NDLI: The specificity of protection against cationic antimicrobial peptides by lactoferrin binding protein B

Content Provider	Springer Nature Link
Author	Morgenthau, Ari Partha, Sarathy K. Adamiak, Paul Schryvers, Anthony B.
Copyright Year	2014
Abstract	A variety of Gram-negative pathogens possess host-specific lactoferrin (Lf) receptors that mediate the acquisition of iron from host Lf. The integral membrane protein component of the receptor, lactoferrin binding protein A specifically binds host Lf and is required for acquisition of iron from Lf. In contrast, the role of the bi-lobed surface lipoprotein, lactoferrin binding protein B (LbpB), in Lf binding and iron acquisition is uncertain. A common feature of LbpBs from most species is the presence of clusters of negatively charged amino acids in the protein’s C-terminal lobe. Recently it has been shown that the negatively charged regions from the Neisseria meningitidis LbpB are responsible for protecting against an 11 amino acid cationic antimicrobial peptide (CAP), lactoferricin (Lfcin), derived from human Lf. In this study we investigated whether the LbpB confers resistance to other CAPs since N. meningitidis is likely to encounter other CAPs from the host. LbpB provided protection against the cathelicidin derived peptide, cathelicidin related antimicrobial peptide (mCRAMP), but did not confer protection against Tritrp 1 or LL37 under our experimental conditions. When tested against a range of rationally designed synthetic peptides, LbpB was shown to protect against IDR-1002 and IDR-0018 but not against HH-2 or HHC10.
Starting Page	923
Ending Page	933
Page Count	11
File Format	PDF
ISSN	09660844
Journal	BioMetals
Volume Number	27
Issue Number	5
e-ISSN	15728773
Language	English
Publisher	Springer Netherlands
Publisher Date	2014-07-20
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Cationic antimicrobial peptides Lactoferrin receptor Lipoprotein Bactericidal Outer membrane protein Neisseria Biochemistry Pharmacology/Toxicology Microbiology Cell Biology Plant Physiology Medicine/Public Health
Content Type	Text
Resource Type	Article
Subject	Metals and Alloys Biochemistry, Genetics and Molecular Biology Biomaterials Agricultural and Biological Sciences

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