Purification of a novel arthropod defensin from the American oyster, Crassostrea virginica

Seo, Jung-Kil; Crawford, Janet; Stone, Kathryn L.; Noga, Edward J.

doi:10.1016/j.bbrc.2005.11.013

Cited by 140 publications

(90 citation statements)

References 31 publications

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“…In recent years, multiple defensins have been identified from marine mollusks, such as Mytilus galloprovincialis (Hubert et al, 1996), Mytilus edulis (Charlet et al, 1996), Crassostrea virginica (Seo et al, 2005), Crassostrea gigas (Gonzalez et al, 2007;Gueguen et al, 2006), Haliotis discus discus (De Zoysa et al, 2010) and Venerupis philippinarum (Adhya et al, 2012).…”

Section: Contents Lists Available At Sciencedirectmentioning

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: Contents Lists Available At Sciencedirectmentioning

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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“…To date, several AMPs have been identified in mollusks such as the gastropod Dolabella auricularia (Iijima et al, 2003); marine bivalves Mytilus edulis (Charlet et al, 1996), M. galloprovincialis (Hubert et al, 1996;Dupuy et al, 2004), Crassostrea virginica (Seo et al, 2005) and C. gigas (Gonzalez et al, 2007;Gueguen et al, 2006). By using biochemical and molecular cloning techniques, the following 4 groups of cationic cysteine-rich AMPs have been isolated from the hemocytes of unchallenged mussels M. galloprovincialis and M. edulis: (i) defensin-like peptides MGD-1 and MGD-2 (Mitta et al, 2000;Romestand et al, 2003;Seo et al, 2005;Gueguen et al, 2006); (ii) myticins (Mitta et al, 2000); (iii) mytilins with 8 cysteine residues but different specific cysteine arrays and amino acid sequences (Mitta et al, 2000); and (iv) mytimycin (Charlet et al, 1996). Except for the AMP described above, a novel antimicrobial peptides named Comparative Biochemistry and Physiology, Part B 157 (2010) 119-126 theromacin was isolated and characterized from annelid Theromyzon tessulatum (Tasiemski et al, 2004) and Hirudo medicinalis (Tasiemski, 2008).…”

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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“…선천성면역에 관련된 물질로는 lectin, pro-phenolioxidase activating factor, phagocytosis, AMP등이 존재한다. 이들은 외부로부터 체내에 미생물들이 침입하면 1차적으로 그것을 없애는 역할을 담당 하고 있다 [17]. 해양 무척추 동물의 대부분은 외부침입에 대한 방어수단으로서 선천성면역에 대부분 의존하고 있기 때문에 AMP의 역할이 매우 중요하게 작용하고 있다.…”

Section: 서 론unclassified

“…해양 무척추 동물의 대부분은 외부침입에 대한 방어수단으로서 선천성면역에 대부분 의존하고 있기 때문에 AMP의 역할이 매우 중요하게 작용하고 있다. 이러한 항균성 단백질 및 펩타이드는 다양한 종류의 해양무척추동물로부터 발견되었다 [5,11,17]. 2).…”

Section: 서 론unclassified

Purification of Two Novel Antimicrobial Peptides from Pyloric Caeca of the Starfish Asterina pectinifera

Go¹,

Bae²,

Park

2014

Journal of Life Science

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PAP-1, a novel antimicrobial peptide isolated from pyloric caeca extract of the starfish Asterina pectinifera was purified and characterized. First, the acidified pyloric caeca extract was put through Sep-Pak C18 solid phase extraction cartridge using a stepwise gradient. Among the eluents, RM 60 (retained materials at 60% methanol) showed good antimicrobial activity against Bacillus subtilis and Escherichia coli D31 and was purified in C18 reversed-phase and ion-exchange high-performance liquid chromatography columns. The purification steps yielded two novel peptides showing strong antimicrobial activities. These peptides were named pyloric caeca A. pectinifera peptide 1 and 2 (PAP-1 and PAP-2).For the characterization of the purified peptides, the molecular weights and amino acid sequences were determined by MALDI-TOF MS and Edman degradation. The molecular weights of PAP-1 and PAP-2 were about 2951.54 Da and 2980.15 Da respectively. The amino acid sequences of PAP-1 and PAP-2 were partially determined: AIQNAGES and AIQNAAES, respectively. PAP-2 is an isoform of PAP-1, differing merely by a single residue at position 6 (glycine or alanine). The comparison of the N-terminal amino acid sequences and molecular weights of the peptides with those of other known antimicrobial peptides revealed that PAP-1 and PAP-2 have no homology with any known peptides. These findings suggest that PAP-1 and PAP-2 play a significant role in the innate defense system of starfish pyloric caeca.Key words : Antimicrobial peptide, pyloric caeca, purification, starfish *Corresponding author *Tel : +82-51-629-5867, Fax : +82-51-629-5863 *E-mail : ngpark@pknu.ac.kr This is an Open-Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Purification of a novel arthropod defensin from the American oyster, Crassostrea virginica

Cited by 140 publications

References 31 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

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

Purification of Two Novel Antimicrobial Peptides from Pyloric Caeca of the Starfish Asterina pectinifera

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