Examination of bovine lactoferrin binding to bifidobacteria.
In the present study, lactoferrin binding to bifidobacteria and detection of lactoferrin-binding protein in membrane fractions of several bifidobacteria have been demonstrated. This is the first report showing the binding of bovine lactoferrin to four Bifidobacterium spp. (B. infantis, B. breve, B. bifidum, B. longum) incubated with biotinylated lactoferrin and fluorescein conjugated-avidin and observed under an inverted confocal laser scanning microscope. Fluorescence staining showed lactoferrin binding at the pole of the bacterial cells. A lactoferrin-binding protein with a molecular weight of approximately 67 kDa was also detected in the membrane fraction of Bifidobacterium spp. by far western blotting technique using biotinylated lactoferrin and horseradish peroxidase-conjugated streptavidin. Based on the results of this and previously reported studies, we suggest that binding of lactoferrin to Bifidobacterium longum is strain-dependent.
Rahman
Md M
MM
Dairy Science Laboratory, Graduate School of Agriculture, Hokkaido University, W-9, N-9, Sapporo, 060-8589, Japan. morshedur68@yahoo.com
Kim
W S
WS
Ito
T
T
Kumura
H
H
Shimazaki
K
K
D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism*; D001644:Bifidobacterium / Q000166:cytology / Q000378:metabolism*; D002417:Cattle; D002473:Cell Wall / Q000378:metabolism*; D007781:Lactoferrin / Q000378:metabolism* / Q000494:pharmacology; D018613:Microscopy, Confocal; D011485:Protein Binding / Q000187:drug effects / Q000502:physiology; D013045:Species Specificity
D001426:Bacterial Proteins; D007781:Lactoferrin