Purification and structural characterisation of phospholipase A1 (Vespapase, Ves a 1) from Thai banded tiger wasp (Vespa affinis) venom

Sukprasert, Sophida; Rungsa, Prapenpuksiri; Uawonggul, Nunthawun; Incamnoi, Paroonkorn; Thammasirirak, Sompong; Daduang, Jureerut; Daduang, Sakda

doi:10.1016/j.toxicon.2012.10.024

Cited by 31 publications

(40 citation statements)

References 28 publications

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“…c6971 from Ooencyrtus telenomicida has 18 and 16 residues in its β9 loop and lid domain, respectively [12]. For some social wasps and ants, their venom-associated phospholipase A1s (PLA1s) have been observed with both shorten β9 loops and small lid domains, indicating that these lipases lack TAG hydrolytic activity either [52][53][54].…”

Section: Identification Of β9 Loop and Lids Of Lipases In P Puparummentioning

confidence: 99%

Insight into the Functional Diversification of Lipases in the Endoparasitoid Pteromalus puparum (Hymenoptera: Pteromalidae) by Genome-scale Annotation and Expression Analysis

Wang

Song

Fang

et al. 2020

Insects

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Lipases play essential roles in digestion, transport, and processing of dietary lipids in insects. For parasitoid wasps with a unique life cycle, lipase functions could be multitudinous in particular. Pteromalus puparum is a pupal endoparasitoid of butterflies. The female adult deposits eggs into its host, along with multifunctional venom, and the developing larvae consume host as its main nutrition source. Parasitoid lipases are known to participate in the food digestion process, but the mechanism remains unclear. P. puparum genome and transcriptome data were interrogated. Multiple alignments and phylogenetic trees were constructed. We annotated a total of 64 predicted lipase genes belonging to five lipase families and suggested that eight venom and four salivary lipases could determine host nutrition environment post-parasitization. Many putative venom lipases were found with incomplete catalytic triads, relatively long β9 loops, and short lids. Data analysis reveals the loss of catalytic activities and weak triacylglycerol (TAG) hydrolytic activities of lipases in venom. Phylogenetic trees indicate various predicted functions of lipases in P. puparum. Our information enriches the database of parasitoid lipases and the knowledge of their functional diversification, providing novel insight into how parasitoid wasps manipulate host lipid storage by using venom lipases.

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Section: Identification Of β9 Loop and Lids Of Lipases In P Puparummentioning

confidence: 99%

Insight into the Functional Diversification of Lipases in the Endoparasitoid Pteromalus puparum (Hymenoptera: Pteromalidae) by Genome-scale Annotation and Expression Analysis

Wang

Song

Fang

et al. 2020

Insects

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“…SDS-PAGE and two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) were slightly modified from Sukprasert et al (2013). After being focused in the first dimension with 7 cm immobilized pH gradient strip pH 3e11 (Amersham Biosciences, Sweden) for 12 h and 9250 total Vhr using Ettan IPGphor (Amersham Bioscience), samples were resolved by 13% Tris-glycine SDS-PAGE for the second dimension.…”

Section: Gel Electrophoresismentioning

confidence: 99%

“…It removes the acyl group from phospholipid causes damage of cell membranes, which leads to severe hemolysis, cardiac dysfunction of victims. It induces platelet aggregation, smooth muscle contraction and the stimulation of cell proliferation (Ho et al, 1999;Sukprasert et al, 2013;Yang et al, 2008).…”

Section: Profiles Of Venom Proteins Proportion Of Protein Componentsmentioning

confidence: 99%

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Comparative proteomic analysis of two wasps venom, Vespa tropica and Vespa affinis

Rungsa

Incamnoi

Sukprasert

et al. 2016

Toxicon

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“…Trong nhóm protein xúc tác, chúng tôi phát hiện một số protein và enzyme điển hình cho nọc độc như phospholipase A1 (PLA1) và arginine kinase. PLA1 là protein phổ biến trong nọc độc của rắn (Richmond, Smith, 2011) và một số loài thuộc chi ong bắp cày như Vespa magnifica (Yang et al, 2008), Vespa affinis (Sukprasert et al, 2013). Trong cơ chế tác động của nọc độc, PLA1 tham gia vào quá trình gây dị ứng, viêm và tạo huyết khối trong động mạch chủ (Yang et al, 2008;Richmond et al, 2011).…”

Section: Hệ Protein Nọc độC V Velutinaunclassified

1Institute of Biotechnology, Vietnam Academy of Science and Technology

Dũng

Anh

Phương

et al. 2018

Vietnam J. Biotechnol.

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Wasp venoms are complex mixtures of various types of compounds, of which proteins and peptides are major components. Beside its toxicity, wasp venom is potential for treatment of diseases. Characterization of venom proteins and peptides is the first and most important step toward its applications in medicine. Vietnam possesses many valuable materials, of which venoms could be used in medicine. In the present work, we aim to identify proteins and peptides in the venom of Vespa velutina (V. velutina), a species of social wasp indigenous to Southeast Asia including Vietnam using proteomic techniques. The venom isolated from V. velutina by manual extraction was digested with trypsin via the FASP (Filter Aided Sample Preparation) method and analyzed with liquid chromatography tandem - mass spectrometry (LC-MS/MS). The following protein identification, protein validation, and peptide de novo sequencing were carried out using the Peaks software. In total, we detected 36 proteins from V. velutina venom and many of them had been reported as venom-specific proteins. According to Gene Ontology Annotation (GOA), V. velutina venom proteins were functionally classified into five categories: binding proteins (53%), catalytic proteins (33%), structural proteins (8%), antioxidants (4%), and proteins with other functions (2%). In addition, 81 peptides were detected in the venom of V. velutina by de novo sequencing, of which 34 peptides (42%) are potential venom peptides. We introduced for the first time the collection of proteins and peptides from V. velutina venom, providing the basis for its further application in medicine.

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Purification and structural characterisation of phospholipase A1 (Vespapase, Ves a 1) from Thai banded tiger wasp (Vespa affinis) venom

Cited by 31 publications

References 28 publications

Insight into the Functional Diversification of Lipases in the Endoparasitoid Pteromalus puparum (Hymenoptera: Pteromalidae) by Genome-scale Annotation and Expression Analysis

Insight into the Functional Diversification of Lipases in the Endoparasitoid Pteromalus puparum (Hymenoptera: Pteromalidae) by Genome-scale Annotation and Expression Analysis

Comparative proteomic analysis of two wasps venom, Vespa tropica and Vespa affinis

1Institute of Biotechnology, Vietnam Academy of Science and Technology

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