Antibacterial and antibiofilm features of SMAP-18 against .

Cholera continues to be a pointed global health issue, prominently in developing nations, where the disease's severe diarrheal symptoms pose substantial public health risks. With the escalating spread of antibiotic resistance among strains, alternative therapeutic approaches are imperative. Antimicrobial peptides are increasingly recognized for their potential, with research focusing on finding the most effective options.

Multifunctional Properties of BMAP-18 and Its Aliphatic Analog against Drug-Resistant Bacteria.

BMAP-18, derived from the N-terminal region of bovine myeloid antimicrobial peptide BMAP-27, demonstrates potent antimicrobial activity without cytotoxicity. This study aimed to compare the antibacterial, antibiofilm, and anti-inflammatory properties of BMAP-18, rich in aromatic phenylalanine residues, with its aliphatic analog, BMAP-18-FL. Both aromatic BMAP-18 and aliphatic BMAP-18-FL exhibited equally potent antimicrobial activities against Gram-positive and Gram-negative bacteria, particularly methicillin-resistant (MRSA) and multidrug-resistant (MDRPA).

Rationally designed PMAP-23 derivatives with enhanced bactericidal and anticancer activity based on the molecular mechanism of peptide-membrane interactions.

Antimicrobial peptides (AMPs) are a crucial component of the natural defense system that the host employs to protect itself against invading pathogens. PMAP-23, a cathelicidin-derived AMP, has potent and broad-spectrum antimicrobial activity. Our earlier studies led us to hypothesize that PMAP-23 adopts a dynamic helix-hinge-helix structure, initially attaching to membrane surfaces through the N-helix and subsequently inserting the C-helix into the lipid bilayer.

A novel hybrid peptide composed of LfcinB6 and KR-12-a4 with enhanced antimicrobial, anti-inflammatory and anti-biofilm activities.

Hybridizing two known antimicrobial peptides (AMPs) is a simple and effective strategy for designing antimicrobial agents with enhanced cell selectivity against bacterial cells. Here, we generated a hybrid peptide Lf-KR in which LfcinB6 and KR-12-a4 were linked with a Pro hinge to obtain a novel AMP with potent antimicrobial, anti-inflammatory, and anti-biofilm activities. Lf-KR exerted superior cell selectivity for bacterial cells over sheep red blood cells.

The Central PXXP Motif Is Crucial for PMAP-23 Translocation across the Lipid Bilayer.

PMAP-23, a cathelicidin-derived host defense peptide, does not cause severe membrane permeabilization, but exerts strong and broad-spectrum bactericidal activity. We have previously shown that it forms an amphipathic α-helical structure with a central hinge induced by the PXXP motif, which is implicated in the interaction of PMAP-23 with negatively charged bacterial membranes. Here, we studied the potential roles of the PXXP motif in PMAP-23 translocation across the lipid bilayer by replacing Pro residues with either α-helix former Ala (PMAP-PA) or α-helix breaker Gly (PMAP-PG).

Conjugation of Cell-Penetrating Peptides to Antimicrobial Peptides Enhances Antibacterial Activity.

Antimicrobial peptides (AMPs), essential elements in host innate immune defenses against numerous pathogens, have received considerable attention as potential alternatives to conventional antibiotics. Most AMPs exert broad-spectrum antimicrobial activity through depolarization and permeabilization of the bacterial cytoplasmic membrane. Here, we introduce a new approach for enhancing the antibiotic activity of AMPs by conjugation of a cationic cell-penetrating peptide (CPP).

Structural analysis and mode of action of BMAP-27, a cathelicidin-derived antimicrobial peptide.

BMAP-27, a member of cathelicidin family, plays an important role against microorganisms, including bacteria and fungi. BMAP-27 may exert antimicrobial effects through membrane integrity disruption, but the exact molecular mechanism remains unclear. To identify the structural features important for antimicrobial activity and propose a mechanism underlying antibacterial effects, we determined the nuclear magnetic resonance structure of BMAP-27 in a membrane-mimetic environment and investigated its interactions with lipid membranes.

Temperature Change Induces the Expression of vuuA Encoding Vulnibactin Receptor and crp Encoding Cyclic AMP Receptor Protein in Vibrio vulnificus.

Upon entering the human body, Vibrio vulnificus, a gram-negative marine bacterium, must withstand a temperature change (TC) from 25 to 37 °C. This bacterium acquires iron mainly via the vulnibactin receptor (VuuA)-mediated iron uptake system (IUS), which is under the positive control of cyclic AMP receptor protein (CRP), a global regulator responsible for catabolite repression. In this study, we examined the effect of TC on the expression of vuuA and crp, and the reciprocal relation between VuuA-mediated IUS and CRP under iron-limited conditions.

Iron-mediated regulation of metalloprotease VvpE production in Vibrio vulnificus.

In Vibrio vulnificus, the production of metalloprotease VvpE is controlled by Crp (cAMP-receptor protein) and SmcR (a quorum sensing regulator) at the transcription level, and by PilD-mediated type II general secretion system (TTGSS) at the extracellular secretion level. Iron is known to stimulate VvpE production but the related mechanisms remain unidentified. Iron stimulated vvpE transcription and extracellular VvpE production even in the background with a crp and/or smcR mutation.

Scrub typhus hepatitis confirmed by immunohistochemical staining.

Scrub typhus is an acute febrile disease caused by Orientia tsutsugamushi (O. tsutsugamushi). We report herein the case of a woman who presented with fever and elevated serum levels of liver enzymes and who was definitively diagnosed with scrub typhus by histopathological examination of liver biopsy specimens, serological tests and nested polymerase chain reaction.

Cyclic AMP and cyclic AMP-receptor protein modulate the autoinducer-2-mediated quorum sensing system in Vibrio vulnificus.

This study was undertaken to determine whether cyclic AMP (cAMP) or cAMP-receptor protein (CRP) modulates the activity of the autoinducer (AI)-2-mediated quorum sensing (QS) system in response to glucose availability in Vibrio vulnificus. A mutation in crp impaired V. vulnificus growth, decreased AI-2 production, and repressed the expression of smcR encoding the master regulator SmcR (a Vibrio harveyi LuxR homolog) of the AI-2-QS system, and these changes were prevented by in trans complementation of wild-type crp.

Cyclic AMP-receptor protein activates aerobactin receptor IutA expression in Vibrio vulnificus.

The ferrophilic bacterium Vibrio vulnificus can utilize the siderophore aerobactin of Escherichia coli for iron acquisition via its specific receptor IutA. This siderophore piracy by V. vulnificus may contribute to its survival and proliferation, especially in mixed bacterial environments.

Differences in clinical features according to Boryoung and Karp genotypes of Orientia tsutsugamushi.

Background: Scrub typhus is an infectious disease caused by Orientia tsutsugamushi. The differences in virulence of O. tsutsugamushi prototypes in humans are still unknown.

Modulation of iron-uptake systems by a mutation of luxS encoding an autoinducer-2 synthase in Vibrio vulnificus.

Vibrio vulnificus possesses multiple iron-uptake systems which are mediated by VuuA (vulnibactin receptor), IutA (aerobactin receptor) and HupA (heme receptor). In this study, we determined the effect of a mutation of luxS encoding autoinducer-2 (AI-2) synthase on the expressions of the three receptors. A mutation and an in trans complementation of luxS did not affect the growing ability of V.

Virulence characteristics of sucrose-fermenting Vibrio vulnificus strains.

We identified 6 sucrose-fermenting Vibrio vulnificus strains and examined their virulence characteristics. They were all encapsulated, motile, capable of producing toxins and utilizing transferrin-bound iron, cytotoxic to cultured cells, and virulent enough to kill mice. They could be definitely identified only by genetic identification methods such as PCR, and not by conventional culture-based identification methods such as API 20E (bioMérieux, France).

Regulation of the Vibrio vulnificus vvpE expression by cyclic AMP-receptor protein and quorum-sensing regulator SmcR.

In Vibrio vulnificus, cAMP-receptor protein (CRP) and the quorum-sensing regulator SmcR are simultaneously and cooperatively required for the metalloprotease vvpE gene expression, rather than sequentially in a regulatory cascade. However, this study shows a new temporal and functional sequence between the two factors in regulating vvpE expression. A crp mutation inhibited vvpE expression with growth impairment from early stage.

Iron differentially regulates gene expression and extracellular secretion of Vibrio vulnificus cytolysin-hemolysin.

In a previous study, we showed that Vibrio vulnificus is a ferrophilic bacterium that requires high levels of available iron for growth. In the present study, we show that iron stimulates, in an unusual manner, the production of cytolysin-hemolysin (VvhA), the most potent exotoxin produced by V. vulnificus.

Effect of iron-chelator deferiprone on the in vitro growth of staphylococci.

The standard iron-chelator deferoxamine is known to prevent the growth of coagulase-negative staphylococci (CoNS) which are major pathogens in iron-overloaded patients. However, we found that deferoxamine rather promotes the growth of coagulase-positive Staphylococcus aureus. Accordingly, we tested whether deferiprone, a new clinically-available iron-chelator, can prevent the growth of S.

Two forms of Vibrio vulnificus metalloprotease VvpE are secreted via the type II general secretion system.

Vibrio vulnificus has been known to secrete one form of metalloprotease VvpE (45 kDa) that is cleaved to 34 kDa-VvpE and 11 kDa-C-terminal propeptide via extracellular autoproteolysis. However, we found that extracellular secretion of both the 34 and 45 kDa forms of VvpE began in the early growth phase; moreover, 34 kDa-VvpE existed as the major form in V. vulnificus cell lysates and culture supernatants.

Identification of an atypical integron carrying an IS26-disrupted aadA1 gene cassette in Acinetobacter baumannii.

An unusual class 1 integron was identified that carries an IS26-disrupted aadA1 gene cassette (designated as 'integron-IS26') in an imipenem-resistant Acinetobacter baumannii (IRAB) outbreak strain. DNA sequencing revealed that integron-IS26 contained two gene cassettes, the aac(6')-Im cassette and a peculiar aadA1 cassette that was disrupted by IS26 (disrupted aadA1 cassette). Southern blotting localised integron-IS26 to the chromosome.

A widespread deferoxamine-mediated iron-uptake system in Vibrio vulnificus.

Vibrio vulnificus can use the standard iron chelator deferoxamine (Desferal) for efficient iron-uptake via the specific receptor DesA, which is encoded by desA. We investigated the ubiquity of the deferoxamine-mediated iron-uptake system in V. vulnificus strains and the potential risk of the system.

Production of Vibrio vulnificus metalloprotease VvpE begins during the early growth phase: usefulness of gelatin-zymography.

Recent studies have demonstrated that expression of the vvpE gene begins during the early growth phase albeit at low levels. However, we found that the traditional protease assay method that is used to measure caseinolytic activity in culture supernatants is not suitable for the measurement of extracellular VvpE that is produced at low levels during the early growth phase. By using gelatin-zymography in place of the protease assay, we could specifically detect only VvpE of several proteases produced by Vibrio vulnificus.

Vibrio vulnificus metalloprotease VvpE is essentially required for swarming.

Bacterial swarming constitutes a good in vitro model for surface adherence and colonization, and is accompanied by expressions of virulence factors related to invasiveness. In this study, it was determined that Vibrio vulnificus swarming was abolished by mutation of the vvpE gene encoding a metalloprotease VvpE and this swarming defect was recovered by complementation of the vvpE gene. Expression of the vvpE gene began simultaneously with the beginning of swarming and increased along with expression of the luxS gene encoding the synthase of the precursor of quorum-sensing signal molecule autoinducer 2, and this increased vvpE expression was decreased by mutation of the luxS gene.