Molecular cloning and response to laminarin stimulation of arginine kinase in haemolymph in Chinese shrimp,

Yao, Cui-Luan; Wu, Changgong; Xiang, Jianhai; Dong, Bo

doi:10.1016/j.fsi.2005.01.006

Cited by 53 publications

(40 citation statements)

References 42 publications

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“…The ORF encodes a polypeptide of 356 amino acids with most of the residues considered necessary for AK's enzymatic function. Its theoretical mass is 40016.43 Da with an estimated isoelectric point of 5.86, which are in the agreement with the results of other recent studies (Wang & Xu, 2006;Yao et al, 2005). In addition, the highly conserved motif CPTNLGT (positions 271-277) around a reactive cysteinyl residue (position 271) is the signature pattern for this family of arginine kinase.…”

Section: Resultssupporting

confidence: 90%

Phyllotreta striolata (Coleoptera: Chrysomelidae): Arginine kinase cloning and RNAi-based pest control

Zhao¹,

Guang²,

Wang‐Pruski³

et al. 2008

Eur. J. Entomol.

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Abstract. Insect pests cause billions of dollars in crop losses and there is the ever-present threat of insecticide resistance, pesticide pollution of food and environmental damage. New ways of controlling insect pests are urgently needed. Arginine kinase (AK) is a phosphotransferase, which plays a critical role in cellular energy metabolism in invertebrates. It only presents in invertebrates and may be a suitable chemotherapeutic target in the control of pests. In this study, we cloned and characterized the full-length AK gene from Phyllotreta striolata, one of the most destructive beetle pests worldwide. Furthermore, we constructed a dsRNA targeting AK and used RNAi to control the beetle. The feeding bioassays indicated that minute quantities of dsRNA greatly impaired the beetle's development. Ingestion of dsRNA not only significantly retarded the development and increased the mortality of adults, it also greatly reduced fecundity and fertility, suggesting that RNAi targeting AK is a potential and attractive tool for controlling insect pests.

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Section: Resultssupporting

confidence: 90%

Phyllotreta striolata (Coleoptera: Chrysomelidae): Arginine kinase cloning and RNAi-based pest control

Zhao¹,

Guang²,

Wang‐Pruski³

et al. 2008

Eur. J. Entomol.

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“…We speculated that the AK function of D. magna was the most close to the congeneric D. pulex. All these findings supported a number of previous studies that provided evidence for an excellent conservation of both primary, secondary and tertiary structures amongst phosphagen kinases (Ellington, 2001;Yao et al, 2005).…”

Section: Discussionsupporting

confidence: 89%

Arginine kinase in the cladoceran Daphnia magna: cDNA sequencing and expression is associated with resistance to toxic Microcystis

et al. 2015

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“…AK is a phosphagen kinase that is the key to energy metabolism in invertebrates. AK catalyzes the reversible transfer of high-energy phosphate from arginine phosphate to ADP to form ATP, thereby regenerating ATP during bursts of cellular activity [11]. Analysis of molecular information of crustacean AKs has revealed an evolutionary relationship between AK and vertebrate creatine kinase, which has a similar metabolic role.…”

Section: Introductionmentioning

confidence: 99%

Molecular Characterization of Arginine Kinase, an Allergen from the Shrimp <i>Litopenaeus vannamei</i>

García-Orozco

Aispuro‐Hernández

Yépiz-Plascencia

et al. 2007

Int Arch Allergy Immunol

149

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Background: Consumption of seafood can produce allergic symptoms in susceptible individuals and crustacean allergies are the most frequently reported causes of allergic reactions. Methods: An allergen from the muscle of the white shrimp Litopenaeus vannamei was purified by ion exchange chromatography and identified by mass spectrometry of tryptic peptides and its specific enzymatic activity. Moreover, the corresponding full-length cDNA was obtained from an L. vannamei muscle cDNA library. Results: A 40-kDa protein was purified and identified as arginine kinase and its cDNA of 1.4 kb encoded a 356 amino acid protein. The obtained arginine kinase was recognized by IgE in serum from shrimp-allergic individuals using ELISA and immunoblotting analysis. Conclusions: This is the first allergen reported for the Pacific white shrimp species; it was named Lit v 2 and has a 96% identity to Pen m 2 from Penaeus monodon.

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Molecular cloning and response to laminarin stimulation of arginine kinase in haemolymph in Chinese shrimp,

Cited by 53 publications

References 42 publications

Phyllotreta striolata (Coleoptera: Chrysomelidae): Arginine kinase cloning and RNAi-based pest control

Phyllotreta striolata (Coleoptera: Chrysomelidae): Arginine kinase cloning and RNAi-based pest control

Arginine kinase in the cladoceran Daphnia magna: cDNA sequencing and expression is associated with resistance to toxic Microcystis

Molecular Characterization of Arginine Kinase, an Allergen from the Shrimp <i>Litopenaeus vannamei</i>

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