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

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

Kupffer cell activation by LPS is mediated via LPS binding protein and CD14

2001 ◽  
Vol 120 (5) ◽  
pp. A27-A27
Author(s):  
M FAN ◽  
S GOYERT ◽  
A AMINLARI ◽  
R KLEIN ◽  
L STEINSTRAESSER ◽  
...  
Keyword(s):  
Kupffer Cell ◽  
Cell Activation ◽  
Binding Protein ◽  
Lps Binding

Hemoglobin Enhances the Binding of Bacterial Endotoxin to Human Endothelial Cells

1996 ◽  
Vol 76 (02) ◽  
pp. 258-262 ◽  
Author(s):  
Robert I Roth
Keyword(s):  
Endothelial Cells ◽  
Binding Protein ◽  
Bacterial Endotoxin ◽  
Dependent Manner ◽  
Serum Free Medium ◽  
Free Medium ◽  
Human Endothelial Cells ◽  
Serum Factors ◽  
Serum Free ◽  
Lps Binding

SummaryHuman endothelial cells, when incubated with bacterial endotoxin (lipopolysaccharide, LPS), modify their surface in association with prominent production of procoagulant tissue factor (TF) activity. This deleterious biological effect of LPS has been shown previously to be enhanced approximately 10-fold by the presence of hemoglobin (Hb), a recently recognized LPS binding protein that causes disaggregation of LPS and increases the biological activity of LPS in a number of in vitro assays. The present study was performed to test the hypothesis that Hb enhances the LPS-induced procoagulant activity of human umbilical vein endothelial cells (HUVEC) by increasing LPS binding to the cells. The binding of 3H-LPS to HUVEC was determined in the absence or presence of Hb or two other known LPS-binding proteins, human serum albumin (HSA) and IgG. LPS binding was substantially increased in the presence of Hb, in a Hb concentration-dependent manner, but was not increased by HSA or IgG. Hb enhancement of LPS binding was observed in serum-free medium, indicating that there was no additional requirement for any of the serum factors known to participate in the interaction of LPS with cells (e.g., lipopolysaccharide (LPS)-binding protein (LBP) and soluble CD14 (sCD14)). Hb enhancement of LPS binding also was observed in the more physiologic condition of 100% plasma. LPS-induced TF activity was stimulated by Hb, but not by HSA or IgG. In serum-free medium, TF activity was not stimulated under any of the conditions tested. Ultrafiltration of LPS was dramatically increased after incubation with Hb but not with HSA or IgG, suggesting that LPS disaggregation by Hb was responsible for the enhanced binding of LPS to HUVEC and the subsequent stimulation of TF activity.

Cationic Antimicrobial Peptides for Tuberculosis: A Mini-Review

2019 ◽  
Vol 20 (9) ◽  
pp. 885-892
Author(s):  
Sara Silva ◽  
Nuno Vale
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Amino Acid ◽  
Antimicrobial Peptides ◽  
Resistance Mechanisms ◽  
Therapeutic Agents ◽  
Pharmacological Properties ◽  
Therapeutic Activity ◽  
Alternative Strategies ◽  
Cationic Antimicrobial Peptides ◽  
Specific Amino Acid

Cationic antimicrobial peptides (CAMPs) can be considered as new potential therapeutic agents for Tuberculosis treatment with a specific amino acid sequence. New studies can be developed in the future to improve the pharmacological properties of CAMPs and also understand possible resistance mechanisms. This review discusses the principal properties of natural and/or synthetic CAMPs, and how these new peptides have a significant specificity for Mycobacterium tuberculosis. Also, we propose some alternative strategies to enhance the therapeutic activity of these CAMPs that include coadministration with nanoparticles and/or classic drugs.

Membrane targeting cationic antimicrobial peptides

2019 ◽  
Vol 537 ◽  
pp. 163-185 ◽  
Author(s):  
Daniela Ciumac ◽  
Haoning Gong ◽  
Xuzhi Hu ◽  
Jian Ren Lu
Keyword(s):  
Antimicrobial Peptides ◽  
Membrane Targeting ◽  
Cationic Antimicrobial Peptides
Sign in / Sign up

Export Citation Format

Share Document