Cysteine‐rich antimicrobial peptides in invertebrates

Dimarcq, Jean‐Luc; Bulet, Philippe; Hétru, Charles; Hoffmann, Jules A.

doi:10.1002/(sici)1097-0282(1998)47:6<465::aid-bip5>3.0.co;2-#

Cited by 236 publications

(163 citation statements)

References 94 publications

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“…Generally, mammalian defensins can be grouped into three subfamilies designated α, β, and the cyclic θ defensins (Wong et al, 2007). Both α and β defensins adopt a triple stranded antiparallel β-sheet structure, while defensins from invertebrates and plants contain an α-helix that is disulphide-linked to an antiparallel two-stranded β-sheet with a cysteine-stabilized α-helix/β-sheet motif (CSαβ) (Dimarcq et al, 1998). This motif is widespread in arthropod and mollusk defensins…”

Section: Introductionmentioning

confidence: 99%

A defensin from clam Venerupis philippinarum: Molecular characterization, localization, antibacterial activity, and mechanism of action

Zhang

Yang

Wang

et al. 2015

Developmental & Comparative Immunology

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A B S T R A C TAntimicrobial peptides (AMPs) are important mediators of the primary host defense system against microbial invasion. In the present study, we cloned and characterized a member of the invertebrate defensin from the clam Venerupis philippinarum, designated VpDef. Amino acid sequence analysis showed that VpDef was similar to defensins from marine mollusks and ticks. In non-stimulated clams, RT-PCR and immunohistochemical analysis revealed that both VpDef mRNA and the encoding peptide were constitutively expressed in hemocytes and mantles, as well as in other major tissues. VpDef transcripts were significantly induced in hemocytes at different time intervals post Vibrio anguillarum infection. The recombinant VpDef (rVpDef) showed the highest activity against Gram-positive bacteria Micrococcus luteus and less effective to Gram-negative bacteria. In addition, incubation of rVpDef with M. luteus at 1 × and 3 × MIC could induce an obvious decrease of the membrane potential and notable changes of membrane permeability in a dose-dependent manner. Membrane integrity and bacterial viability analysis also revealed that rVpDef increased the membrane permeability of M. luteus and then resulted in cell death at 2 × and 10 × MIC. Overall, these results suggest that VpDef has an important function in host defense against invasive pathogens, probably killing microbes by inducing membrane lesions.

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Section: Introductionmentioning

confidence: 99%

A defensin from clam Venerupis philippinarum: Molecular characterization, localization, antibacterial activity, and mechanism of action

Zhang

Yang

Wang

et al. 2015

Developmental & Comparative Immunology

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“…Antimicrobial peptides (AMPs), widely distributed in the whole living kingdom, play an important role in the immunological defense especially in those organisms which lack adaptive immunity (Boman 1995;Dimarcq et al 1998;Hancock and Lehrer 1998;Zasloff 2002;Otvos 2002;Bulet et al 2004). AMPs are promptly synthesized at low metabolic cost, easily stored in large amounts and readily available shortly after an infection, to rapidly kill a broad range of microbes (Hancock 1997(Hancock , 2001Prenner et al 1999a,b).…”

Section: Introductionmentioning

confidence: 99%

Molecular characterization of a crustin-like antimicrobial peptide in the giant tiger shrimp, Penaeus monodon, and its expression profile in response to various immunostimulants and challenge with WSSV

et al. 2011

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a b s t r a c tA crustin-like antimicrobial peptide from the haemocytes of giant tiger shrimp, Penaeus monodon was partially characterized at the molecular level and phylogenetic analysis was performed. The partial coding sequence of 299 bp and 91 deduced amino acid residues possessed conserved cysteine residues characteristic of the shrimp crustins. Phylogenetic tree and sequence comparison clearly confirmed divergence of this crustin-like AMP from other shrimp crustins. The differential expression of the crustin-like AMP in P. monodon in response to the administration of various immunostimulants viz., two marine yeasts (Candida haemulonii S27 and Candida sake S165) and two ␤-glucan isolates (extracted from C. haemulonii S27 and C. sake S165) were noted during the study. Responses to the application of two gram-positive probiotic bacteria (Bacillus MCCB101 and Micrococcus MCCB104) were also observed. The immune profile was recorded pre-and post-challenge white spot syndrome virus (WSSV) by semi-quantitative RT-PCR. Expressions of seven WSSV genes were also observed for studying the intensity of viral infection in the experimental animals. The crustin-like AMP was found to be constitutively expressed in the animal and a significant down-regulation could be noted post-challenge WSSV. Remarkable down-regulation of the gene was observed in the immunostimulant fed animals pre-challenge followed by a significant up-regulation post-challenge WSSV. Tissue-wise expression of crustin-like AMP on administration of C. haemulonii and Bacillus showed maximum transcripts in gill and intestine. The marine yeast, C. haemulonii and the probiotic bacteria, Bacillus were found to enhance the production of crustin-like AMP and confer significant protection to P. monodon against WSSV infection.

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“…This variation does not seem to affect the cleavage site at position 21. Glycine is the most common residue identified at this position in carcinin, and is often the first residue in the mature fragment of several AMPs (Tossi et al, 2000), particularly in arthropods (Dimarcq et al, 1998). The carcinin protein fragment sequenced by Relf et al (1999) identified an asparagine (N) residue at position 26.…”

Section: Aj786653) Into a Family Of Related Proteins (Prodom Accessiomentioning

confidence: 99%

Gene characterisation, isoforms and recombinant expression of carcinin, an antibacterial protein from the shore crab, Carcinus maenas

Brockton

Hammond

Smith

2007

Molecular Immunology

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Carcinin is a whey acidic protein (WAP) domain-containing antimicrobial protein, produced by the circulating haemocytes of the shore crab, Carcinus maenas. Cloning of its full coding cDNA reveals that it shows some similarity to invertebrate defensins and has a valine-rich signal sequence followed by a defined cleavage site but no obvious acidic anionic 'pro' sequence. The C-terminus exhibits a unique cysteine array that is predicted to form 6 disulphide bonds in the tertiary structure. This 12 cysteine array arrangement is conserved in ESTs from related genera and seems to represent a novel tertiary structure amongst AMPs, unique to the Crustacea. There are at least 5 putative isoforms of the mature protein that may arise through the transcription of one or two alleles of a multi-exon gene. Several of the same transcripts have been found in different animals. These isoforms do not arise as a result of alternate splicing of the exons, but by the transcription of different alleles and /or single point mutation of the transcript at up to four loci in the gene. The most commonly expressed transcript of the protein was recombinantly expressed in bacterial fusion system to a yield of ca 2-3 µg ml -1 of culture. In vitro expression with or without the leader sequence confirms the bioinformatic prediction that the stability of the mature protein is reduced when the leader sequence is removed. Carcinin is one of very few invertebrate AMPs characterised at the gene, transcript and protein level and to be recombinantly expressed in vitro in a bacterial system.

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Cysteine‐rich antimicrobial peptides in invertebrates

Cited by 236 publications

References 94 publications

A defensin from clam Venerupis philippinarum: Molecular characterization, localization, antibacterial activity, and mechanism of action

A defensin from clam Venerupis philippinarum: Molecular characterization, localization, antibacterial activity, and mechanism of action

Molecular characterization of a crustin-like antimicrobial peptide in the giant tiger shrimp, Penaeus monodon, and its expression profile in response to various immunostimulants and challenge with WSSV

Gene characterisation, isoforms and recombinant expression of carcinin, an antibacterial protein from the shore crab, Carcinus maenas

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