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

Little, Stephen F. ; Novak, Jeanne M. ; Lowe, John R. ; Leppla, Stephen H. ; Singh, Yogendra ; Klimpel, Kurt R. ; Lidgerding, Burton C. ; Friedlander, Arthur M. (1996) Characterization of lethal factor binding and cell receptor binding domains of protective antigen of Bacillus anthracis using monoclonal antibodies Microbiology, 142 (3). pp. 707-715. ISSN 1350-0872

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Official URL: http://mic.sgmjournals.org/content/142/3/707.short

Related URL: http://dx.doi.org/10.1099/13500872-142-3-707

Abstract

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 125I-LF to cell-bound PA. Mapping showed that one mab, 1G3PA63, recognized an epitope on a 17 kda fragment located between amino acid residues Ser-168 and Phe-314. The three other mabs, 2D3PA, 2D5PA and 10D2PA, recognized an epitope between amino acids Ile-581 and Asn-601. A single antigenic region was recognized by the three mAbs, 3B6PA, 14B7PA and 10E10PA63, that inhibited binding of 125I-PA to cells. This region was located between amino acids Asp-671 and Ile-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.

Item Type:Article
Source:Copyright of this article belongs to Society for General Microbiology.
Keywords:Bacillus anthracis; Protective Antigen; Epitope Mapping
ID Code:64829
Deposited On:15 Oct 2011 12:46
Last Modified:15 Oct 2011 12:46

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