Lipopolysaccharide (LPS) detoxification of analogue peptides derived from limulus anti-LPS factor

Ren, Jiandong; Gao, Hongfu; Tang, Min; Gu, Jiande; Xia, Peiyuan; Xiao, Guangxia

doi:10.1016/j.peptides.2010.07.004

Cited by 19 publications

(13 citation statements)

References 23 publications

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“…Some AMPs have been shown to bind to LPS and neutralize LPS-stimulated proinflammatory responses (13)(14)(15). Related to this, different studies have shed light on AMPs with antiendotoxin properties (13,14,(16)(17)(18)(19)(20)(21)(22)(23)(24). However, the rules governing the design of AMPs with antiendotoxin properties are still not very clear (13)(14)(15).…”

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confidence: 99%

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Ultrashort Antimicrobial Peptides with Antiendotoxin Properties

Chih

Lin

Yip

et al. 2015

Antimicrob Agents Chemother

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bRelease of lipopolysaccharide (LPS) (endotoxin) from bacteria into the bloodstream may cause serious unwanted stimulation of the host immune system. Some but not all antimicrobial peptides can neutralize LPS-stimulated proinflammatory responses. Salt resistance and serum stability of short antimicrobial peptides can be boosted by adding ␤-naphthylalanine to their termini. Herein, significant antiendotoxin effects were observed in vitro and in vivo with the ␤-naphthylalanine end-tagged variants of the short antimicrobial peptides S1 and KWWK.

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confidence: 99%

“…The ability of LPS neutralization in vitro was measured by a limulus amebocyte lysate (LAL) assay (Cape Cod Inc., USA) (19,23). Peptides at concentrations of 12.5, 25, 50, 100, or 200 g/ml were incubated with 5 endotoxin units (EU) of LPS in 96-well plates at 37°C.…”

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confidence: 99%

Ultrashort Antimicrobial Peptides with Antiendotoxin Properties

Chih

Lin

Yip

et al. 2015

Antimicrob Agents Chemother

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“…It has also been reported that CLP19 is able to reduce secretion of TNF-α from PBMCs stimulated with LPS in the presence of human serum [65], and to block LPS induced phosphorylation of the MAPK signaling proteins p38, ERK1/2, ABD and JNK1/2 in PBMCs [65]. In addition, two analogs of CRP19, CRP19-1 (CRKPTFRRLKWKIKGKFKC) and CRP19-2 (CRKPTFRRLKWKYKGKFKC), were synthesized to assess the effect of altering the hydrophobicity of the parent molecule [66]. The order of hydrophobicity was CRP-19 > CRP19-1 > CRP19-2.…”

Section: Anti-lps Factorsmentioning

confidence: 99%

The Role of Biophysical Parameters in the Antilipopolysaccharide Activities of Antimicrobial Peptides from Marine Fish

2014

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Numerous antimicrobial peptides (AMPs) from marine fish have been identified, isolated and characterized. These peptides act as host defense molecules that exert antimicrobial effects by targeting the lipopolysaccharide (LPS) of Gram-negative bacteria. The LPS-AMP interactions are driven by the biophysical properties of AMPs. In this review, therefore, we will focus on the physiochemical properties of AMPs; that is, the contributions made by their sequences, net charge, hydrophobicity and amphipathicity to their mechanism of action. Moreover, the interactions between LPS and fish AMPs and the structure of fish AMPs with LPS bound will also be discussed. A better understanding of the biophysical properties will be useful in the design of AMPs effective against septic shock and multidrug-resistant bacterial strains, including those that commonly produce wound infections.

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“…Functional characterization of ALFs has been conducted by chemically synthesizing the LPS domain region, [16][17][18][19][20][21][22] and by recombinant expression of mature peptides. 9,13,[23][24][25][26][27][28] Biological activity reported so far for ALFs include antibacterial, 6,9,20 antifungal, 6,27 antiviral, 29,30 immunomodulatory, 31 antitumor, 32 anti-inflammatory, and antiprotozoal activity.…”

Section: Introductionmentioning

confidence: 99%

“…21 Using homology modeling with the template recombinant-ALF-Pm3 (SMTL id: 2job.1) NMR structure (chosen for its shared similarity of 38.61%), prediction of the spatial 3D structure of Cf-ALF1 demonstrated the presence of three α-helices packed against four strands of β-sheets (Figure 4). Somboonwiwat et al studied and elucidated the functional role of recombinant-ALF-Pm3 expressed in the Pichia pastoris system, and demonstrated a comprehensive spectrum of activity against the filamentous fungi, and both Gram-positive and Gram-negative bacteria.…”

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confidence: 99%

Molecular characterization and phylogenetic analysis of an anti-lipopolysaccharide factor from the crucifix crab, Charybdis feriatus

Sruthy¹,

Nair²,

Cubelio³

et al. 2015

OAAP

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Antimicrobial peptides are small cationic, gene-encoded, amphipathic, host defense peptides with a ubiquitous distribution in all living kingdoms. They are ,10 kDa in size, with 15-100 amino acids having a net positive charge of +2 to +9. Anti-lipopolysaccharide factor (ALF) is a cationic antimicrobial peptide which constitutes one of the key effector molecules in the innate immune system of crustaceans, and is capable of binding and neutralizing lipopolysaccharides. In the present study, an ALF homolog (Charybdis feriatus [Cf]-ALF1)-encoding cDNA sequence from the hemocytes of the crucifix crab, C. feriatus, was cloned, identified, and characterized. The deduced peptide of Cf-ALF1 encoded for a 123 amino acid peptide with a 97 residue mature peptide (11.16 kDa) that had a net charge of +10. Two conserved cysteine residues and a putative lipopolysaccharide binding domain were observed in the Cf-ALF1 mature peptide. BLAST analysis of Cf-ALF1 nucleotides showed a 99% similarity to Scylla serrata. The spatial structure of Cf-ALF1 was composed of three α-helices packed against a four-strand β-sheet. Two of these helices were linked by a disulfide bond to form an amphipathic loop similar to the structure of anti-lipopolysaccharide factor isoform 3 from Penaeus monodon (ALF-Pm3). All these features suggest that Cf-ALF1 could play a significant role in the innate immune defense mechanism of C. feriatus.

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Lipopolysaccharide (LPS) detoxification of analogue peptides derived from limulus anti-LPS factor

Cited by 19 publications

References 23 publications

Ultrashort Antimicrobial Peptides with Antiendotoxin Properties

Ultrashort Antimicrobial Peptides with Antiendotoxin Properties

The Role of Biophysical Parameters in the Antilipopolysaccharide Activities of Antimicrobial Peptides from Marine Fish

Molecular characterization and phylogenetic analysis of an anti-lipopolysaccharide factor from the crucifix crab, Charybdis feriatus

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