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Structure/Function Aspects of Actinobacillus actinomycetemcomitans Leukotoxin
Author(s) -
Lally Edward T.,
Kieba Irene R.,
Golub Ellis E.,
Lear James D.,
Tanaka Jacqueline C.
Publication year - 1996
Publication title -
journal of periodontology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.036
H-Index - 156
eISSN - 1943-3670
pISSN - 0022-3492
DOI - 10.1902/jop.1996.67.3s.298
Subject(s) - actinobacillus , virulence , microbiology and biotechnology , organism , periodontitis , function (biology) , bacterial outer membrane , toxin , virulence factor , biology , pasteurellaceae , chemistry , bacteria , computational biology , gene , escherichia coli , biochemistry , medicine , genetics , antibiotics , dentistry , haemophilus influenzae
A ctinobacillus actinomycetemcomitans has been implicated as a causative organism in early‐onset periodontitis. The mechanisms by which A. actinomycetemcomitans is pathogenic are not known, but the organism produces several potential virulence factors, one of which is a leukotoxin. As a group, bacterial protein toxins are made up of structural domains which control various aspects of toxic activity, such as target cell recognition, membrane insertion, and killing. The purpose of this article is to review the structure of RTX, with special emphasis to its relation to toxin function. In addition, we will propose a model based upon other bacterial proteins whereby the water‐soluble A. actinomycetemcomitans leukotoxin is able to achieve insertion into a biological membrane. J Periodontol 1996;67:298–308.