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1
Use of synthetic peptides and site-specific antibodies to localize a diphtheria toxin sequence associated with ADP-ribosyltransferase activity.使用合成肽和位点特异性抗体来定位与ADP-核糖基转移酶活性相关的白喉毒素序列。
J Bacteriol. 1993 Feb;175(3):898-901. doi: 10.1128/jb.175.3.898-901.1993.
2
Diphtheria toxin and Pseudomonas aeruginosa exotoxin A: active-site structure and enzymic mechanism.白喉毒素与铜绿假单胞菌外毒素A：活性位点结构与酶促机制
Curr Top Microbiol Immunol. 1992;175:27-41. doi: 10.1007/978-3-642-76966-5_2.
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FEMS Microbiol Immunol. 1992 Jul;4(5):267-72. doi: 10.1111/j.1574-6968.1992.tb05005.x.
4
Generation of neutralizing antipeptide antibodies to the enzymatic domain of Pseudomonas aeruginosa exotoxin A.针对铜绿假单胞菌外毒素A酶结构域的中和性抗肽抗体的产生。
Infect Immun. 1998 May;66(5):2170-9. doi: 10.1128/IAI.66.5.2170-2179.1998.
5
Cytotoxic activity of a recombinant chimaeric protein between Pseudomonas aeruginosa exotoxin A and Corynebacterium diphtheriae diphtheria toxin.铜绿假单胞菌外毒素A与白喉棒状杆菌白喉毒素之间的重组嵌合蛋白的细胞毒性活性
Mol Microbiol. 1992 May;6(10):1281-7. doi: 10.1111/j.1365-2958.1992.tb00849.x.
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Structure-activity relationships in diphtheria toxin and Pseudomonas aeruginosa exotoxin A.白喉毒素与铜绿假单胞菌外毒素A的构效关系
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Mapping the enzymatic active site of Pseudomonas aeruginosa exotoxin A.绘制铜绿假单胞菌外毒素A的酶活性位点图谱。
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本文引用的文献

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The amino-acid sequence of two non-toxic mutants of diphtheria toxin: CRM45 and CRM197.白喉毒素的两种无毒突变体CRM45和CRM197的氨基酸序列。
Nucleic Acids Res. 1984 May 25;12(10):4063-9. doi: 10.1093/nar/12.10.4063.
2
Cloning, nucleotide sequence, and expression in Escherichia coli of the exotoxin A structural gene of Pseudomonas aeruginosa.铜绿假单胞菌外毒素A结构基因的克隆、核苷酸序列及在大肠杆菌中的表达
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3
NAD binding site of diphtheria toxin: identification of a residue within the nicotinamide subsite by photochemical modification with NAD.白喉毒素的NAD结合位点：通过用NAD进行光化学修饰鉴定烟酰胺亚位点内的一个残基。
Proc Natl Acad Sci U S A. 1984 Jun;81(11):3307-11. doi: 10.1073/pnas.81.11.3307.
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Cleavage of structural proteins during the assembly of the head of bacteriophage T4.在噬菌体T4头部组装过程中结构蛋白的切割
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Localization of the active site of diphtheria toxin.白喉毒素活性位点的定位
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6
Mapping the enzymatic active site of Pseudomonas aeruginosa exotoxin A.绘制铜绿假单胞菌外毒素A的酶活性位点图谱。
Proteins. 1988;3(3):146-54. doi: 10.1002/prot.340030303.
7
Structure of exotoxin A of Pseudomonas aeruginosa at 3.0-Angstrom resolution.铜绿假单胞菌外毒素A在3.0埃分辨率下的结构
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8
Active site of Pseudomonas aeruginosa exotoxin A. Glutamic acid 553 is photolabeled by NAD and shows functional homology with glutamic acid 148 of diphtheria toxin.铜绿假单胞菌外毒素A的活性位点。谷氨酸553被NAD光标记，并与白喉毒素的谷氨酸148显示出功能同源性。
J Biol Chem. 1987 Jun 25;262(18):8707-11.
9
Diphtheria toxin: quantification and assay.白喉毒素：定量与测定
Methods Enzymol. 1988;165:218-25. doi: 10.1016/s0076-6879(88)65034-8.
10
Histidine 21 is at the NAD+ binding site of diphtheria toxin.组氨酸21位于白喉毒素的NAD⁺结合位点。
J Biol Chem. 1989 Jul 25;264(21):12385-8.

使用合成肽和位点特异性抗体来定位与ADP-核糖基转移酶活性相关的白喉毒素序列。

Use of synthetic peptides and site-specific antibodies to localize a diphtheria toxin sequence associated with ADP-ribosyltransferase activity.

作者信息

Olson J C

机构信息

Department of Pathology and Laboratory Medicine, Medical University of South Carolina, Charleston 29425.

出版信息

J Bacteriol. 1993 Feb;175(3):898-901. doi: 10.1128/jb.175.3.898-901.1993.

DOI:10.1128/jb.175.3.898-901.1993
PMID:8423159
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC196241/
Abstract

Diphtheria toxin (DT) and Pseudomonas aeruginosa exotoxin A have the same molecular mechanism of toxicity; both toxins ADP-ribosylate a modified histidine residue in elongation factor 2. To help identify amino acids involved in this reaction, sequences in DT that share homology with P. aeruginosa exotoxin A were synthesized and examined for a role in the ADP-ribosyltransferase reaction. By using this approach, residues 32 to 54 of DT were found to define an epitope associated with antibody-mediated inhibition of DT enzyme activity. This lends further support to the notion that residues in this region of DT are involved in the enzymatic reaction.

摘要

白喉毒素（DT）和铜绿假单胞菌外毒素A具有相同的毒性分子机制；这两种毒素都将ADP-核糖基连接到延伸因子2中一个修饰的组氨酸残基上。为了帮助确定参与该反应的氨基酸，合成了DT中与铜绿假单胞菌外毒素A具有同源性的序列，并检测其在ADP-核糖基转移酶反应中的作用。通过使用这种方法，发现DT的32至54位残基定义了一个与抗体介导的DT酶活性抑制相关的表位。这进一步支持了DT这一区域的残基参与酶促反应的观点。