-labile enterotoxin derived from enterotoxigenic escherichia coli
指導教授:張甘楠
學位類別:碩士
校院名稱:國立屏東科技大學
系所名稱:獸醫學系
學門:獸醫學門
學類:獸醫學類
論文種類:學術論文
論文出版年:2002
畢業學年度:90
語文別:中文
論文頁數:114
中文關鍵詞:D型巴氏桿菌毒素
相關次數:
  • 被引用被引用:0
  • 點閱點閱:183
  • 評分評分:
  • 下載下載:37
  • 收藏至我的研究室書目清單書目收藏:0
中文摘要
本試驗旨在研究D型巴氏桿菌毒素(Pasteurella multocida type D toxin,PMT)基因(tox A),除了對此基因之產物加以定性,並進一步分別求證PMT之毒性及其免疫性是座落在5’端或3’端?PMT毒素基因全長為3.8 kb,其分子量約為143 kDa,惟全段3.8 kb太長,因此,以基因刪除(Gene deletion)方法將全段PMT 3.8 kb分為5’端deletion (Δ5’)及3’端deletion (Δ3’)等兩段進行選殖及大量表現及純化其GST融合蛋白,共選殖有1.5 kbΔ3’ clone 1521(83 kDa)、2.3 kbΔ5’ clone 23XL-17(112kDa) 及連結LT clone 23LTBXL-20(126 kDa)等基因片段,與取自Pasteurella multocida type D 所抽取之PMT(143 kDa)分別進行天竺鼠皮膚毒性試驗結果獲知源自Pasteurella multocida之PMT(143 kDa)及Δ3’ clone1521(83 kDa)對天竺鼠皮膚會產生出血壞死病變,可見PMT之毒性座落在5’端,而Δ5’ clone 23XL-17(112 kDa)對天竺鼠皮膚並無產生病變。以西方氏轉漬法分析結果,上述所選殖之表現蛋白均具有抗原性。至於PMT之免疫性可由對小鼠之保護效力結果得知取自Pasteurella multocida type D之 PMT(143 kDa)為100﹪(8/8),其免疫後母鼠所產下的第一子代保護效力亦為100﹪(8/8),1.5 kbΔ3’ clone 1521(83 kDa)為0﹪(0/8),2.3 kbΔ5’ clone 23XL-17(112kDa)免疫劑量(5μg)免疫組為 25﹪(2/8),免疫劑量(2.5μg)免疫組為 62.5﹪(5/8),免疫劑量(1.25μg)免疫組為 87.5﹪(7/8),至於連結LT clone 23LTBXL-20(126 kDa)免疫劑量(5μg)免疫組為37.5﹪(3/8),免疫劑量(2.5μg)免疫組為12.5﹪(1/8),免疫劑量(1.25μg)免疫組為 25﹪(2/8),由上述免疫保護效力之結果顯示重組PMT之免疫性基因座落在PMT基因之3’端,亦即2.3 kbΔ5’ clone 23XL-17(112kDa)組中免疫劑量(1.25μg)之免疫組具有87.5﹪之保護效力,惟該clone連接LTB後則免疫保護效力下降至12.5﹪至37.5﹪之間,此可能LTB與PMT基因3’端之PMT 2.3 kb之基因融合後,所表現之重組PMT是否在結構上因而有所改變,而導致免疫性亦隨之改變,有待日後進一步之探討。

Abstract
For characterization of Pasteurella multocida toxin (PMT)derived from tox A gene of Pasteurella multocida type D had been cloned. This study was also focusing on the epitopes of the PMT which could be encoded in either 5’ end or 3’ end of tox A gene﹐and then the immunogenic part of PMT will be studied by using an approach of gene deletion and polymerase chain reaction(PCR)cloning technique as well. Two clones‚ 1.5 kb Δ3’ clone 1521 and 2.3 kb Δ5’ clone 23XL-17 were selected since they were harboring the fragment of PMT gene of interest inserted into the pGEX6p-1 in E. coli BL21 ( DE-3 ). After expression‚ the purified GST fusion protein with molecular weight of 83 kDa ( 1.5 kb Δ3’ clone 1521 ) and 112 kDa ( 2.3 kbΔ5’ clone 23XL-17 ) were obtained respectively. The 83 kDa ( 1.5 kb Δ3’ clone 1521 ) other than 112 kDa ( 2.3 kb Δ5’ clone 23XL-17 ) and PMT ( 143 kDa ) originally derived from P. multocida type D demonstrated toxic activity in skin test in guinea pigs. It revealed that the functional toxicity of PMT from tox A gene could be located on 5’ end of PMT gene itself. The purified 83 kDa and 112 kDa GST fusion protein were strongly reactive to the specific antibody against PMT arised from immunized rabbits by using Western blotting assay in terms of antigenicity. Moreover‚ Only the 112 kDa ( 2.3 kb Δ5’ clone 23XL-17 ) had the immunoprotection as high as 87.5﹪( 7/8 ) against‚ ip‚ PMT challenge in BALB/c mice mean while 83 kDa ( 1.5 kb Δ3’ clone 1521 ) and control group of mice had no immunoprotection 0﹪( 0/8 ) at all against the same challenge. However‚ the LTB gene from heat-labile enterotoxin B subunit of E. coli which could be an adjuvant potential fused to 2.3 kb Δ5’ clone 23XL-17 derived from PMT gene and expressed as 126 kDa ( 2.3 kb Δ5’ linked to LTB, clone 23LTBXL-20 ) GST fusion protein. It showed unexpectedly immunoprotection rate as low as 12.5﹪( 1/8 ) to 37.5﹪( 3/8 ). This could be due to the conformational changes of antigen after fusion LTB gene to 2.3 kb of PMT gene ( Δ5’ clone 23XL-17 ). Further research need to be studied in the near future.

目錄
頁次
中文摘要 Ⅰ
英文摘要 Ⅲ
誌謝 Ⅴ
目錄 Ⅶ
圖次 Ⅹ
表次 ⅩⅢ
第一章 前言 1
第二章 文獻探討 4
2. 1 巴氏桿菌 4
2. 2 巴氏桿菌之型態及生化性狀 5
2. 3 巴氏桿菌之分離及鑑定 6
2. 4 豬萎縮性鼻炎之臨床性狀及組織病理學變化 7
2. 5 豬萎縮性鼻炎之致病機轉 9
2. 6 巴氏桿菌毒素 12
2. 6. 1 巴氏桿菌毒素純化及其特性 12
2. 6. 2 巴氏桿菌毒素之生物活免疫學特性 16
2. 6. 3 巴氏桿菌毒素之毒素基因 20
2. 7 豬萎縮性鼻炎之疫苗 23
第三章 材料及方法 25
3. 1 菌株分離及鑑定 25
3. 2 巴氏桿菌毒素之製備 25
3. 3 引子設計 26
3. 4 模板 ( Template ) DNA之製備 27
3. 5 聚合酶鏈反應 ( Polymerase chain reaction; PCR ) 29
3. 6 瓊膠(agarose)電泳 30
3. 7 PCR產物及載體Vector DNA之處理 30
3. 8 連結(Ligation) 31
3. 9 轉型(Transformation) 31
3. 10 選殖(Cloning) 32
3. 11 次選殖(Subcloning) 33
3. 12 表現(Expression) 33
3. 13 DNA序列之測定 34
3. 14 DNA序列之比對分析 34
3. 15 GST(Glutathione S-transferase)融合蛋白純化 35
3. 16 聚丙烯醯胺膠片(Sodium dodecyl sulfate-
polyacrylamide gel electrophoresis,SDS-PAGE )
電泳分析 36
3. 17 蛋白質濃度測定(Protein assay) 36
3. 18 兔子抗PMT毒素抗體之製備 37
3. 19 西方氏轉漬法(Western blotting) 37
3. 20 動物毒性試驗 38
3. 20. 1 PMT最小致死量(Minimum lethal dose)測定
38
3. 20. 2 肉眼及組織病理學檢查 39
3. 20. 3 天竺鼠皮膚壞死試驗 40
3. 21. 疫苗效力試驗 40
3. 21. 1 攻擊(Challenge) 40
3. 21. 2 幼鼠移行抗體保護效力試驗 41
第四章 結果 42
4. 1 全段3.8 kb之巴氏桿菌毒素基因選殖 42
4. 2 Δ3’ 1.5 kb之巴氏桿菌毒素基因選殖 43
4. 3 Δ5’ 2.3 kb之巴氏桿菌毒素基因選殖 43
4. 4 Δ5’ 2.3 kb之巴氏桿菌毒素基因連結E.coli忌熱性腸毒素B次單位(LTB)基因融合之選殖
44
4. 5 重組蛋白質之表現及純化 45
4. 6 重組蛋白質之DNA及胺基酸序列之比對及分析 46
4. 7 巴氏桿菌毒素及表現純化之重組蛋白之毒性試驗 46
4. 8 組織病理學變化 47
4. 9 PMT重組蛋白之抗原性 48
4. 10 PMT重組蛋白之免疫性 48
第五章 討論 50
參考文獻 81
附錄 107
附錄一 DNA之純化 107
附錄二 質體之抽取 109
附錄三 Glutathione Sepharose 4B再生及保存 111
附錄四 蛋白質濃度測定之標準曲線 113
作者簡介 114
圖次
頁次
圖4-1. 以Api 20E快速鑑定Pasteurella multocida(本試驗所分離之菌株編號為Pm-5) 56
圖4-2. 載體pGEX6p-1之圖式 57
圖4-3. PMT △3’ 1.5 kb clone 1521之Insert DNA之確認1.2% agarose電泳圖:M:λⅡ DNA marker (以Hind III切割),列1:100 bp DNA marker,列2、3:PMT 1.5 kb clone 1521。抽取PMT △3’ 1.5 kb clone 1521重組質體之DNA,以BamH I與XhoI限制酶切割後,確有Insert DNA 1.5 kb與載體pGEX6P-1DNA為4.9 kb 58
圖4-4. PMT △5’ 2.3 kb PCR產物之0.9% agaorse電泳圖:M:λⅡ DNA marker (以Hind III切割),列1-2:增幅PMT 基因之PCR product 2.3 kb 59
圖4-5. PMT △5’ 2.3 kb clone 23XL-17之Insert DNA之確認1.2% agarose電泳圖:M:λⅡ DNA marker (以Hind III切割),列1-14為抽取PMT △5’ 2.3 kb 之14個選殖菌株之重組質體DNA並以BamH I及Sma I限制酶切割後,其中列2確有PMT 2.3 kb之 Insert DNA存在,列6為pGEX6P-1(4.9 kb) 60
圖4-6. PMT △5’ 2.3 kb clone 連結LTB之Insert DNA之確認1.2% agarose電泳圖:M:λⅡ DNA marker (以Hind III切割),列1:100 bp DNA ladder,列2-7為所篩之菌株,其中列3、5、6確有LTB 372 bp之 Insert DNA存在。篩選PMT △5’ 2.3 kb 與連結LTB基因之菌株抽取其重組質體DNA,並以clone 19-24重組質體之DNA。以BamH I限制酶切割 61
圖4-7. PMT △3’ 1.5 kb clone 1519-1522純化表現蛋白之10% SDS-PAGE:M:蛋白分子量之marker,列1-4為所篩選之菌株(菌株編號為PMT △3’ 1.5 kb clone 1519-1522)所表現之純化的GST融合蛋(83 kDa) 62
圖4-8. PMT △5’ 2.3 kb clone 23XL-17純化表現蛋白之10% SDS- PAGE:M:蛋白分子量之marker,列1:PMT △5’ 2.3 kb clone 23XL-17 所表現之粗製蛋白,列2:PMT △5’ 2.3 kb clone 23XL-17 所表現之純化的GST融合蛋白(112 kDa) 63
圖4-9. PMT △5’ 2.3 kb連結LTB clone 23LTBXL-20及23純化表現蛋白之10% SDS-PAGE:M:蛋白分子量之marker,列1:PMT △5’ 2.3 kb連結LTB clone 20所表現之純化的GST融合蛋白(126 kDa),列2:PMT △5’ 2.3 kb連結LTB clone 23LTBXL-23所表現之純化的GST融合蛋白(126 kDa) 64
圖4-10. PMT △5’ 2.3 kb clone 23XL-17之DNA序列圖 65
圖4-11. PMT △5’ 2.3 kb clone 23XL-17之胺基酸序列圖 69
圖4-12. 天竺鼠皮膚毒性試驗之結果:1~3呈現出血壞死之病灶,4及5無任何病變。1:取自Pasteurella multocida type D之PMT,2:PMT 3.8 kb clone 90表現純化之GST融合蛋白(170 kDa),3:PMT △3’ 1.5 kb clone 1521表現純化之GST融合蛋白(83 kDa),4:PMT △5’ 2.3 kb clone 23XL-17表現純化之GST融合蛋白(112 kDa),5:陰性對照組(0.85﹪NaCl) 71
圖4-13. PMT(陽性對照組)之組織學變化:於天竺鼠皮膚接種之部位其鏡下可見皮膚之真皮層呈廣泛性嚴重充、出血。H&E,A:100倍,B:400倍 72
圖4-14. PMT 3.8 kb clone 90之組織學變化:於天竺鼠皮膚接種之部位其鏡下亦可見皮膚之真皮層呈廣泛性嚴重充、出血。H&E,A:100倍,B:400倍 73
圖4-15. PMT △3’ 1.5 kb clone 1521之組織學變化:於天竺鼠皮膚接種之部位其鏡下可見皮膚之真皮層充、出血。H&E,A:100倍,B:400倍 74
圖4-16. PMT △5’ 2.3 kb clone 23XL-17之組織學變化:於天竺鼠皮膚接種之部位其鏡下可見皮膚之真皮層無任何病變。H&E,A:100倍,B:400倍 75
圖4-17. 生理食鹽水(陰性對照組)之組織學變化:於天竺鼠皮膚接種之部位其鏡下可見皮膚之真皮層為正常皮膚構造。H&E,A:100倍,B:400倍 76
圖4-18. PMT △3’ 1.5 kb clone 1521之西方氏轉漬法:列1:PMT △3’ 1.5 kb clone 1521所表現及純化之GST融合蛋白(83 kDa),列2:該純化之GST融合蛋白能與特異性抗體(兔子抗PMT)產生特異性的結合反應 77
圖4-19. PMT △5’ 2.3 kb clone 23XL-17之西方氏轉漬法:M:蛋白分子量之marker,列1:PMT △5’ 2.3 kb clone 23XL-17所表現之純化的GST融合蛋白(112 kDa)(轉印自SDS-PAGE),列2:PMT △5’ 2.3 kb clone 23XL-17所表現之純化的GST融合蛋白(112 kDa)能與特異性抗體(兔子抗PMT)產生特異性的結合反應 78
表次
頁次
表 4-1. PMT重組蛋白之天竺鼠皮膚毒性試驗結果 79
表 4-2. PMT重組蛋白之BALB/c鼠免疫保護效力試驗結果 80

參考文獻
許聰文、劉正義、王渭賢、簡茂盛。1996。豬萎縮性鼻炎巴氏桿菌A型與D型菌毒素之致病性與生物性狀。中華獸醫誌 22(5):348-355。
劉燃炎、呂榮修、詹益波、王銘堪。1967。豬傳染性萎縮性鼻炎發生調查報告。台灣省家畜衛生試驗所研究報告 4:23-25。
劉瑞生。1973。豬萎縮性鼻炎自然與實驗病例早期感染與病理研究。台灣省畜牧學會會報 22:50-61。
劉正義、許聰文、簡茂盛、林正忠。1997。豬萎縮性鼻炎D型巴氏桿菌類毒素之免疫原性狀 中華獸醫誌 23(5):441-449。
Ackerman, M. R., Rimler, R. B., Thurston, J. R. 1991. Experimental model of atrophic rhinitis in gnotobiotic pigs. Infect Immun. 59 : 3626-3629.
Ackerman, M. R., Adams, D. A., Gerken, L. L., Beckman, M. J., Rimler, R. B. 1993. Purified Pasteurella multocida protein toxin reduces acid phosphatase-positive osteoclasts in the ventral nasal concha of gnotobiotic pigs. Calcif. Tissue Res. 52 : 455-459.
Baalsrud, K. J. 1987. Vaccination against atrophic rhinitis: effect on clinical symptoms, growth rate and turbinate atrophy. Acta Vet Scand. 28 : 305-311.
Baalsrud, K. J. 1987. Atrophic rhinitis in goats in Norway. Veterinary Record. 121 : 350-353.
Barber, P., Nair, S., Wilson, M., Nishihara, T., Henderson, B. 1995. Electron microscopy of a Gro-El-like protein from Actinobacillus actinomycetemcomitans. J. Dent. Res. 74 : 479.
Bording, A., Foged, N. T. 1991. Characterization of the immuno- genicity of formaldehyde detoxified Pasteurella multocida toxin. Vet Microbiol. 29 : 267-80.
Brim, T., A., Backstrom, L., Collins, M. T. 1986. Transmission of atrophic rhinitis by natural exposure of diseased pigs to unaffected pigs: Development of turbinate lesions and Bordetella bronchiseptica and Pasteurella multocida nasal microflora. I.P.V.S. 9th congress , p245.
Busch, C., Orth, J., Djouder, N., Aktories, K. 2001. Biological activity of a C-terminal fragment of Pasturella multocida toxin. Infect Immun.3628-3634.
Buys, W. E., Smith, H. E., Kamps, A. M., Kamp, E. M., Smits, M. A. 1990. Seuqence of the dermonecrotic toxin of Pasteurella multicda ssp. multocida. Nulceic Acids Res. 18 : 2815-2816.
Chanter, N., Rutter, J. M., Mackenie, A. 1986a. Partial purification of an osteolytic toxin from Pasteurella multocida. J. Gen. Microbiol.132 : 1089-1097.
Chanter, N., Rutter, J. M., Mackenie, A. 1986b. Partial purification of an osteolytic toxin from Pasteurella multocida. I.P.V.S. 9th congress , p228.
Chanter, N., Rutter, J. M., Luther, P. D. 1986. Rapid detection of toxigenic P. multocida by an agar overlay methods. Vet. Rec. 119 : 629-630.
Chanter, N., Rutter, J. M. 1989a. Comparison of method for the sampling and isolation of toxigenic Pasteurella multocida from the nasal cavity of pigs. Vet. Sci. Res. 47 : 355-358.
Chanter, N., Rutter, J. M. 1989b. Pasteurella and Pasteurellosis. Academic Press. Harcourt Brace Ivoanovien, London, p161-192.
Chanter, N., Rutter, J. M. 1990. Colonization by P. multocida in atrophic rhinitis of pigs and immunity to the osteolytic toxin. Vet. Microbiol. 25 : 518-520.
Chrisp, C. E., Foged, N. T. 1991. Induction of pneumonia in rabbits by use of a purified protein toxin from P. multocida. Am. J. Vet. Res. 52 : 56-61.
Carter, G. R. 1955. Studies on Pasteurella multocida. I. A hemagglutination test for the identification of serological types. Am. J. Vet. Res. 16 : 481-484.
Carter, G. R., Subronto, P. 1973. Identification of type D strains of Pasteurella multocida with acriflavine. Am. J. Vet. Res. 34 : 293-294.
Carter, G. R., Rundell, S. W. 1975. Identification of the type A strains Pasteurella multocida using Staphylococcal hyaluronidase. Vet. Rec. 96 : 343.
Confer, A. W., Nutt, S. H., Dabo, S. M., Panciera, R. J. 1996. Antibody responses of cattle to outer membrane proteins of pasteurella multocida A:3. Am. J. Vet. Res. 57 : 1453-1457.
Deeb, B. J. 1996. Respiratory disease and the Pasteurella complex . In Hillyerand, E. and Quesenberry K. (ed.), Clinical medicine and surgery of ferrets,rabbits and rodents. Saunders, W. B. Philadelphia, Pa. p189-201.
de Jong, M. F., Dei, J. L., Tetenburg, G. J. 1980. AR-pathogenicity- tests for Pasteurella multocida isolates. In Proceedings of the 6th international Pig Veterianry society : p211.
de Jong, M. F. 1983a. Atrophic rhinitis in the Netherlands. Atrophic Rhinitis. CEC Luxembourg. p52-60.
de Jong, M. F. 1983b. Treatment and control of atrophic rhinitis in the Netherlands. Atrophic rhinitis. CEC Luxembourg. p165-176.
de Jong, M. F. 1992. Progressive atrophic rhinitis. Disease of swine. 7th ed. Wolfe, Ames, Iowa. p414-435.
DiGiacomo, R. F., Deeb, B. J., Bernard, B. L., Klaassen, J. M. Chengappa, M. M. 1987. Safety and efficacy of a streptomycin dependent live Pasteurella multocida vaccine in rabbits. Lab Anim Sci. 37 : 187-90.
Dominick, M. A., Rimler, R. B. 1986. Turbinate atrophy in gnotobiotic pigs intranasally inoculated with protein toxin isolated from type D Pasteurella multocida. Am. J. Vet. Res. 47 : 1532-1536.
Dominick, M. A., Rimler, R. B. 1988. Turbinate osteoporosis in pigs following intranasal inoculation of Pasteurella toxin : histomorphometric and ultrastructural studies. Vet Pathol. 25 : 17-27.
Donnio, P. Y., Avril, J. L., Andre, PM M., Vaucel, J. 1991. Dermonerotic toxin production by strains of Pasteurella multocida isolated from man. J. Med. Microbiol. 34 : 333-337.
Eilon, G., Raisz, L. G. 1978. Comparison of the effects of stimulators and inhibitor of resorption on the release of lysosomal enzymes and radioactive calcium from fetal bone in organ culture. Endocrinology. 103 : 1968-1975.
Erler, W., Jacob, B., Schlegel, J. 1994. The influence of actions on the lethality and on the formation of the toxin of Pasteurella multocida. Microbiol. Res. 149 : 89-93.
Farrington, D. O., Switzer, W. P. 1979. Parenteral vaccination of young swine against Bordetella bronchiseptica. Am. J. Vet. Res. 40 : 1347-1351.
Felix, R., Fleisch, H., Frandsen, P. L. 1992. Effect of Pasteurella multocida toxin on bone resorption in vitro. Infect Immun. 60 : 4984-4988.
Flatau, G., Lemichez, E., Gauthier, M., Chardin, P., Paris, S., Florentini, C., Boquet, P. 1997. Toxin-induced activation of the G protein p21 Rho by deamidation of glutamine. Nature. 387 : 729-733.
Foged, N. T., Elling, F. Pedersen, K. B.1986. Isolation and characterization of a toxin from Pasteurella multocida. I.P.V.S.9th Congress. p231.
Foged, N. T., Pedersen, K. B., Elling, F. 1987. Characterization and biological effects of the Pasteurella multocida toxin. FEMS Microbiology Letter. 43 : 45-51.
Foged, N. T., Nielsen, J. P., Pedersen, K. B. 1988. Differentiation of toxigenic from nontoxigenic isolates of Pasteurella multocida by enzyme-linked immunosorbent assay. J. Clin. Micrbiol. 26 : 1419-1420.
Foged, N. T. 1992. Pasteurella multocida toxin. The characterization of the toxin and its significance in the diagnosis and prevention of progressive atrophic rhinitis in pigs. APMIS Suppl. 25 : 1-56.
Garcia, V. F. 1997. Animal bites and Pasteurella infections. Pediatr. Rev. 18 : 127-130.
Giles, C. J. 1986. Atrophic rhinitis. Disease of swine.6th ed. Ames : Iowa State Univ Press, p455-469.
Gwaltney, S. M., Galvin, R. J., Register, K. B., Rimler, R. B., Ackermann, M. R. 1997. Effects of Pasteurella multocida toxin on porcine bone marrow cell differentiation into osteoclasts and osteoblasts. Vet Pathol. 34 : 421-430.
Horiguchi, Y., Nakal, T., Kume, K. 1989. Purification and characterization of Bordetella bronchisetpica dermonecrotic toxin. Microb. Pathog. 6 : 361-368.
Horiguchi, Y., Nakal, T., Kume, K. 1990. Simplified procedure for purification of Bordetella bronchiseptica dermonecrotic toxin. FEMS Microbiol. Lett. 661 : 39-43.
Horowitz, M. C. 1993. Cytokines and estrogen in bone: anti- osteoporotic effects. Science. 260 : 626-627.
Idali, C., Foged, N. T., Frandsen, P. L., Nielsen, M. H., Elling, F. 1991. Ultrastructural localization of the Pasteurella multocida toxin in a toxin-producing strain. J. Gen. Microbiol. p1067-1071.
Il'ina, Z. M., Zasukhin, M. I. 1975. Role of Pasteurella toxins in the pathgenesis of infectious atrophic rhinitis. Sb Nauchn Rab Sib Nauchno-Issled Vet Inst. 25 : 76-86.
Jarvinen, L. Z., Hogenesch, H., Suckow, M. A., Bowersock, T. L. 1998. Induction of protective immunity in rabbits by coadministration of inactivated Pasteurella multocida toxin and potassium thiocyanate extract. Infect Immun. 66 : 3788-3795.
Kamp, E. M., van der Hejjden, P. J., Tetenburg, G. J. 1987. Purification of a heat-labile dermonecrotic toxin from culture fluid of Pasteurella multocida. Vet Microbiol. 13 : 235-248.
Kamp, E. M., Kimman, T. G. 1988. Induction of nasal turbinate atrophy in germ-free pigs, using Pasteurella multocida as well as bacterium-free crude and purified dermonnecrotic toxin of P. multocida. Am. J. Vet. Res. 49 : 1844-1849.
Kamps, A. M. I. E., Buys, W. E. C. M., Kamp, E. M., Smits, M. A. 1990. Specificity of DNA probes for the detection of toxigenic multocida stains. J. Clin. Microbiol. 28 : 1858-1861.
Kashimoto, T., Katahira, J., Cornejo, W. R., Masuda, M., Fukuoh, A., Matsuzawa, T., Ohnishi, T., Horiguchi, Y. 1999. Identification of funcitonal domains of Bordetella dermoncrotizing toxin. Infect Immun. 67 : 3727-3732.
Kim, B. H., Tak, R. B., Jang, I. H. 1992. Clinical and bacteriological studies on atrophic rhinitis of pigs in Korea. I.P.V.S. 11th Congress, p176.
Kimman, T. G., Lowik, C. W., Wee-Pals, L. J. A. V. D., Thesingh, C. W., Defize, P., Kamp, E. M., Bijvoet, O. L. M. 1987. Stimulation of bone resorption by inflamed nasal mucosa, dermonecrotic toxin-containing codnitioned medium from Pasteurella multocida, and purified dermonecrotic toxin from P. multoicda. Infect Immun. 55 : 2110-2116.
Klein, N. C., Cunha, B A. 1997. Pasteurella multocida pneumonia. Semin. Respir. Infect. 12 : 54-56.
Kobisch, M., Madec, F.1983. Economic significance of atrophic rhinitis in France. Atrophic rhinitis in pigs, CEC Luxembourg. p43-45.
Kobisch, M., Pennings, A. 1989. An evaluation in pigs of Nobi-Vac AR and an experimental atrophic rhinitis vaccine containing P. multocida DNT-toxoid and B. bronchiseptica. Vet. Rec. 124 : 57-61.
Kume, K., Nakai, T. 1985. Dissociation of Pasteurella multocida dermonecrotic toxin into three polypeptide fragment. Jpn. J. Vet. Sci. 47 : 829-833.
Kume, K., Nakai, T., Samejima, Y. 1986. Porperties of dermonecrotic toxin prepared from sonic extracts of Bordetella bronchiseptica. Infect Immun. 52 : 370-377.
Lariviere, S., Leblanc, L., Mittal, K. R., Martineau, G. P. 1992. Characterization of Pasteurella multocida from nasal cavities of piglets from farms with or without atrophic rhinitis. J. Clin. Microbiol. 30 : 1398-1401.
Lax, A. J., Chanter, N. 1990. Cloning of the gene from Pasteurella multocida and its role in atrophic rhinitis. J. Gen. Mirobiol. 36 : 81-87.
Lemichez, E., Flatau, G., Bruzzone, M. Boquet, P., Gauthier, M. 1997. Molecular locatization of the Escherichia coli cytotoxic necrotizing factor CNF1 cell-binding and catalytic domains. Mol Microbiol. 24 : 1061-1070.
Litwin, C. M., Calderwood, S. B. 1993. Role of iron in regulation of virulence genes. Clin. Microbiol. Rev. 6 : 137-149.
Magyar, T. 1989. Study of the toxin—producing ability of Pasteurella multocida in mice. Acta Veterinaria Hungarica. p319-325.
Magyar, T., Glavits, R. 1990. Immunopathological changes in mice caused by Bordetella bronchiseptica and Pasteurella multocida. Acta Veterinaria Hungarica. p203-210.
Magyar, T., Rimler, R. B.1991. Detection and enumeration of toxin-producing Pasteurella multocida with a colony-blot assay. J. Clin. Microbiol. 29 : 1328-1332.
Martineau-Doize, B., Menard, J., Girard, C., Frantz, J. C., Martineau, G. P. 1991. Effects of purified Pasteurella multocida dermonecro- toxin on the nasal ventral turbinates of fattening pigs: histological observaltions. Can. J. Vet. Res. 55 : 377-379.
Martineau-Doize, B., Caya, I., Gagne, S., Jutras, I., Dumas, G. 1993. Effects of Pasteurella multocida toxin on the osteoclast population of the rat. J. Comp. Pathol. 108 : 81-91.
Miller, J. H., Mekalanos, J. J., Falkow, S. 1989. Coordinate regulation and sensory transduction in the control of bacterial virulence. Science. 243 : 916-922.
Mullan, P. B., Lax, A. J. 1996. Pasteurella multocida toxin is a mitogen for bone cells in primary culture. Infect Immun. 64 : 959-965.
Mullan, P. B., Lax, A. J. 1988. Pasteurella multocida toxin stimulates bone resorption by osteoclasts via interaction with osteoblasts. Calcif. tissue Int. 63 : 340-345.
Nair, S. P., Meghji, S., Wilson, M., Reddi, K., With, P., Henderson, B. 1996. Bacterially induced bone destruction: mechanisms and misconceptions. Infect Immun. 64 : 2371-2380.
Nakai, T., Sawata, A., Tsuji, M., Kume, K. 1984a. Characterization of dermonecrotic toxin produced by serotype D strains of Pasteurella multocida. Am. J. Vet. Res. 45 : 2410-2413.
Nakai, T., Sawata, A., Tsuji, M., Kume, K. 1984b. Purification of dermonecrotic toxin from a sonic extract of Pasteurella multocida SP-72 serotype D. Infect Immun. 56 : 234-240.
Nakai, T., Sawata, A., Kume, K. 1985. Intracellular locations of dermonecrotic toxins in Pasteurella multocida and in Bordetella bronchiseptica. Am. J. Vet. Res. 46 : 870-874.
Nielsen, N. C. 1983. Prevalence and economic significance of atrophic rhinitis. CEC Luxembourg. p35-42.
Nielson, J. P., Bisgaard, M., Pederson, K. B. 1986. Production of toxin in strains previously classified as Pasteurella multocida. Acta Pathol. Microbiol. Immunol. Scand. Sect. B. 94 : 203-204.
Oswald, E., Sugat, M., Labigne, A., Wu, H. C., Fiorentini, C., Boquet, P., O'Brien, A. D. 1994. Cytotoxic necrotizing factor type 2 produced by virulent Escherichia coli modifies the small GTP-binding proteins Rho involved in assembly of actin stress fibers. Proc Natl Acad Sci U S A. 91 : 3814-3818.
Pedersen, K.B. 1984. The pathogenesis of atrophic rhinitis in pigs induced by toxigenic Pasteurella multocida. J. Comp. Pathol.. 94 : 203-214.
Penning, A. M. M. A., Strom, P. K. 1984. A test in Vero-cell monolayers for toxin production by strains of P. multocida isolated from pigs suspected of having atrophic rhinitis. Vet. Microbiol. 9 : 503-508.
Petersen, S. K., Foged, N. T. 1989. Cloning and expression of the Pasteurella multocida toxin gene, toxA, in Escherichia coli. Infect Immun. 57 : 3907-3913.
Petersen, S. K. 1990. The complete nucleotide sequence of the Pasteurella multocida toxin gene and evidence for a transcritpional repressor, TxaR. Mol Microbiol. 4 : 821-830.
Petersen, S. K., Foged, N. T., Bording, A., Nielsen, J. P., Riemann, H. K., Frandsen. P. L. 1991. Recombinant derivatives of Pasteurella multocida toxin: candidates for a vaccine against progressive atrophic rhinitis. Infect Immun. 59 : 1387-1393.
Pettit, R. K., Ackermann, M. R., Rimler, R. B. 1993. Receptor-mediated binding of Pasteurlla muloticda from atrophic rhinitis of pigs. Vet. Rec. 114 : 393-396.
Rimler, R. B., Brogden, K. A. 1986. Pasteurella multocida isolated from rabbits and swine: serologic types and toxin production. Am. J. Vet. Res. 47 : 730-737.
Rimler, R. B., Rhoades, K. R. 1987. Serogroup F, a new capsular serogroup of Pasteurella multocida. J. Clin. Microbiol. 25 : 615-618.
Rozengurt, E., Higgins, T., Chanter, N., Lax, A. J., Staddon, J. M. 1990. Pasteutella multocida toxin: potent mitogen for cultured fibroblasts. Proc Natl Acad Sci U S A. 87 : 123-127.
Rutter, J.M., Luther, P. D. 1984. Cell culture assay for toxigenic Pasteurella multocida from atrophic rhinitis of pigs. Vet. Rec. 114 : 393-396.
Rutter, J. M., Mackenzie, A. 1984. Pathogenesis of atrophic rhinitis in pigs: a new perspective. Vet. Rec. 114 : 89-90.
Schoss, P.1983. Clinical diagnosis of atrophic rhinitis. In Atrophic Rhinitis of pigs. CEC Luxembourg. p13-21.
Sterner-Kock, A., Lanske, B., Uberschar, S., Atkinson, M. J. 1995. Effects of the Pasteurella multocida toxin on osteoblastic cells in vitro. Vet. Pathol. 32 : 274-279.
Thurston, J. R., Cheville, N. F., Rimler, R. B., Sacks, J. 1989. Serum complement activity and serum enzymes in rats after a subcutaneuos injection of toxin prepared from Pasteurella multocida type D. Vet. Immunol. Immunopathol. 23 : 385-388.
Thurston, J. R., Rimler, R. B., Ackermann, M. R., Cheville, N. F., Sacks, J. M. 1991. Immunity induced in rats vaccinated with toxoid prepared from heat-labile toxin produced by Pasteurella multocida serogroup D. Vet Microbiol. 27 : 169-74.
Townsend, K. M., Hanh, T. X., O'Boyle, D., Wilkie, I., Phan, T. T., Wijewardana, T. G., Trung, N. T., Frost, A. J. 2000. PCR detection and analysis of Pasteurella multocida from the tonsils fo slaughtered pigs in Vietham. Vet. Microbiol.. 72 : 69-78.
van Diemen, P. M., de Jong, M. F., de Vries Reilingh, G., van der Hel, P., Schrama, J. W. 1994. Intranasal administration of Pasteurella multocida toxin in a challenge-exposure model used to induce subclinical signs of atrophic rhinitis in pigs. Am. J. Vet. Res. 55 : 49-54.
van Diemen, P. M., de Vries Reilingh, G., Parmentier, H. K. 1994. Immune responses of piglets to Pasteurella multocida toxin and toxoid. Vet. Immunol. Immunopathol. 41 : 307-321.
van der Heijden P. J., van Es, C. D. M., Kamp, E. M., Pals-van Dam, J. W. 1983. Partial purification and characterization of a heat-labile dermonecrotic toxin from Pasteurella multocida. CEC Luxembourg. p114-120.
Walker, K. E., Weiss, A. A. 1994. Characterization of the dermonecrotic toxin in members of the genus Bordetella. Infect Immun. 62 : 3817-3828.
Ward, P. N., Miles, A. J., Sumner, I. G., Thomas, L. H., Lax, A. J. 1998. Activity of the mitogenic Pasteruella multocida toxin requires an essential C-terminal residue. Infect Immun. 68 : 5636-5642.
Wilson, B. A., Ponferrada, V. G., Vallance J. E., Ho, M. F. 1999. Localization of the intracellular activiaty domain of Pasteurella multocida toxin to the N terminus. Infect Immun. 67 : 80-87.
Wilson, B. A., Aminova, L. R., Ponferrada, V. G., Ho, M. 2000. Differential modulation and subsequent blockade of mitogenic signaling and cell cycle progression by Pasteurella multocida toxin. Infect Immun. 68 : 4531-4538.

QRCODE
 
 
 
 
 
                                                                                                                                                                                                                                                                                                                                                                                                               
第一頁 上一頁 下一頁 最後一頁 top