Involvement of domain 3 in oligomerization by the protective antigen moiety of anthrax toxin.
J Bacteriol
; 183(6): 2111-6, 2001 Mar.
Article
in En
| MEDLINE
| ID: mdl-11222612
ABSTRACT
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, PA(63), 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 PA(63) heptamer, indicating that this may be the primary function of this domain.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Bacterial Toxins
/
Antigens, Bacterial
Limits:
Animals
Language:
En
Journal:
J Bacteriol
Year:
2001
Document type:
Article
Affiliation country: