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1 January 2003

Volume 187, Number 1
The Journal of Infectious Diseases 2003;187:87–95
© 2003 by the Infectious Diseases Society of America. All rights reserved.
0022-1899/2003/18701-0012$15.00
DOI: 10.1086/345875
MAJOR ARTICLE

Human Lactoferrin Impairs Virulence of Shigella flexneri

Henry F. Gomez,

Theresa J. Ochoa,

Lily G. Carlin, and

Thomas G. Cleary

Division of Infectious Diseases, Department of Pediatrics, University of Texas–Houston Medical School, Houston

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).

Received 2 May 2002; revised 12 September 2002; electronically published 13 December 2002.

Reprints or correspondence: Dr. Thomas G. Cleary, Div. of Infectious Diseases, Dept. of Pediatrics, University of Texas, Houston, 6431 Fannin St., JFB 1.739, Houston, TX 77030 ().

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  • Financial support: National Institutes of Health (grant HD‐13021); Agennix.

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