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Lactoferrin Inhibits Respiratory Pathogens
Bovine lactoferrin inhibits the efficiency of invasion of respiratory
A549 cells of different iron-regulated morphological forms of
Pseudomonas aeruginosa and Burkholderia cenocepacia. [Journal Article]
Int J Immunopathol Pharmacol 2008 Jan-Mar; 21(1):51-9.
Berlutti F, Superti F, Nicoletti M, Morea C, Frioni A, Ammendolia MG,
Battistoni A, Valenti P
Pseudomonas aeruginosa and Burkholderia cenocepacia are two important
opportunistic respiratory pathogens of cystic fibrosis (CF) patients.
Infections caused by these microorganisms are particularly difficult
to eradicate because they are usually highly resistant to several
currently available broad-spectrum antibiotics.
Lactoferrin (Lf), a glycoprotein found in physiological fluids of
mammals and present at high concentrations in infected and inflamed
tissues, plays an important role in the natural defence mechanism
against pathogens and in immune regulation.
In the present study, we evaluate the ability of bovine lactoferrin
(bLf) to influence P. aeruginosa PAO1 and B. cenocepacia PV1
adhesiveness and invasiveness, using the A549 human bronchial cell
line.
Three different iron-induced morphological forms of bacteria (free-
living, aggregates and biofilm) were assayed.
The addition of bLf to cells just before infection had little
influence on adhesion efficiency for all three of the morphological
forms of B. cenocepacia PV1, while a slight increase in adhesion
efficiency by P. aeruginosa PAO1 was noticed.
Conversely, invasion of all three morphological forms of both P.
aeruginosa and B. cenocepacia was strongly inhibited by the presence
of bLf, independently of its degree of iron-binding activity. This is
the first report demonstrating an anti-invasive property of bLf for
strains of P. aeruginosa and B. cenocepacia.
International journal of immunopathology and pharmacology [Int J
Immunopathol Pharmacol]
--------------------------------------------------------------------------------
Journal of Dairy Science Vol. 76 No. 7 1876-1881
(c) 1993 by American Dairy Science Association (R) This Article
Iron-Binding Properties of Bovine Lactoferrin in Iron-Rich Solution
Yoko Nagasako 1, Hitoshi Saito 1, Yoshitaka Tamura 1, Seiichi
Shimamura 1, and Mamoru Tomita 1
1 Nutritional Science Laboratory, Morinaga Milk Industry Co., Ltd.,
1-83, 5-Chome, Higashihara, Zama-City, Kanagawa-Prefecture, 228, Japan
The iron-binding properties of bovine lactoferrin in iron-rich
solution were investigated.
Ferrous iron was not stable in solution and was easily changed to the
insoluble ferric state, but solubility of ferrous iron was stabilized
by the presence of lactoferrin.
However, casein hydrolysate or BSA was not effective in stabilizing
iron in solution.
As indicated by use of cibacron blue affinity gel, iron bound to
lactoferrin, and the charge of supersaturated lactoferrin was higher
than that of normal iron-saturated lactoferrin according to native
PAGE electrophoresis.
The evidence suggests that lactoferrin can bind iron at sites other
than its chelate-binding sites, thereby stabilizing iron in solution.
Key Words: lactoferrin * iron binding * affinity gel * electrophoresis
Submitted on August 12, 1992
Accepted on January 28, 1993
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Tom
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* jesuswasavegetarian.7h . com
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A549 cells of different iron-regulated morphological forms of
Pseudomonas aeruginosa and Burkholderia cenocepacia. [Journal Article]
Int J Immunopathol Pharmacol 2008 Jan-Mar; 21(1):51-9.
Berlutti F, Superti F, Nicoletti M, Morea C, Frioni A, Ammendolia MG,
Battistoni A, Valenti P
Pseudomonas aeruginosa and Burkholderia cenocepacia are two important
opportunistic respiratory pathogens of cystic fibrosis (CF) patients.
Infections caused by these microorganisms are particularly difficult
to eradicate because they are usually highly resistant to several
currently available broad-spectrum antibiotics.
Lactoferrin (Lf), a glycoprotein found in physiological fluids of
mammals and present at high concentrations in infected and inflamed
tissues, plays an important role in the natural defence mechanism
against pathogens and in immune regulation.
In the present study, we evaluate the ability of bovine lactoferrin
(bLf) to influence P. aeruginosa PAO1 and B. cenocepacia PV1
adhesiveness and invasiveness, using the A549 human bronchial cell
line.
Three different iron-induced morphological forms of bacteria (free-
living, aggregates and biofilm) were assayed.
The addition of bLf to cells just before infection had little
influence on adhesion efficiency for all three of the morphological
forms of B. cenocepacia PV1, while a slight increase in adhesion
efficiency by P. aeruginosa PAO1 was noticed.
Conversely, invasion of all three morphological forms of both P.
aeruginosa and B. cenocepacia was strongly inhibited by the presence
of bLf, independently of its degree of iron-binding activity. This is
the first report demonstrating an anti-invasive property of bLf for
strains of P. aeruginosa and B. cenocepacia.
International journal of immunopathology and pharmacology [Int J
Immunopathol Pharmacol]
--------------------------------------------------------------------------------
Journal of Dairy Science Vol. 76 No. 7 1876-1881
(c) 1993 by American Dairy Science Association (R) This Article
Iron-Binding Properties of Bovine Lactoferrin in Iron-Rich Solution
Yoko Nagasako 1, Hitoshi Saito 1, Yoshitaka Tamura 1, Seiichi
Shimamura 1, and Mamoru Tomita 1
1 Nutritional Science Laboratory, Morinaga Milk Industry Co., Ltd.,
1-83, 5-Chome, Higashihara, Zama-City, Kanagawa-Prefecture, 228, Japan
The iron-binding properties of bovine lactoferrin in iron-rich
solution were investigated.
Ferrous iron was not stable in solution and was easily changed to the
insoluble ferric state, but solubility of ferrous iron was stabilized
by the presence of lactoferrin.
However, casein hydrolysate or BSA was not effective in stabilizing
iron in solution.
As indicated by use of cibacron blue affinity gel, iron bound to
lactoferrin, and the charge of supersaturated lactoferrin was higher
than that of normal iron-saturated lactoferrin according to native
PAGE electrophoresis.
The evidence suggests that lactoferrin can bind iron at sites other
than its chelate-binding sites, thereby stabilizing iron in solution.
Key Words: lactoferrin * iron binding * affinity gel * electrophoresis
Submitted on August 12, 1992
Accepted on January 28, 1993
Who loves ya.
Tom
Jesus Was A Vegetarian!
* jesuswasavegetarian.7h . com
Man Is A Herbivore!
* tinyurl . com /a3cc3
DEAD PEOPLE WALKING
* tinyurl . com /zk9fk
