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VF category: Transferrin/Lactoferrin binding (total 67 related VFs in database, current show from 1 to 10)
 
VF Bacteria Brief description
Tbp
(Transferrin-binding protein)
Haemophilus
(H. influenzae Rd KW20)
Instead of using siderophores, H. influenzae and other species, such as N. gonorrohoeae and N. meningitidis, express proteins at the their cell surface that specifically bind hot iron-carrying molecules (such as transferrin and lactoferrin) and scavenge iron from these host molecules. Two H. influenzae iron-repressible transferrin-binding protein called Tbp1 and Tbp2 were identified. ...
Lbp
(Lactoferrin-binding protein)
Neisseria
(N. meningitidis MC58)
The entry site of N. meningitidis into the body is the nasopharynx, where lactoferrin predominates as the main source of iron. ...
Tbp
(Transferrin-binding protein)
Neisseria
(N. meningitidis MC58)
The tbp locus is a bicistronic operon consisting of tbpA and tbpB. Unlike the case for many other genes of Neisseria, there is no phase variation of the transferrin receptor. ...
ViuPDGC system
Vibrio
(V. cholerae O1 biovar El Tor str. N16961)
Periplasmic binding protein-dependent ABC transport systems. ...
Tbp
(Transferrin-binding protein)
Haemophilus
(H. influenzae 86-028NP)
Instead of using siderophores, H. influenzae and other species, such as N. gonorrohoeae and N. meningitidis, express proteins at the their cell surface that specifically bind hot iron-carrying molecules (such as transferrin and lactoferrin) and scavenge iron from these host molecules. Two H. influenzae iron-repressible transferrin-binding protein called Tbp1 and Tbp2 were identified. ...
Tbp
(Transferrin-binding protein)
Haemophilus
(H. influenzae PittEE)
Instead of using siderophores, H. influenzae and other species, such as N. gonorrohoeae and N. meningitidis, express proteins at the their cell surface that specifically bind hot iron-carrying molecules (such as transferrin and lactoferrin) and scavenge iron from these host molecules. Two H. influenzae iron-repressible transferrin-binding protein called Tbp1 and Tbp2 were identified. ...
Tbp
(Transferrin-binding protein)
Haemophilus
(H. influenzae PittGG)
Instead of using siderophores, H. influenzae and other species, such as N. gonorrohoeae and N. meningitidis, express proteins at the their cell surface that specifically bind hot iron-carrying molecules (such as transferrin and lactoferrin) and scavenge iron from these host molecules. Two H. influenzae iron-repressible transferrin-binding protein called Tbp1 and Tbp2 were identified. ...
Tbp
(Transferrin-binding protein)
Haemophilus
(H. somnus 129PT)
Instead of using siderophores, H. influenzae and other species, such as N. gonorrohoeae and N. meningitidis, express proteins at the their cell surface that specifically bind hot iron-carrying molecules (such as transferrin and lactoferrin) and scavenge iron from these host molecules. Two H. influenzae iron-repressible transferrin-binding protein called Tbp1 and Tbp2 were identified. ...
Tbp
(Transferrin-binding protein)
Haemophilus
(H. somnus 2336)
Instead of using siderophores, H. influenzae and other species, such as N. gonorrohoeae and N. meningitidis, express proteins at the their cell surface that specifically bind hot iron-carrying molecules (such as transferrin and lactoferrin) and scavenge iron from these host molecules. Two H. influenzae iron-repressible transferrin-binding protein called Tbp1 and Tbp2 were identified. ...
Lbp
(Lactoferrin-binding protein)
Neisseria
(N. gonorrhoeae NCCP11945)
The entry site of N. meningitidis into the body is the nasopharynx, where lactoferrin predominates as the main source of iron. ...
   


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