Characterization of lethal factor binding and cell receptor binding domains of protective antigen of Bacillus anthracis using monoclonal antibodies

被引：105

作者：

Little, SF ^{[1
]}

Novak, JM ^{[1
]}

Lowe, JR ^{[1
]}

Leppla, SH ^{[1
]}

Singh, Y ^{[1
]}

Klimpel, KR ^{[1
]}

Lidgerding, BC ^{[1
]}

Friedlander, AM ^{[1
]}

机构：

[1] NIDR, MICROBIAL ECOL LAB, BETHESDA, MD 20892 USA

来源：

MICROBIOLOGY-SGM | 1996年 / 142卷

关键词：

Bacillus anthracis; protective antigen; epitope mapping;

D O I：

10.1099/13500872-142-3-707

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Lethal toxin from Bacillus anthracis is composed of protective antigen (PA) and lethal factor (LF). Anti-PA mAbs that neutralized lethal toxin activity, either in vivo or in vitro, identified three non-overlapping antigenic regions on PA. Two distinct antigenic regions were recognized by the four mAbs that neutralized lethal toxin activity by inhibiting the binding of I-125-LF to cell-bound PA. Mapping showed that one mAb, 1G3(PA63), recognized an epitope on a 17 kDa fragment located between amino acid residues Ser-168 and Phe-314. The three other mAbs, ZD3(PA), ZD5(PA) and 10D2(PA), recognized an epitope between amino acids IIe-581 and Asn-601. A single antigenic region was recognized by the three mAbs, 3B6(PA), 14B7(PA) and 10E10(PA63), that inhibited binding of I-125-PA to cells. This region was located between amino acids Asp-671 and IIe-721. These results confirm previously defined functional domains of PA and suggest that LF may interact with two different sites on PA to form lethal toxin.

引用

页码：707 / 715

页数：9

共 31 条

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