Penaeidins, a family of antimicrobial peptides from penaeid shrimp (Crustacea, Decapoda)

Destoumieux, Delphine; Muñoz, Marcelo; Bulet, Philippe; Bachère, Evelyne

doi:10.1007/pl00000764

Cited by 175 publications

(113 citation statements)

References 74 publications

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“…3) by a dipeptidyl aminopeptidase. This latter mechanism has been reported for other antimicrobial peptides such as cecropin (34) or penaeidin (35). Gambicin exists in an oxidized and a nonoxidized form; the former shows significantly higher bacteriocidal activity.…”

Section: Discussionsupporting

confidence: 64%

Gambicin: A novel immune responsive antimicrobial peptide from the malaria vector Anopheles gambiae

Vizioli

Bulet

Hoffmann

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

178

136

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A novel mosquito antimicrobial peptide, gambicin, and the corresponding gene were isolated in parallel through differential display-PCR, an expressed sequence tag (EST) project, and characterization of an antimicrobial activity in a mosquito cell line by reverse-phase chromatography. The 616-bp gambicin ORF encodes an 81-residue protein that is processed and secreted as a 61-aa mature peptide containing eight cysteines engaged in four disulfide bridges. Gambicin lacks sequence homology with other known proteins. Like other Anopheles gambiae antimicrobial peptide genes, gambicin is induced by natural or experimental infection in the midgut, fatbody, and hemocyte-like cell lines. Within the midgut, gambicin is predominantly expressed in the anterior part. Both local and systemic gambicin expression is induced during early and late stages of natural malaria infection. In vitro experiments showed that the 6.8-kDa mature peptide can kill both Gram-positive and Gram-negative bacteria, has a morphogenic effect on a filamentous fungus, and is marginally lethal to Plasmodium berghei ookinetes. An oxidized form of gambicin isolated from the cell line medium was more active against bacteria than the nonoxidized form from the same medium.Anopheles gambiae ͉ antimicrobial peptide ͉ innate immunity ͉ malaria

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Section: Discussionsupporting

confidence: 64%

Gambicin: A novel immune responsive antimicrobial peptide from the malaria vector Anopheles gambiae

Vizioli

Bulet

Hoffmann

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

178

136

View full text Add to dashboard Cite

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“…Similar immune responses occurred in shrimp. However, some pre-synthetized AMPs, such as penaeidins, stored in hemocytes could be released upon immune stimulation (50). Therefore, we performed an initial challenge and then made a second challenge against S. aureus in the bacterial clearance assay (see under "Experimental Procedures").…”

Section: Discussionmentioning

confidence: 99%

β-Arrestins Negatively Regulate the Toll Pathway in Shrimp by Preventing Dorsal Translocation and Inhibiting Dorsal Transcriptional Activity

Sun

Lan

Shi

et al. 2016

Journal of Biological Chemistry

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The Toll signaling pathway plays an important role in the innate immunity of Drosophila melanogaster and mammals. The activation and termination of Toll signaling are finely regulated in these animals. Although the primary components of the Toll pathway were identified in shrimp, the functions and regulation of the pathway are seldom studied. We first demonstrated that the Toll signaling pathway plays a central role in host defense against Staphylococcus aureus by regulating expression of antimicrobial peptides in shrimp. We then found that ␤-arrestins negatively regulate Toll signaling in two different ways. ␤-Arrestins interact with the C-terminal PEST domain of Cactus through the arrestin-N domain, and Cactus interacts with the RHD domain of Dorsal via the ankyrin repeats domain, forming a heterotrimeric complex of ␤-arrestin⅐Cactus⅐ Dorsal, with Cactus as the bridge. This complex prevents Cactus phosphorylation and degradation, as well as Dorsal translocation into the nucleus, thus inhibiting activation of the Toll signaling pathway. ␤-Arrestins also interact with non-phosphorylated ERK (extracellular signal-regulated protein kinase) through the arrestin-C domain to inhibit ERK phosphorylation, which affects Dorsal translocation into the nucleus and phosphorylation of Dorsal at Ser 276 that impairs Dorsal transcriptional activity. Our study suggests that ␤-arrestins negatively regulate the Toll signaling pathway by preventing Dorsal translocation and inhibiting Dorsal phosphorylation and transcriptional activity.

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“…Penaedins are antimicrobial peptides found in various species of shrimp. They contain a 26-residue, chitin-binding C-terminal domain (CACYRLSVS DARNCCIKFGSCCHLVK-NH 2 ), the six cysteines of which form three intramolecular disulfide bonds (88,89).…”

Section: Discussionmentioning

confidence: 99%

Multivalent Binding of Carbohydrates by the Human α-Defensin, HD5

Lehrer

Jung

Ruchala

et al. 2009

The Journal of Immunology

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Four of the six human α-defensins (human neutrophil peptides 1–3 and human α-defensin 5; HD5) have a lectin-like ability to bind glycosylated proteins. Using HD5 as a model, we applied surface plasmon resonance techniques to gain insights into this property. HD5 bound natural glycoproteins > neoglycoproteins based on BSA > nonglycosylated BSA ≫ free sugars. The affinity of HD5 for simple sugars covalently bound to BSA was orders of magnitude greater than its affinity for the same sugars in solution. The affinity of HD5 for protein-bound carbohydrates resulted from multivalent interactions which may also involve noncarbohydrate residues of the proteins. HD5 showed concentration-dependent self-association that began at submicromolar concentrations and proceeded to dimer and tetramer formation at concentrations below 5 μM. The (R9A, R28A) and (R13A, R32A) analogs of HD5 showed greatly reduced self-association as well as minimal binding to BSA and to BSA-affixed sugars. From this and other evidence, we conclude that the extensive binding of HD5 to (neo)glycoproteins results from multivalent nonspecific interactions of individual HD5 molecules with carbohydrate and noncarbohydrate moieties of the target molecule and that the primary binding events are magnified and enhanced by subsequent in situ assembly and oligomerization of HD5. Self-association and multivalent binding may play integral roles in the ability of HD5 to protect against infections caused by viruses and other infectious agents.

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Penaeidins, a family of antimicrobial peptides from penaeid shrimp (Crustacea, Decapoda)

Cited by 175 publications

References 74 publications

Gambicin: A novel immune responsive antimicrobial peptide from the malaria vector Anopheles gambiae

Gambicin: A novel immune responsive antimicrobial peptide from the malaria vector Anopheles gambiae

β-Arrestins Negatively Regulate the Toll Pathway in Shrimp by Preventing Dorsal Translocation and Inhibiting Dorsal Transcriptional Activity

Multivalent Binding of Carbohydrates by the Human α-Defensin, HD5

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