Human Lactoferrin Impairs Virulence of Shigella flexneri

Lactoferrin is a glycoprotein present in most human mucosal secretions, including human milk. Lactoferrin is bacteriostatic in low iron media and, in some settings, bactericidal. Lactoferrin impairs ability of Shigella flexneri serotype 5 strain M90T to invade HeLa cells. To determine the mechanism...

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Bibliographic Details
Published in:The Journal of infectious diseases 2003-01, Vol.187 (1), p.87-95
Main Authors: Gomez, Henry F., Ochoa, Theresa J., Carlin, Lily G., Cleary, Thomas G.
Format: Article
Language:English
Subjects:
Antigens
Antigens, Bacterial - metabolism
Bacteria
Bacterial Adhesion - drug effects
Bacterial Proteins - metabolism
Biological and medical sciences
Epithelial cells
General aspects
HeLa Cells
Human infectious diseases. Experimental studies and models
Humans
Infectious diseases
Lactoferrin - pharmacology
Lipid A - metabolism
Medical sciences
Plasmids
Protease Inhibitors - pharmacology
Proteins
Secretion
Shigella
Shigella flexneri
Shigella flexneri - drug effects
Shigella flexneri - growth & development
Shigella flexneri - pathogenicity
Virulence
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Summary:Lactoferrin is a glycoprotein present in most human mucosal secretions, including human milk. Lactoferrin is bacteriostatic in low iron media and, in some settings, bactericidal. Lactoferrin impairs ability of Shigella flexneri serotype 5 strain M90T to invade HeLa cells. To determine the mechanism by which lactoferrin decreases invasiveness of Shigella organisms, its effect on the major virulence proteins responsible for bacterial uptake by host cells was evaluated. Lactoferrin induced degradation of invasion plasmid antigens IpaB and, to a lesser extent, IpaC, the key proteins responsible for bacteria-directed phagocytosis by mammalian cells. The lipid A–binding N-terminal portion of lactoferrin (residues 1–33) induces release of invasion antigens but does not induce degradation of IpaBC. Lactoferrin does not directly degrade previously released invasion plasmid antigens but works by making IpaBC susceptible to breakdown by surface-expressed protease(s)
ISSN:0022-1899
1537-6613
DOI:10.1086/345875