Panusin represents a new family of β-defensin-like peptides in invertebrates

Montero-Alejo, Vivian; Corzo, Gerardo; Porro-Suardíaz, Javier; Pardo-Ruíz, Zenia; Perera, Erick; Rodríguez-Viera, Leandro; Sánchez-Díaz, Gabriela; Hernández-Rodríguez, Erix W.; Álvarez, Carlos; Peigneur, Steve; Tytgat, Jan; Perdomo-Morales, Rolando

doi:10.1016/j.dci.2016.09.002

Cited by 20 publications

(27 citation statements)

References 59 publications

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“…The only other known case of peptides bearing a β-defensinlike cysteine array in Ecdysozoa is that of panusins, a family of HDPs which have been first identified in a crustacean, the spiny lobster Panulirus spp. (27,28). In spite of a significant primary sequence homology with the C-terminal domain of big defensins, panusins are completely devoid of the N-terminal region and more closely resemble the architecture of vertebrate β-defensins.…”

Section: Preamblementioning

confidence: 99%

Functional Insights From the Evolutionary Diversification of Big Defensins

et al. 2020

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Big defensins are antimicrobial polypeptides believed to be the ancestors of β-defensins, the most evolutionary conserved family of host defense peptides (HDPs) in vertebrates. Nevertheless, big defensins underwent several independent gene loss events during animal evolution, being only retained in a limited number of phylogenetically distant invertebrates. Here, we explore the evolutionary history of this fascinating HDP family and investigate its patchy distribution in extant metazoans. We highlight the presence of big defensins in various classes of lophotrochozoans, as well as in a few arthropods and basal chordates (amphioxus), mostly adapted to life in marine environments. Bivalve mollusks often display an expanded repertoire of big defensin sequences, which appear to be the product of independent lineage-specific gene tandem duplications, followed by a rapid molecular diversification of newly acquired gene copies. This ongoing evolutionary process could underpin the simultaneous presence of canonical big defensins and non-canonical (β-defensin-like) sequences in some species. The big defensin genes of mussels and oysters, two species target of in-depth studies, are subjected to gene presence/absence variation (PAV), i.e., they can be present or absent in the genomes of different individuals. Moreover, big defensins follow different patterns of gene expression within a given species and respond differently to microbial challenges, suggesting functional divergence. Consistently, current structural data show that big defensin sequence diversity affects the 3D structure and biophysical properties of these polypeptides. We discuss here the role of the N-terminal hydrophobic domain, lost during evolution toward β-defensins, in the big defensin stability to high salt concentrations and its mechanism of action. Finally, we discuss the potential of big defensins as markers for animal health and for the nature-based design of novel therapeutics active at high salt concentrations.

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Section: Preamblementioning

confidence: 99%

Functional Insights From the Evolutionary Diversification of Big Defensins

et al. 2020

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“…The cis-defensin superfamily (present in insects, fungi and plants), has the central beta-strand stabilised by disulphide bridges, connected to the same alpha-helix in the "cis" orientation. This is in contrast to the vertebrate (and some invertebrate) defensins, in which the central beta strand has disulphide bridges that stabilise structures in non-cis or "trans" orientations (3,4). Both cis and trans families have undergone rapid expansion and evolutionary change to reveal a repertoire of diverse functions that are only recently becoming clear (5).…”

Section: Introductionmentioning

confidence: 99%

The Dichotomous Responses Driven by β-Defensins

2020

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Defensins are short, rapidly evolving, cationic antimicrobial host defence peptides with a repertoire of functions, still incompletely realised, that extends beyond direct microbial killing. They are released or secreted at epithelial surfaces, and in some cases, from immune cells in response to infection and inflammation. Defensins have been described as endogenous alarmins, alerting the body to danger and responding to inflammatory signals by promoting both local innate and adaptive systemic immune responses. However, there is now increasing evidence that they exert variable control on the response to danger; creating a dichotomous response that can suppress inflammation in some circumstances but exacerbate the response to danger and damage in others and, at higher levels, lead to a cytotoxic effect. Focussing in this review on human β-defensins, we discuss the evidence for their functions as proinflammatory, immune activators amplifying the response to infection or damage signals and/or as mediators of resolution of damage, contributing to a return to homeostasis. Finally, we consider their involvement in the development of autoimmune diseases.

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“…Cysrich AMPs are widely distributed in animals and plants, but although having the same number of cysteine residues, the paralithocins show a cysteine arrangement pattern and disulfide connectivity different from any known Cys-rich AMPs (Table 1). Disregarding the flanking cysteines (Cys1 and Cys8) of the paralithocins, the remaining cysteines fold into a Cys1-Cys5, Cys2-Cys4, and Cys3-Cys6 connectivity, identical to the lobster panusin 23 and the vertebrate β-defensins and the invertebrate big defensins. 42 However, homology searches and sequence alignment with selected peptides obtained from these classes reveal no similarities to the paralithocins.…”

Section: Identification Of Genes and Complete Primary Structuresmentioning

confidence: 99%

“…15 Recently, panusin, a β-defensin-like AMP containing six Cys with Cys1-Cys5, Cys2-Cys4, and Cys3-Cys6 connectivity was discovered. 23 Although the disulfide bridges are not essential for biological activity in some disulfidecontaining AMPs, [24][25][26] a stable tertiary structure is usually imperative for proper biological function and stability of disulfide-rich peptides. 27 A peptide with n Cys have i possible arrangements for disulfide bridge connectivity:…”

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confidence: 99%

Paralithocins, Antimicrobial Peptides with Unusual Disulfide Connectivity from the Red King Crab,Paralithodes camtschaticus

et al. 2018

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As part of an ongoing exploration of marine invertebrates as a source of new antimicrobial peptides, hemocyte extracts from the red king crab, Paralithodes camtschaticus, were studied. Three cationic cysteine (Cys)-rich peptides, named paralithocins 1-3, were isolated by bioassay-guided purification, and their amino acid sequences determined by Edman degradation and expressed sequences tag analysis. Disulfide bond mapping was performed by high-resolution tandem mass spectrometry. The peptides (38-51 amino acids in length) share a unique Cys motif composed of eight Cys, forming four disulfide bridges with a bond connectivity of (Cys relative position) Cys1-Cys8, Cys2-Cys6, Cys3-Cys5, and Cys4-Cys7, a disulfide arrangement that has not been previously reported among antimicrobial peptides. Thus, paralithocins 1-3 may be assigned to a previously unknown family of antimicrobial peptides within the group of Cys-rich antimicrobial peptides. Although none of the isolated peptides displayed antimicrobial activity against the target strains Escherichia coli, Pseudomonas aeruginosa, or Staphylococcus aureus, they inhibited the growth of several marine bacterial strains with minimal inhibitory concentrations in the 12.5-100 μM range. These findings corroborate the hypothesis that marine organisms are a valuable source for discovering bioactive peptides with new structural motifs.

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Panusin represents a new family of β-defensin-like peptides in invertebrates

Cited by 20 publications

References 59 publications

Functional Insights From the Evolutionary Diversification of Big Defensins

Functional Insights From the Evolutionary Diversification of Big Defensins

The Dichotomous Responses Driven by β-Defensins

Paralithocins, Antimicrobial Peptides with Unusual Disulfide Connectivity from the Red King Crab,Paralithodes camtschaticus

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