2004
DOI: 10.1007/978-1-4757-4242-8_65
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Lactoferrin Blocks the Initial Host Cell Attachment Mechanism of Enteropathogenic E. Coli (EPEC)

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Cited by 11 publications
(5 citation statements)
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“…This leads to the disruption and permeabilization of the bacterial membrane and ultimately cell death. Furthermore, the N-terminus of lactoferrin possesses a serine protease-like activity, which potentially degrades secreted proteins 78 .…”
Section: Antimicrobial Activity Of Lactoferrinmentioning
confidence: 99%
“…This leads to the disruption and permeabilization of the bacterial membrane and ultimately cell death. Furthermore, the N-terminus of lactoferrin possesses a serine protease-like activity, which potentially degrades secreted proteins 78 .…”
Section: Antimicrobial Activity Of Lactoferrinmentioning
confidence: 99%
“…Recombinant human lactoferrin causes loss and degradation of E. coli secreted proteins A, B and D (EspABD), especially EspB. These secreted proteins are components of the type III machinery and are known to be key elements in EPEC pathogenesis [41]. EspB plays a central role in pathogenesis both by its membrane lytic and its myosin-binding functions.…”
Section: Enteropathogenic E Coli (Epec)mentioning
confidence: 99%
“…They observed that Lf treatment of Shigella fl exneri 5 strain M90T impaired invasiveness [60] by inducing release and degradation of invasion plasmid antigens B and C (IpaB and IpaC) [61,62]. They also found that Lf blocks Enteropathogenic E. coli adherence, hemolysis and induction of actin polymerisation in HEp2 cells as a result of the Lf-mediated degradation of E. coli secreted proteins A, B and D (EspABD) [63,64]. Massucci et al [65] characterised in vitro the proteolytic activity of bovine Lf towards synthetic substrates.…”
Section: Antibacterial Activity Related To Proteolysismentioning
confidence: 92%