Consulta: creatorFacets:"Perazzolo, Luciane Maria"
Registros recuperados: 3
Data/hora: 08/06/2024 18:33:14

Functional Divergence in Shrimp Anti-Lipopolysaccharide Factors (ALFs): From Recognition of Cell Wall Components to Antimicrobial Activity
Provedor de dados: Institutional Archive of Ifreme (ArchiMer)
Autores: Rosa, Rafael Diego; Vergnes, Agnes; De Lorgeril, Julien; Goncalves, Priscila; Perazzolo, Luciane Maria; Saune, Laure; Romestand, Bernard; Fievet, Julie; Gueguen, Yannick; Bachere, Evelyne; Destoumieux-garzon, Delphine.
Antilipopolysaccharide factors (ALFs) have been described as highly cationic polypeptides with a broad spectrum of potent antimicrobial activities. In addition, ALFs have been shown to recognize LPS, a major component of the Gram-negative bacteria cell wall, through conserved amino acid residues exposed in the four-stranded beta-sheet of their three dimensional structure. In penaeid shrimp, ALFs form a diverse family of antimicrobial peptides composed by three main variants, classified as ALF Groups A to C. Here, we identified a novel group of ALFs in shrimp (Group D ALFs), which corresponds to anionic polypeptides in which many residues of the LPS binding site are lacking. Both Group B (cationic) and Group D (anionic) shrimp ALFs were produced in a...
Tipo: Text
Ano: 2013
URL: http://archimer.ifremer.fr/doc/00160/27077/25236.pdf

Massive Gene Expansion and Sequence Diversification Is Associated with Diverse Tissue Distribution, Regulation and Antimicrobial Properties of Anti-Lipopolysaccharide Factors in Shrimp
Provedor de dados: Institutional Archive of Ifreme (ArchiMer)
Autores: Matos, Gabriel Machado; Schmitt, Paulina; Barreto, Caire; Farias, Natanael Dantas; Toledo-silva, Guilherme; Guzman, Fanny; Destoumieux Garzon, Delphine; Perazzolo, Luciane Maria; Rosa, Rafael Diego.
Anti-lipopolysaccharide factors (ALFs) are antimicrobial peptides with a central β-hairpin structure able to bind to microbial components. Mining sequence databases for ALFs allowed us to show the remarkable diversity of ALF sequences in shrimp. We found at least seven members of the ALF family (Groups A to G), including two novel Groups (F and G), all of which are encoded by different loci with conserved gene organization. Phylogenetic analyses revealed that gene expansion and subsequent diversification of the ALF family occurred in crustaceans before shrimp speciation occurred. The transcriptional profile of ALFs was compared in terms of tissue distribution, response to two pathogens and during shrimp development in Litopenaeus vannamei, the most...
Tipo: Text
Palavras-chave: Host defense peptide; Antimicrobial peptide; Anti-LPS factor; Hostmicrobe relationship; Functional diversity; Invertebrate immunity; Crustacean; Antimicrobial activity.
Ano: 2018
URL: https://archimer.ifremer.fr/doc/00464/57523/59711.pdf

Litopenaeus vannamei stylicins are constitutively produced by hemocytes and intestinal cells and are differentially modulated upon infections
Provedor de dados: Institutional Archive of Ifreme (ArchiMer)
Autores: Farias, Natanael Dantas; Falchetti, Marcelo; Matos, Gabriel Machado; Schmitt, Paulina; Barreto, Cairé; Argenta, Nicolas; Rolland, Jean-luc; Bachère, Evelyne; Perazzolo, Luciane Maria; Rosa, Rafael Diego.
Stylicins are anionic antimicrobial host defense peptides (AAMPs) composed of a proline-rich N-terminal region and a C-terminal portion containing 13 conserved cysteine residues. Here, we have increased our knowledge about these unexplored crustacean AAMPs by the characterization of novel stylicin members in the most cultivated penaeid shrimp, Litopenaeus vannamei. We showed that the L. vannamei stylicin family is composed of two members (Lvan-Stylicin1 and Lvan-Stylicin2) encoded by different loci which vary in gene copy number. Unlike the other three gene-encoded antimicrobial peptide families from penaeid shrimp, the expression of Lvan-Stylicins is not restricted to hemocytes. Indeed, they are also produced by the columnar epithelial cells lining the...
Tipo: Text
Palavras-chave: Crustacean; Penaeid shrimp; Invertebrate immunity; Antimicrobial peptide; Host defense peptide; Molecular diversity.
Ano: 2019
URL: https://archimer.ifremer.fr/doc/00466/57816/60102.pdf