TY - JOUR
T1 - Analyses of diverse mammals' milk and lactoferrin glycans using five pathogenic bacterial lectins
AU - Zinger-Yosovich, Keren D.
AU - Sudakevitz, Dvora
AU - Iluz, David
AU - Gilboa-Garber, Nechama
PY - 2011/2
Y1 - 2011/2
N2 - Milk indigested glycans hamper infections by blocking pathogen adhesion to babies' cells via lectins (sugar-binding proteins). This study describes usage of five pathogenic bacterial lectins and two plant lectins for analyses of alpaca, buffalo, camel, cow, dog, fallow deer, giraffe, goat, horse, human, rabbit, and sheep milks, and also commercial human and cow milk lactoferrins. The lectins used differentially reacted with the 12 milks - most strongly with humans' ones. Most of them (excluding Pseudomonas aeruginosa galactophilic PA-IL) were also sensitive to the human and cow lactoferrins. The fucophilic bacterial lectins were most sensitive to human lactoferrin, while the mannophilic ones - to the cow's. The actual function of bacterial lectins in pathogen adhesion and their non-glycosylated structures (evading non-specific interactions) are advantageous for such studies. This study shows the efficiency of the bacterial lectins for milk analyses: differentiating between the diverse milks, estimating their anti-infection potentials, and probing their active glycans.
AB - Milk indigested glycans hamper infections by blocking pathogen adhesion to babies' cells via lectins (sugar-binding proteins). This study describes usage of five pathogenic bacterial lectins and two plant lectins for analyses of alpaca, buffalo, camel, cow, dog, fallow deer, giraffe, goat, horse, human, rabbit, and sheep milks, and also commercial human and cow milk lactoferrins. The lectins used differentially reacted with the 12 milks - most strongly with humans' ones. Most of them (excluding Pseudomonas aeruginosa galactophilic PA-IL) were also sensitive to the human and cow lactoferrins. The fucophilic bacterial lectins were most sensitive to human lactoferrin, while the mannophilic ones - to the cow's. The actual function of bacterial lectins in pathogen adhesion and their non-glycosylated structures (evading non-specific interactions) are advantageous for such studies. This study shows the efficiency of the bacterial lectins for milk analyses: differentiating between the diverse milks, estimating their anti-infection potentials, and probing their active glycans.
KW - Glycans
KW - Lactoferrins
KW - Lectin blocking
KW - Milks
KW - Pathogenic bacterial lectins
KW - Western blotting
UR - http://www.scopus.com/inward/record.url?scp=77957017407&partnerID=8YFLogxK
U2 - 10.1016/j.foodchem.2010.07.084
DO - 10.1016/j.foodchem.2010.07.084
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AN - SCOPUS:77957017407
SN - 0308-8146
VL - 124
SP - 1335
EP - 1342
JO - Food Chemistry
JF - Food Chemistry
IS - 4
ER -