scholarly journals A comparative, cross-species investigation of the properties and roles of transferrin- and lactoferrin-binding protein B from pathogenic bacteria

2017 ◽  
Vol 95 (1) ◽  
pp. 5-11 ◽  
Author(s):  
N. Ostan ◽  
A. Morgenthau ◽  
R.H. Yu ◽  
S.D. Gray-Owen ◽  
A.B. Schryvers
Keyword(s):  
Antimicrobial Peptides ◽  
Protective Effect ◽  
Transgenic Mouse ◽  
Pathogenic Bacteria ◽  
Binding Protein ◽  
Host Proteins ◽  
Cationic Antimicrobial Peptides ◽  
Surface Receptors ◽  
Protein B

Pathogenic bacteria from the families Neisseriaeceae and Moraxellaceae acquire iron from their host using surface receptors that have the ability to hijack iron from the iron-sequestering host proteins transferrin (Tf) and lactoferrin (Lf). The process of acquiring iron from Tf has been well-characterized, including the role of the surface lipoprotein transferrin-binding protein B (TbpB). In contrast, the only well-defined role for the homologue, LbpB, is in its protection against cationic antimicrobial peptides, which is mediated by regions present in some LbpBs that are highly enriched in glutamic or aspartic acid. In this study we compare the Tf-TbpB and the Lf-LbpB interactions and examine the protective effect of LbpB against extracts from human and transgenic mouse neutrophils to gains insights into the physiological roles of LbpB. The results indicate that in contrast to the Tf-TbpB interaction, Lf-LbpB interaction is sensitive to pH and varies between species. In addition, the results with transgenic mouse neutrophils raise the question of whether there is species specificity in the cleavage of Lf to generate cationic antimicrobial peptides or differences in the potency of peptides derived from mouse and human Lf.

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

BioMetals ◽  
2014 ◽  
Vol 27 (5) ◽  
pp. 923-933 ◽  
Author(s):  
Ari Morgenthau ◽  
Sarathy K. Partha ◽  
Paul Adamiak ◽  
Anthony B. Schryvers
Keyword(s):  
Antimicrobial Peptides ◽  
Binding Protein ◽  
Cationic Antimicrobial Peptides ◽  
Protein B

scholarly journals The dlt Operon of Bacillus cereus Is Required for Resistance to Cationic Antimicrobial Peptides and for Virulence in Insects

2009 ◽  
Vol 191 (22) ◽  
pp. 7063-7073 ◽  
Author(s):  
Z. Abi Khattar ◽  
A. Rejasse ◽  
D. Destoumieux-Garzón ◽  
J. M. Escoubas ◽  
V. Sanchis ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Bacillus Cereus ◽  
Cell Walls ◽  
Type Strain ◽  
Pathogenic Bacteria ◽  
Wild Type Strain ◽  
Wild Type ◽  
Gram Positive ◽  
Cationic Antimicrobial Peptides ◽  
Humoral Immune

ABSTRACT The dlt operon encodes proteins that alanylate teichoic acids, the major components of cell walls of gram-positive bacteria. This generates a net positive charge on bacterial cell walls, repulsing positively charged molecules and conferring resistance to animal and human cationic antimicrobial peptides (AMPs) in gram-positive pathogenic bacteria. AMPs damage the bacterial membrane and are the most effective components of the humoral immune response against bacteria. We investigated the role of the dlt operon in insect virulence by inactivating this operon in Bacillus cereus, which is both an opportunistic human pathogen and an insect pathogen. The ΔdltBc mutant displayed several morphological alterations but grew at a rate similar to that for the wild-type strain. This mutant was less resistant to protamine and several bacterial cationic AMPs, such as nisin, polymyxin B, and colistin, in vitro. It was also less resistant to molecules from the insect humoral immune system, lysozyme, and cationic AMP cecropin B from Spodoptera frugiperda. ΔdltBc was as pathogenic as the wild-type strain in oral infections of Galleria mellonella but much less virulent when injected into the hemocoels of G. mellonella and Spodoptera littoralis. We detected the dlt operon in three gram-negative genera: Erwinia (Erwinia carotovora), Bordetella (Bordetella pertussis, Bordetella parapertussis, and Bordetella bronchiseptica), and Photorhabdus (the entomopathogenic bacterium Photorhabdus luminescens TT01, the dlt operon of which did not restore cationic AMP resistance in ΔdltBc ). We suggest that the dlt operon protects B. cereus against insect humoral immune mediators, including hemolymph cationic AMPs, and may be critical for the establishment of lethal septicemia in insects and in nosocomial infections in humans.

scholarly journals Cutting Edge: Cationic Antimicrobial Peptides Block the Binding of Lipopolysaccharide (LPS) to LPS Binding Protein

2000 ◽  
Vol 164 (2) ◽  
pp. 549-553 ◽  
Author(s):  
Monisha G. Scott ◽  
Anita C. E. Vreugdenhil ◽  
Wim A. Buurman ◽  
Robert E. W. Hancock ◽  
Michael R. Gold
Keyword(s):  
Antimicrobial Peptides ◽  
Binding Protein ◽  
Cutting Edge ◽  
Cationic Antimicrobial Peptides ◽  
Lps Binding

Role of antimicrobial peptides system in inflammatory periodontal diseases non-specific oral cavity protection

2021 ◽  
Vol 66 (7) ◽  
pp. 422-427
Author(s):  
N. V. Davidovich ◽  
N. V. Solovieva ◽  
A. S. Galieva ◽  
S. Yu. Lepeshkin ◽  
E. N. Bashilova ◽  
...  
Keyword(s):  
Oral Cavity ◽  
Antimicrobial Peptides ◽  
Chronic Periodontitis ◽  
Pathogenic Bacteria ◽  
Periodontal Diseases ◽  
Control Group ◽  
Periodontal Pathogens ◽  
Local Immunity ◽  
Microbial Invasion

The system of antimicrobial peptides (AMP) is one of the most ancient mechanisms of the macroorganism resistance to infectious pathogens invasion. The aim of the study was to determine the role of the antimicrobial peptides system and periodontal pathogenic markers in the development and progression of inflammatory periodontal diseases. Gingival pocket washes (91 samples in total) for the research were received from patients with inflammatory periodontal diseases (chronic periodontitis and gingivitis) and intact periodontium. Using ELISA, the content of antimicrobial peptides was determined: human alpha-defensin (HNP 1-3), beta-defensin (HBD 1-3) and cathelicidin (LL-37). Periodontal pathogenic markers were isolated during RT-PCR. The study revealed differences in AMP concentrations by groups: level of HBD 2 in patients with chronic periodontitis was 1,36 times higher than those in the group of patients with chronic gingivitis (p=0,023) and 2,39 times higher than those in the control group (p<0,001), the content of HNP 1-3 in the group of patients with chronic periodontitis was reduced by 1,23 times compared with the indicators of the group of patients with gingivitis (p=0,045) and by 1,97 times compared with the indicators of the control group (p<0,001). The frequency of detection of periodontal pathogenic bacteria genes was 88,0% in patients with periodontitis, 76,92% in patients with gingivitis and 33,3% in the group with intact periodontium. HBD 2 content moderately correlated with the definition of P. gingivalis (r=0,612; p=0,022), T. forsythensis (r= 0,434; p=0,015), A. actinomycetemcomitans (r=0,483; p=0,006), a moderate negative correlation was detected between the content of HNP 1-3 and the release of periodontal pathogens in associations (P. gingivalis with T. forsythensis and T. denticola) (r=-0,388; p=0,031) in the group of patients with chronic periodontitis. Thus, the revealed relationships and correlations indicate shifts in the processes of reparative regeneration of the oral cavity and the regulation of local immunity in response to microbial invasion.

The role of lactoferrin binding protein B in mediating protection against human lactoferricin1This article is part of a Special Issue entitled Lactoferrin and has undergone the Journal's usual peer review process.

2012 ◽  
Vol 90 (3) ◽  
pp. 417-423 ◽  
Author(s):  
Ari Morgenthau ◽  
Margaret Livingstone ◽  
Paul Adamiak ◽  
Anthony B. Schryvers
Keyword(s):  
Peer Review Process ◽  
Binding Protein ◽  
Iron Acquisition ◽  
Protein A ◽  
Human Lactoferrin ◽  
Cationic Antimicrobial Peptide ◽  
Iron Source ◽  
Iron Deficient ◽  
Protein B

Bacteria that inhabit the mucosal surfaces of the respiratory and genitourinary tracts of mammals encounter an iron-deficient environment because of iron sequestration by the host iron-binding proteins transferrin and lactoferrin. Lactoferrin is also present in high concentrations at sites of inflammation where the cationic, antimicrobial peptide lactoferricin is produced by proteolysis of lactoferrin. Several Gram-negative pathogens express a lactoferrin receptor that enables the bacteria to use lactoferrin as an iron source. The receptor is composed of an integral membrane protein, lactoferrin binding protein A (LbpA), and a membrane-bound lipoprotein, lactoferrin binding protein B (LbpB). LbpA is essential for growth with lactoferrin as the sole iron source, whereas the role of LbpB in iron acquisition is not yet known. In this study, we demonstrate that LbpB from 2 different species is capable of providing protection against the killing activity of a human lactoferrin-derived peptide. We investigated the prevalence of lactoferrin receptors in bacteria and examined their sequence diversity. We propose that the protection against the cationic antimicrobial human lactoferrin-derived peptide is associated with clusters of negatively charged amino acids in the C-terminal lobe of LbpB that is a common feature of this protein.

scholarly journals MprF-Mediated Lysinylation of Phospholipids in Staphylococcus aureus Leads to Protection against Oxygen-Independent Neutrophil Killing

2003 ◽  
Vol 71 (1) ◽  
pp. 546-549 ◽  
Author(s):  
Sascha A. Kristian ◽  
Manuela Dürr ◽  
Jos A. G. Van Strijp ◽  
Birgid Neumeister ◽  
Andreas Peschel
Keyword(s):  
Staphylococcus Aureus ◽  
Antimicrobial Peptides ◽  
Host Defense ◽  
Membrane Lipids ◽  
Human Monocytes ◽  
Wild Type ◽  
Cationic Antimicrobial Peptides ◽  
The Impact ◽  
Defense Molecules

ABSTRACT Staphylococcus aureus achieves resistance to defensins and similar cationic antimicrobial peptides (CAMPs) by modifying anionic membrane lipids via MprF with l-lysine, which leads to repulsion of these host defense molecules. S. aureus ΔmprF, which lacks the modification, was very efficiently killed by neutrophil defensins and CAMP-producing leukocytes, even when oxygen-dependent killing was disrupted, but was as susceptible as wild-type bacteria to inactivation by myeloperoxidase or human monocytes lacking defensins. These results demonstrate the impact and specificity of MprF-mediated CAMP resistance and underscore the role of defensin-like peptides in innate host defense.

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