siderophilins

sid·er·oph·i·lins

(sid'ĕr-of'i-linz),
Nonheme, iron-binding proteins; there are three central classes of siderophilins: transferrin (1) (in vertebrate blood), lactoferrin (in mammalian milk and other secretions), and conalbumin or ovotransferrin (avian blood and avian egg white).
References in periodicals archive ?
To obtain host iron, successful pathogens use one or more of four strategies: binding of ferrated siderophilins with extraction of iron at the cell surface; erythrocyte lysis, digestion of hemoglobin, and heme assimilation; use of siderophores that withdraw iron from transferrin; and procurement of host intracellular iron.
Bacterial receptors recognize siderophilins generally from a single or closely related host species.
Virulent streptococci are examples of bacteria that neither bind siderophilins [ILLEGIBLE TEXT] produce siderophores yet proficiently invade and replicate in many tissues in [ILLEGIBLE TEXT] host species.
Unable to [ILLEGIBLE TEXT] siderophilins or form siderophores, L.
However, not every pathogen that uses siderophilin binding has a narrow host [ILLEGIBLE TEXT] For example, Staphylococcus aureus can be virulent for a variety of mammalian species.