Lactoferrin / iron binding / Pseudomonas aeruginosa

Doe

J Clin Gastroenterol. 2004 Jul;38:S127-S129. Related Articles, Links

Lactoferrin Functions: Current Status and Perspectives.

Valenti P, Berlutti F, Conte MP, Longhi C, Seganti L.

*Department of Experimental Medicine, II University of
Naples; and daggerDepartment of Public Health Sciences,
University of Rome, "La Sapienza," Italy.

Lactoferrin, an iron-binding glycoprotein synthesized by
neutrophils and exocrine glands, plays an important role in
human innate defense mechanisms against bacteria, fungi, and
viruses. First, a bacteriostatic activity of lactoferrin,
depending on iron withholding to bacteria, and successively
a bactericidal iron-independent effect, related to its
binding on bacterial surfaces, was recognized. Many other
functions have been ascribed to this cationic protein,
including the inhibiting action toward bacterial adhesion
and invasion of target host cells. Recent research also
reported the lactoferrin influence on bacterial aggregation
and biofilm development of Pseudomonas aeruginosa and
Streptococcus mutans. The different lactoferrin functions
can be justified by different physicochemical properties of
the molecule, which include the iron-binding capability, the
binding to anionic cell surfaces and molecules, and serine
protease activity.

PMID: 15220678 [PubMed - as supplied by publisher]

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