NMR structure of <i>r</i>ALF‐<i>Pm3</i>, an anti‐lipopolysaccharide factor from shrimp: Model of the possible lipid A‐binding site

Yang, Yinshan; Boze, Hélène; Chemardin, Patrick; Padilla, André; Moulin, Gabrielle; Tassanakajon, Anchalee; Pugnière, Martine; Roquet, Françoise; Destoumieux-Garzón, Delphine; Gueguen, Yannick; Bachère, Evelyne; Aumelas, André

doi:10.1002/bip.21119

Cited by 80 publications

(67 citation statements)

References 56 publications

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“…Unfortunately, we were unable to determine those molecular determinants by NMR due to the insolubility of the Cg-Defh2-lipid II complex in aqueous buffer. Such an insolubility was previously reported for another invertebrate AMP referred to as anti-lipopolysaccharide factor, which precipitated when incubated in presence of lipid A, used as a docking molecule at the surface of Gram-negative bacteria (37). Such precipitations can result from the hiding of the peptide charges at the peptide-lipid interface of the complex giving rise to an unfavorable pI value for the solubility of the complex.…”

Section: Discussionsupporting

confidence: 52%

Insight into Invertebrate Defensin Mechanism of Action

Schmitt

Wilmes

Pugnière

et al. 2010

Journal of Biological Chemistry

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121

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Three oyster defensin variants (Cg-Defh1, Cg-Defh2, and CgDefm) were produced as recombinant peptides and characterized in terms of activities and mechanism of action. In agreement with their spectrum of activity almost specifically directed against Gram-positive bacteria, oyster defensins were shown here to be specific inhibitors of a bacterial biosynthesis pathway rather than mere membrane-active agents. Indeed, at lethal concentrations, the three defensins did not compromise Staphylococcus aureus membrane integrity but inhibited the cell wall biosynthesis as indicated by the accumulation of the UDP-Nacetylmuramyl-pentapeptide cell wall precursor. In addition, a combination of antagonization assays, thin layer chromatography, and surface plasmon resonance measurements showed that oyster defensins bind almost irreversibly to the lipid II peptidoglycan precursor, thereby inhibiting the cell wall biosynthesis. To our knowledge, this is the first detailed analysis of the mechanism of action of antibacterial defensins produced by invertebrates. Interestingly, the three defensins, which were chosen as representative of the oyster defensin molecular diversity, bound differentially to lipid II. This correlated with their differential antibacterial activities. From our experimental data and the analysis of oyster defensin sequence diversity, we propose that oyster defensin activity results from selective forces that have conserved residues involved in lipid II binding and diversified residues at the surface of oyster defensins that could improve electrostatic interactions with the bacterial membranes.

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Section: Discussionsupporting

confidence: 52%

Insight into Invertebrate Defensin Mechanism of Action

Schmitt

Wilmes

Pugnière

et al. 2010

Journal of Biological Chemistry

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121

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“…Most ALFs bind to Lipid A from Gram-negative bacteria, but they can also interact with lipoteichoic acid (LTA) from Grampositive bacteria [62] and b-glucan from fungi [63]. The known three-dimensional structures of ALFs consist of three a-helices (one at the N-terminus and two at the C-terminus) packed against a four-stranded b-sheet (table 1) [61,64].…”

Section: (B) Gene-encoded Amps From Penaeid Shrimp (I) Penaeidinsmentioning

confidence: 99%

Antimicrobial peptides in marine invertebrate health and disease

Destoumieux-Garzón

Rosa

Schmitt

et al. 2016

Phil. Trans. R. Soc. B

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116

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One contribution of 13 to a theme issue 'Evolutionary ecology of arthropod antimicrobial peptides'. Aquaculture contributes more than one-third of the animal protein from marine sources worldwide. A significant proportion of aquaculture products are derived from marine protostomes that are commonly referred to as 'marine invertebrates'. Among them, penaeid shrimp (Ecdysozosoa, Arthropoda) and bivalve molluscs (Lophotrochozoa, Mollusca) are economically important. Mass rearing of arthropods and molluscs causes problems with pathogens in aquatic ecosystems that are exploited by humans. Remarkably, species of corals (Cnidaria) living in non-exploited ecosystems also suffer from devastating infectious diseases that display intriguing similarities with those affecting farmed animals. Infectious diseases affecting wild and farmed animals that are present in marine environments are predicted to increase in the future. This paper summarizes the role of the main pathogens and their interaction with host immunity, with a specific focus on antimicrobial peptides (AMPs) and pathogen resistance against AMPs. We provide a detailed review of penaeid shrimp AMPs and their role at the interface between the host and its resident/pathogenic microbiota. We also briefly describe the relevance of marine invertebrate AMPs in an applied context. This article is part of the themed issue 'Evolutionary ecology of arthropod antimicrobial peptides'.

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“…2). The conserved region is believed to be essential for the antimicrobial activity and for the stability of the 3D structure of ALFs (Yang et al, 2009).…”

Section: Resultsmentioning

confidence: 99%

Two isoforms of anti-lipopolysaccharide factors identified and characterized from the hemocytes of portunid crabs, Portunus pelagicus and Scylla tranquebarica

Afsal

Antony

Chaithanya

et al. 2012

Molecular Immunology

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a b s t r a c tAnti-lipopolysaccharide factors (ALFs), a type of cationic antimicrobial peptides (AMPs), and their derivatives are becoming predominant candidates for potential drugs in viral and bacterial diseases. This study reports the first ALF from the mud crab Scylla tranquebarica (StALF, JQ899453) and the second ALF isoform from the blue swimmer crab Portunus pelagicus (PpALF2, JQ899452). Both sequences encoded for precursor molecules, starting with a signal peptide containing 26 amino acid residues, followed by a highly cationic mature peptide, containing two conserved cysteine residues flanking a putative lipopolysaccharide (LPS)-binding domain. BLAST analysis revealed that both PpALF2 and StALF exhibited significant similarity with crustacean ALF sequences. The predicted molecular mass of the mature ALFs was 11.2 kDa with an estimated pI of 10.0. PpALF2 and StALF also showed the typical pattern of alternating hydrophobic and hydrophilic residues in their putative disulphide loop, suggesting that they comprise the same functional domain. Phylogenetic analysis showed that PpALF2 and StALF have similar evolutionary status and they were phylogenetically ancient immune effector molecules which may play an essential role in the host defense mechanism. The spatial structures of PpALF2 and StALF possessed four beta-strands and two alpha-helices. The results indicated that there were more than one ALF involved in crab immunity against various pathogens. ALFs would provide candidate promising therapeutic or prophylactic agents in health management and diseases control in crustacean aquaculture.

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NMR structure of rALF‐Pm3, an anti‐lipopolysaccharide factor from shrimp: Model of the possible lipid A‐binding site

Cited by 80 publications

References 56 publications

Insight into Invertebrate Defensin Mechanism of Action

Insight into Invertebrate Defensin Mechanism of Action

Antimicrobial peptides in marine invertebrate health and disease

Two isoforms of anti-lipopolysaccharide factors identified and characterized from the hemocytes of portunid crabs, Portunus pelagicus and Scylla tranquebarica

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