Involvement of penaeidins in defense reactions of the shrimp Litopenaeus stylirostris to a pathogenic vibrio

Muñoz, Marcelo; Vandenbulcke, Franck; Garnier, Julien; Gueguen, Yannick; Bulet, Philippe; Saulnier, Denis; Bachère, Evelyne

doi:10.1007/s00018-003-3441-9

Cited by 60 publications

(43 citation statements)

References 31 publications

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“…In contrast, the expression level of some AMPs decreased after bacterial challenge. For example, within about 6-24 h of Vibrio challenge, a significant decrease was observed in the mRNA expression of AMPs such as crustin, mytilin B, and penaeidin, and this decrease was followed by a recovery process (Destoumieux et al, 2000;Munoz et al, 2004;Supungul et al, 2004). The level of Cg-defh2 transcripts is markedly low in the circulating hemocyte population but high in the gill and mantle tissue (Gonzalez et al, 2007).…”

Section: Discussionmentioning

confidence: 99%

“…In addition to AMPs, different species often have a reservoir of structurally diverse peptides to combat pathogens (Mitta et al, 2000). Marine invertebrates are solely dependent on physical barriers and the innate immune system for protection against pathogenic agents, and natural antibiotics have been shown to participate in the immune response during experimental bacterial challenges (Munoz et al, 2004). AMPs have been isolated from several marine invertebrates, including chelicerates, molluscs, and crustaceans (Tincu and Taylor, 2004).…”

Section: Introductionmentioning

confidence: 99%

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cDNA sequence and expression analysis of an antimicrobial peptide, theromacin, in the triangle-shell pearl mussel Hyriopsis cumingii

Wang

Yuan

et al. 2010

Comparative Biochemistry and Physiology Part B: Biochemistry an

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

cDNA sequence and expression analysis of an antimicrobial peptide, theromacin, in the triangle-shell pearl mussel Hyriopsis cumingii

Wang

Yuan

et al. 2010

Comparative Biochemistry and Physiology Part B: Biochemistry an

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“…The time course of Cg-bpi gene expression was analyzed in response to bacterial challenge using quantitative in situ hybridization with 35 S-radiolabeled riboprobes. This methodology gives access to the amounts of transcript of interest [quantified as arbitrary units (AU)] in individual cells and to the percentage of cells expressing that transcript.…”

Section: Cg-bpi Gene Expression Is Constitutive In Oyster Epithelia Amentioning

confidence: 99%

Evidence of a bactericidal permeability increasing protein in an invertebrate, theCrassostrea gigas Cg-BPI

González-Aravena

Gueguen

Destoumieux-Garzón

et al. 2007

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

125

124

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A cDNA sequence with homologies to members of the LPS-binding protein and bactericidal/permeability-increasing protein (BPI) family was identified in the oyster Crassostrea gigas. The recombinant protein was found to bind LPS, to display bactericidal activity against Escherichia coli, and to increase the permeability of the bacterial cytoplasmic membrane. This indicated that it is a BPI rather than an LPS-binding protein. By in situ hybridization, the expression of the C. gigas BPI (Cg-bpi) was found to be induced in hemocytes after oyster bacterial challenge and to be constitutive in various epithelia of unchallenged oysters. Thus, Cg-bpi transcripts were detected in the epithelial cells of tissues/organs in contact with the external environment (mantle, gills, digestive tract, digestive gland diverticula, and gonad follicles). Therefore, Cg-BPI, whose expression profile and biological properties are reminiscent of mammalian BPIs, may provide a first line of defense against potential bacterial invasion. To our knowledge, this is the first characterization of a BPI in an invertebrate.antimicrobial ͉ epithelia ͉ hemocyte ͉ mollusk ͉ oyster innate immunity M arine invertebrates including bivalve mollusks have evolved in the continuous presence of microorganisms. The oysters, such as Crassostrea gigas, harbor a diverse microflora both on their surface (epibiosis) and inside the body cavities and hemolymph (endobiosis). They have developed an efficient immune system for maintaining balance with commensal and pathogenic bacteria, in particular with the Gram-negative Vibrio spp. abundant in their tissues/organs. LPS from Gram-negative bacteria play an important role in the interaction and activation of the innate immune system including the antimicrobial defense (1, 2). In invertebrates, LPSbinding proteins (LBP) participate in the transduction of cellular signals from LPS. LBPs have been characterized in the freshwater crayfish Pacifastacus leniusculus (3), the shrimp Litopenaeus stylirostris (4), the earthworm Eisenia foetida (5), and the silkworm Bombyx mori (6). In mammals, LBP is an acute phase plasma protein constitutively secreted by liver that induces cellular responses (7). In particular, LBP participates in the acute mobilization of circulating neutrophils to sites of tissue injury. Stored in the mobilized neutrophils, antimicrobial peptides and the bactericidal/ permeability-increasing protein (BPI) contribute to the elimination of bacteria (8, 9). BPI, another LBP, is a 55-kDa cationic protein specifically active against Gram-negative bacteria. It increases the permeability of the bacterial membranes (10). Accumulated extracellularly, BPI opsonizes bacteria, which enhances phagocytosis by neutrophils (11). LBP and BPI are structurally related, with 45% sequence identity. They have a coordinated function in the response to invading bacteria. The antibacterial BPI displays LPSneutralizing properties and suppresses LPS inflammatory activity whereas LBP is an acute-phase reactant (8, 12) that displays a concen...

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“…A total of 36 nucleotide sequences were retrieved from GenBank ( [6,7,11,13,16,18,22,24,25]; Table 1). Sequences were aligned using DAMBE version 4.5.2 [38,39] and BioEdit version 7.0.5.3 [40].…”

Section: Nucleotide Phylogenymentioning

confidence: 99%

“…AMPs have been identified and characterized in many vertebrates [3], invertebrates [1] and plants [4]. Due to the lack of adaptive immunity, invertebrates are dependent on the innate immune system for protection from pathogens [5,6]. The devastating disease outbreaks in many commercially important penaeid shrimps has caused serious setback in the aquaculture industry, therefore, the focus has been now towards a better understanding of penaeid shrimp immunity, which would help in designing efficient strategies for disease control [5].…”

Section: Introductionmentioning

confidence: 99%

Adaptive evolution after duplication of penaeidin antimicrobial peptides

Padhi

Verghese

Otta

et al. 2007

Fish & Shellfish Immunology

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Penaeidin antimicrobial peptides in penaeid shrimps are an important component of their innate immune system that provides immunity against infection caused by several gram-positive bacteria and filamentous fungal species. Despite the knowledge on the identification and characterization of these peptides in penaeid shrimps, little is known about the evolutionary pattern of these peptides and the underlying genetic mechanisms that maintain high sequence diversities in the penaeidin gene family. Based on the phylogenetic analyses and maximum likelihood-based codon substitution analyses, here we present the convincing evidence that multiple copies of penaeidins have evolved by gene duplication, and positive Darwinian selection (adaptive evolution) is the likely cause of accelerated rate of amino acid substitutions among these duplicated genes.While the average ratio of non-synonymous to synonymous substitutions (u) for the entire coding region of both active domains is 0.9805, few codon sites showed significantly higher u (3.73). The likelihood ratio tests that compare models incorporating positive selection (u > 1) at certain codon sites with models not incorporating positive selection (u < 1), failed to reject (p ¼ 0) the evidence of positive Darwinian selection. The rapid adaptive evolution of this gene family might be directed by the pathogens and the faster rate of amino acid substitutions in the N-terminal proline-rich and C-terminal cysteine-rich domains could be due to their direct involvement in the protection against pathogens. When the host expose to different habitats/environment an accelerated rate of amino acid substitutions in both the active domains may also be expected.

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Involvement of penaeidins in defense reactions of the shrimp Litopenaeus stylirostris to a pathogenic vibrio

Cited by 60 publications

References 31 publications

cDNA sequence and expression analysis of an antimicrobial peptide, theromacin, in the triangle-shell pearl mussel Hyriopsis cumingii

cDNA sequence and expression analysis of an antimicrobial peptide, theromacin, in the triangle-shell pearl mussel Hyriopsis cumingii

Evidence of a bactericidal permeability increasing protein in an invertebrate, theCrassostrea gigas Cg-BPI

Adaptive evolution after duplication of penaeidin antimicrobial peptides

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