Open AccessClostridium difficileToxin A Alters In Vitro–Adherent Neutrophil Morphology and Function
Author(s) -
Gerly Anne de Castro Brito,
Gail W. Sullivan,
William P. Ciesla,
Holliday T. Carper,
Gerald L. Mandell,
Richard L. Guerrant
Publication year - 2002
Publication title -
the journal of infectious diseases
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.69
H-Index - 252
eISSN - 1537-6613
pISSN - 0022-1899
DOI - 10.1086/340236
Subject(s) - toxin , clostridium difficile toxin a , actin cytoskeleton , in vitro , actin , chemistry , pneumolysin , proinflammatory cytokine , microbiology and biotechnology , biology , cytoskeleton , clostridium difficile , inflammation , biochemistry , immunology , cell , virulence , antibiotics , gene
The effects of purified toxin A in vitro on the shape and function of polymorphonuclear leukocytes (PMNL) were examined. Toxin A induced changes in adherent PMNL shape from a compact spherical or pyramidal shape to a thin and rope-like shape. This change in shape was accompanied by rearrangement of the F-actin cytoskeleton into aggregates. Toxin A-treated PMNL exhibited increased adherence and expressed less L-selectin and more Mac-1, compared with untreated PMNL. In contrast to these proinflammatory actions, toxin A impaired both directed and non-directed PMNL migration in response to N-formylmethionylleucylphenylalanine. In addition, toxin A decreased the oxidative activity of adherent PMNL stimulated by recombinant human tumor necrosis factor-alpha. These effects could be explained by toxin A-induced glucosylation of the signaling small-size guanine 5'-triphosphate-binding proteins of the Rho family in human PMNL.
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