Involvement of Domain 3 in Oligomerization by the Protective Antigen Moiety of Anthrax Toxin
AUTOR(ES)
Mogridge, Jeremy
FONTE
American Society for Microbiology
RESUMO
Protective antigen (PA), a component of anthrax toxin, binds receptors on mammalian cells and is activated by a cell surface protease. The resulting active fragment, PA63, forms ring-shaped heptamers, binds the enzymic moieties of the toxin, and translocates them to the cytosol. Of the four crystallographic domains of PA, domain 1 has been implicated in binding the enzymic moieties; domain 2 is involved in membrane insertion and oligomerization; and domain 4 binds receptor. To determine the function of domain 3, we developed a screen that allowed us to isolate random mutations that cause defects in the activity of PA. We identified several mutations in domain 3 that affect monomer-monomer interactions in the PA63 heptamer, indicating that this may be the primary function of this domain.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=95109Documentos Relacionados
- Oligomerization of Anthrax Toxin Protective Antigen and Binding of Lethal Factor during Endocytic Uptake into Mammalian Cells
- Identification of a Receptor-Binding Region within Domain 4 of the Protective Antigen Component of Anthrax Toxin
- Anthrax toxin: channel-forming activity of protective antigen in planar phospholipid bilayers.
- A role for PACE4 in the proteolytic activation of anthrax toxin protective antigen.
- The lethal and edema factors of anthrax toxin bind only to oligomeric forms of the protective antigen