Proteome analysis of mouse macrophages treated with anthrax lethal toxin

Chandra, Harish ; Gupta, Pradeep K. ; Sharma, Kirti ; Mattoo, Abid R. ; Garg, Satyendra K. ; Gade, W. N. ; Sirdeshmukh, Ravi ; Maithal, Kapil ; Singh, Yogendra (2005) Proteome analysis of mouse macrophages treated with anthrax lethal toxin Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics, 1747 (2). pp. 151-159. ISSN 1570-9639

Full text not available from this repository.

Official URL:

Related URL:


Anthrax toxin produced by bacillus anthracis is a tripartite toxin comprising of protective antigen (PA), lethal factor (LF) and edema factor (EF). PA is the receptor-binding component, which facilitates the entry of LF or EF into the cytosol. EF is a calmodulin-dependent adenylate cyclase that causes edema whereas LF is a zinc metalloprotease and leads to necrosis of macrophages. It is also important to note that the exact mechanism of LF action is still unclear. With this view in mind, in the present study, we investigated a proteome wide effect of anthrax lethal toxin (LT) on mouse macrophage cells (J774A.1). Proteome analysis of LT-treated and control macrophages revealed 41 differentially expressed protein spots, among which phosphoglycerate kinase I, enolase I, ATP synthase (β subunit), tubulin β2, γ-actin, Hsp70, 14-3-3 zeta protein and tyrosine/tryptophan-3-monooxygenase were found to be down-regulated, while T-complex protein-1, vimentin, ERp29 and GRP78 were found to be up-regulated in the LT-treated macrophages. Analysis of up- and down-regulated proteins revealed that primarily the stress response and energy generation proteins play an important role in the LT-mediated macrophage cell death.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Lethal Toxin; Bacillus anthracis; Proteomics; Stress; ATP; Cytoskeletal
ID Code:64849
Deposited On:15 Oct 2011 12:49
Last Modified:15 Oct 2011 12:49

Repository Staff Only: item control page