Lactoferricin B Inhibits the Phosphorylation of the Two-Component System Response Regulators BasR and CreB

Ho, Yu Hsuan; Sung, Tzu Cheng; Chen, Chien Sheng

doi:10.1074/mcp.m111.014720

Cited by 41 publications

(38 citation statements)

References 62 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Furthermore, bLfcin inhibits phosphorylation of the response regulators and of the two-component system's (TCSs) cognate sensor kinases. The role of the TCS is to protect the integrity of bacterial cell membranes against antimicrobial peptides [76]. However, the homologous examination of response regulators and sensor kinases in probiotics, including Bifidobacterium and Lactobacillus, showed that this motif was not present, suggesting that bLfcin may have only marginal effects on the microbioma probiotics in the intestine [76].…”

Section: In Vitro Antibacterial and Anti-fungal Activitymentioning

confidence: 99%

“…The role of the TCS is to protect the integrity of bacterial cell membranes against antimicrobial peptides [76]. However, the homologous examination of response regulators and sensor kinases in probiotics, including Bifidobacterium and Lactobacillus, showed that this motif was not present, suggesting that bLfcin may have only marginal effects on the microbioma probiotics in the intestine [76]. In addition to antimicrobial properties, Lfcin of human and bovine origin has also been found to be effective in inhibiting the classical complement pathway.…”

Section: In Vitro Antibacterial and Anti-fungal Activitymentioning

confidence: 99%

See 1 more Smart Citation

Antimicrobial Activity of Lactoferrin-Related Peptides and Applications in Human and Veterinary Medicine

Bruni¹,

et al. 2016

View full text Add to dashboard Cite

Antimicrobial peptides (AMPs) represent a vast array of molecules produced by virtually all living organisms as natural barriers against infection. Among AMP sources, an interesting class regards the food-derived bioactive agents. The whey protein lactoferrin (Lf) is an iron-binding glycoprotein that plays a significant role in the innate immune system, and is considered as an important host defense molecule. In search for novel antimicrobial agents, Lf offers a new source with potential pharmaceutical applications. The Lf-derived peptides Lf(1-11), lactoferricin (Lfcin) and lactoferrampin exhibit interesting and more potent antimicrobial actions than intact protein.Particularly, Lfcin has demonstrated strong antibacterial, anti-fungal and antiparasitic activity with promising applications both in human and veterinary diseases (from ocular infections to osteo-articular, gastrointestinal and dermatological diseases).

show abstract

Section: In Vitro Antibacterial and Anti-fungal Activitymentioning

confidence: 99%

Section: In Vitro Antibacterial and Anti-fungal Activitymentioning

confidence: 99%

Antimicrobial Activity of Lactoferrin-Related Peptides and Applications in Human and Veterinary Medicine

Bruni¹,

et al. 2016

View full text Add to dashboard Cite

show abstract

“…Lactoferricin B was the first AMP shown to interfere with phosphorylation of the two-component system to suppress bacterial growth (91). It inhibits phosphorylation of the two response regulators by their cognate sensor kinases BasS and CreC.…”

Section: Protein Biosynthesis and Metabolism Inhibitorsmentioning

confidence: 99%

Intracellular Targeting Mechanisms by Antimicrobial Peptides

Fang

Sekaran

2017

Antimicrob Agents Chemother

427

366

View full text Add to dashboard Cite

Antimicrobial peptides (AMPs) are expressed in various living organisms as first-line host defenses against potential harmful encounters in their surroundings. AMPs are short polycationic peptides exhibiting various antimicrobial activities. The principal antibacterial activity is attributed to the membrane-lytic mechanism which directly interferes with the integrity of the bacterial cell membrane and cell wall. In addition, a number of AMPs form a transmembrane channel in the membrane by self-aggregation or polymerization, leading to cytoplasm leakage and cell death. However, an increasing body of evidence has demonstrated that AMPs are able to exert intracellular inhibitory activities as the primary or supportive mechanisms to achieve efficient killing. In this review, we focus on the major intracellular targeting activities reported in AMPs, which include nucleic acids and protein biosynthesis and protein-folding, protease, cell division, cell wall biosynthesis, and lipopolysaccharide inhibition. These multifunctional AMPs could serve as the potential lead peptides for the future development of novel antibacterial agents with improved therapeutic profiles.

show abstract

“…The proteome array that contains ϳ90% of the proteins encoded by the E. coli K12 genome has been constructed. It has been used to investigate DNA damage (19), identify serological biomarkers of inflammatory bowel disease (20), and reveal the inhibition mechanism of lactoferricin B (21). The proteome chip is a good tool to comprehensively screen for bacterial proteins potentially able to interact with fimS or its adjacent regions.…”

Section: Discussionmentioning

confidence: 99%

“…As for bacterial proteome chips, we have previously constructed the E. coli K12 proteome array that contains the proteins encoded in 4256 of the 4288 genes in the E. coli K12 genome (19). This array has been used for investigating DNA damage (19), identifying serological biomarkers of inflammatory bowel disease (20), and revealing the inhibition mechanism of lactoferricin B (21). In the present study, we used the E. coli K12 proteome chip to screen for novel E. coli proteins that can interact with the promotercontaining fimS.…”

mentioning

confidence: 99%

Identification of Bacterial Factors Involved in Type 1 Fimbria Expression using an Escherichia coli K12 Proteome Chip

Chen

Teng

et al. 2014

Molecular & Cellular Proteomics

Self Cite

View full text Add to dashboard Cite

Type 1 fimbriae are filamentous structures on Escherichia coli. These structures are important adherence factors. Because binding to the host cells is the first step of infection, type 1 fimbria is an important virulence factor of pathogenic E. coli. Expression of type 1 fimbria is regulated by a phase variation in which each individual bacterium can alternate between fimbriated (phase-ON) and nonfimbriated (phase-OFF) states. The phase variation is regulated by the flipping of the 314-bp fimS fragment, which contains the promoter driving the expression of the genes required for the synthesis of type 1 fimbria. Thus, the bacterial proteins able to interact with fimS are likely to be involved in regulating the expression of type 1 fimbria. To identify novel type 1 fimbria-regulating factors, we used an E. coli K12 proteome chip to screen for the bacterial factors able to interact with a 602-bp DNA fragment containing fimS and its adjacent regions. The Spr protein was identified by the proteome chip-based screening and further confirmed to be able to interact with fimS by electrophoretic mobility shift assay. Deletion of spr in the neonatal meningitis E. coli strain RS218 significantly increased the ratio of the bacterial colonies that contained the type 1 fimbria phase-ON cells on agar plates. In addition, Spr interfered with the interactions of fimS with the site-specific recombinases, FimB and FimE, which are responsible for mediating the flipping of fimS. These results suggest that Spr is involved in the regulation of type 1 fimbria expression through direct interaction with the invertible element fimS. These findings facilitate our understanding of the regulation of type 1 fimbria. Molecular &

show abstract

Lactoferricin B Inhibits the Phosphorylation of the Two-Component System Response Regulators BasR and CreB

Cited by 41 publications

References 62 publications

Antimicrobial Activity of Lactoferrin-Related Peptides and Applications in Human and Veterinary Medicine

Antimicrobial Activity of Lactoferrin-Related Peptides and Applications in Human and Veterinary Medicine

Intracellular Targeting Mechanisms by Antimicrobial Peptides

Identification of Bacterial Factors Involved in Type 1 Fimbria Expression using an Escherichia coli K12 Proteome Chip

Contact Info

Product

Resources

About