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铜绿假单胞菌外毒素A结构域Ib和III的两个片段的比较免疫化学

Comparative immunochemistry of two fragments from domains Ib and III of Pseudomonas aeruginosa exotoxin A.

作者信息

Rutault K, Vacheron M J, Guinand M, Michel G

机构信息

Laboratoire de Biochimie Microbienne, Université Claude Bernard Lyon I, France.

出版信息

Infect Immun. 1993 Dec;61(12):5417-20. doi: 10.1128/iai.61.12.5417-5420.1993.

DOI:10.1128/iai.61.12.5417-5420.1993
PMID:8225617
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC281335/
Abstract

Two rabbit polyclonal antisera have been produced by immunization with two fragments corresponding to sequences 392 to 404 and 392 to 613 of Pseudomonas aeruginosa exotoxin A. Both antisera inhibit the ADP-ribosyltransferase activity of exotoxin A but do not inhibit its NAD-glycohydrolase activity. In addition, only the second antiserum was capable of neutralizing exotoxin A cytotoxicity in cell culture and in vivo. Consequently, the common sequence 392 to 404 of the two fragments is not a neutralizing epitope and such an epitope should reside within residues 405 to 613 of exotoxin A. The sequence 392 to 404 was shown to be hidden in the native molecule, and the results suggest that this sequence is most likely in close proximity to residues involved in eukaryotic elongation factor 2 binding.

摘要

通过用与铜绿假单胞菌外毒素A的392至404和392至613序列相对应的两个片段进行免疫，制备了两种兔多克隆抗血清。两种抗血清均抑制外毒素A的ADP - 核糖基转移酶活性，但不抑制其NAD - 糖水解酶活性。此外，只有第二种抗血清能够在细胞培养和体内中和外毒素A的细胞毒性。因此，两个片段的共同序列392至404不是中和表位，这样的表位应该位于外毒素A的405至613残基内。已证明序列392至404在天然分子中是隐藏的，结果表明该序列很可能紧邻参与真核延伸因子2结合的残基。

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