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2013 | 60 | 1 |

Tytuł artykułu

Biochemical and electrophoretic analyses of saliva from the predatory reduviid species Rhynocoris marginatus (Fab.)

Warianty tytułu

Języki publikacji

PL

Abstrakty

EN
The saliva of Rhynocoris marginatus consists of amylase, invertase, trehalase, protease, acid phosphatase, alkaline phosphatase, phospholipase, lipase, trypsin, hyaluronidase, and esterase. All enzyme activities were significantly higher in the saliva of female R. marginatus when compared to the saliva of male individuals. The saliva was analyzed by tricine SDS/PAGE, sephadex column chromatography, FT-IR, and MALDI-TOF. The pH of the saliva was slightly alkali. The SDS/PAGE revealed a few proteins with molecular masses greater than 29.5 and 36.2 kDa for male and female predator saliva respectively. The FT-IR spectrum confirmed the acidic, proteinaceous, enzymatic, and aromatic nature of the saliva. The MALDI-TOF-MS revealed the presence of enzymes, proteins, peptides, and other biomolecules. The most prominent peptides were named as RmIT-1 (3.79kDa), RmIT-2 (9.7kDa), and RmIT-3 (10.94kDa) (Rhynocoris marginatus Insect Toxin). Further studies are underway to isolate and identify these biomolecules.

Słowa kluczowe

Wydawca

-

Rocznik

Tom

60

Numer

1

Opis fizyczny

p.91-97,fig.,ref.

Twórcy

autor
  • Crop Protection Research Centre, Department of Advanced Zoology and Biotechnology, St. Xavier's College (Autonomous), Palayamkottai, Tamil Nadu, India
  • UPASI Tea Research Foundation, Tea Research Institute, Nirar Dam (po), Valparai Tamil Nadu, India
autor
  • Department of Biology, Loyola University Maryland, Baltimore, Maryland USA

Bibliografia

  • Ambrose DP (1999) Assassin bugs. Science publishers, New Hampshire, USA and Oxford and IBH Publ. Co. Pvt. Ltd, New Delhi, India, pp. 337.
  • Areas EP, Giglio JR, Arantes EC, Kawano Y (1987) Raman and infrared spectra of toxin γ from the venom of the scorpion Tityus serrulatus. Biochim Biophys Acta 915: 292-298. 
  • Arrondo JL, Muga A, Castresana J, Goni FM (1993) Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy. Progress Biophys Mol Biol 59: 23-56. 
  • Asgari S, Rivers DB (2011) Venom proteins from endoparasitoid wasps and their role in host-parasite interactions. Ann Rev Entomol 56: 313-335. 
  • Beaufay H, Berihet J, Duve CD (1954) Les systeme hexose-phosphatasique. V. Influence de diverse agents sur I' activite et la stabilite de la glucose 6-phosphatase. Bull Soc Chimiq Belges 36: 1539-1550.
  • Bernfeld JE (1955) Amylases α and β. Methods in Enzymology 1: 149-158.
  • Cherry IS, Crandall Jr LA (1932) The specificity of pancreatic lipase in appearance in the blood after pancreatic injury. Am J Physiol 100: 266-273.
  • Cho JR, Kim YJ, Kim JJ, Kim HS, Yoo JK, Lee JO (1999) Electrophoretic pattern of larval esterases in field and laboratory-selected strains of the tobacco cutworm, Spodoptera litura (Fabricius). J Asia-Pacific Entomol 2: 39-44.
  • Cohen AC (1993) Organization of digestion and preliminary characaterization of salivary trypsin-like enzymes in a predaceous heteropteran, Zelus reinardii. J Insect Physiol 39: 823-829.
  • Cohen AC (1996) Plant feeding by predatory Heteroptera: evolutionary and adaptational aspects of trophic switching. In Zoophytophagous Heteroptera: implications for life history and integrated pest management (Alomar O, Wiedenmann RN eds.), Thomas Say Publications in Entomology, pp. 1-17. Entomology Society of America, Lanham, MD.
  • Cohen AC (1998) Solid-to-liquid feeding: the inside(s) story of extra-oral digestion in predaceous Arthropoda. Am Entomol 44: 103-117.
  • Corzo G, Adachi-Akahane S, Nagao T, Kusui Y, Nakajima T (2001) Novel peptides from assassin bugs (Hemiptra: Reduviidae): isolation, chemical and biological characterization. FEBS Letter 499: 256-261. 
  • Dani MP, Edwards JP, Richards EH (2005) Hydrolase activity in the venom of the pupal endoparasitic wasp, Pimpla hypochondriaca. Comp Biochem Physiol B Biochem Mol Biol 141: 373-381. 
  • de Lima PR, Braga MRB (2003) Hymenoptera venom review focusing on Apis mellifera. J Ven Anim Toxins Tropical Dise 9: 1-10.
  • Edwards JS (1961) The action and composition of the saliva of an assassin bug Platymeris rhadamanthus Gaerst. (Hemiptera: Reduviidae). J Exp Biol 8: 61-77.
  • Ishaaya I, Swirski E (1970) Invertase and amylase activity in the armored scales Chrysomphalus aonidum and Aonidiella avantii. J Insect Physiol 16: 1599-1606. 
  • Ishaaya I, Swriski E (1976) Trehalase, invertase and amylase activities in the black scale, Saissetia oleae, and their relation to host adaptability. J Insect Physiol 22: 1025-1029.
  • Ji SJ, Liu F, Li EQ, Zhu YX (2002) Recombinant scorpion insectotoxin AaIT kills specifically insect cells but not human cells. Cell Res 12: 143-150.  
  • Leonard GJ (1972) The isolation of a toxic factor from sawfly (Lophyrotoma interrupta Klug) larvae. Toxicon 10: 597-603. 
  • Liu ZH, Qian W, Li J, Zhang Y, Lian S (2009) Biochemical and pharmacological study of venom of the wolf spider Lycosa singoriensis. J Venom Anim Toxins Tropic Dis 15: 79-92.
  • Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193: 265-275.  
  • Maran PM (2000) Chosen reduviid predators-prey interaction: nutritional and pheromonal chemical ecology (Insecta: Heteroptera: Reduviidae). Manonmaniam Sundaranar University, India.
  • Morey SS, Kiran KM, Gadag JR (2006) Purification and properties of hyaluronidase from Palamneus gravimanus (Indian black scorpion) venom. Toxicon 47: 188-195. 
  • Moreau SJ, Guillot S (2005) Advances and prospects on biosynthesis, structures and functions of venom proteins from parasitic wasps. Insect Biochem Mol Biol 35: 1209-1223. 
  • Morrison NM (1989) Gel electrophoretic studies with reference to functional morphology of the salivary glands of Acanthaspis pedestris Stål. (Insecta: Heteroptera: Reduviidae). Proc Indian Acad Sci (Anim Sci) 98: 167-173.
  • Parkinson N, Smith I, Audsley N, Edwards JP (2002) Purification of pimplin, a paralytic heterodimeric polypeptide from venom of the parasitoid wasp Pimpla hypochondriaca, and cloning of the cDNA encoding one of the subunits. Insect Biochem Mol Biol 32: 1769-1773. 
  • Pukrittayakamee S, Warrell DA, Desakorn V, McMichael AJ, White NJ, Bunnag GD (1988) The hyaluronidase activities of some south east Asian snake venoms. Toxicon 26: 629-637.  
  • Rash LD, Hodgson WC (2002) Pharmacology and biochemistry of spider venoms. Toxicon 40: 225-254.  
  • Rivers DB, Uçkan F, Ergin E, Keefer DA (2010) Pathological and ultrastructural changes in cultured cells induced by venom from the ectoparasitic wasp Nasonia vitripennis (Walker) (Hymenoptera: Pteromalidae). J Insect Physiol 56: 1935-1948. 
  • Sahayaraj K (2007) Pest Control Mechanism of Rediviids, pp 204. Oxford Book Company, Narayan Niwas, Jaipur, India.
  • Sahayaraj K, Kumar SM (2011) Zootoxic effects of reduviid Rhynocoris marginatus (Fab.) (Hemiptera: Reduviidae) salivary venom on Spodoptera litura (Fab.). Toxicon 58: 415-425. 
  • Sahayaraj K, Borgio JF, Kumar SM, Anandh GP (2006a) Antimicrobial activity of Rhynocoris marginatus (Fab) and Catamirus brevipennis (Servile) (Hemiptera: Reduviidae) venom on selected human pathogens. J Venomous Anim Toxins Tropic Dis 12: 487-496.
  • Sahayaraj K, Kumar SM, Anandh GP (2006b) Evaluation of milking and electric shock methods for venom collection from hunter reduviids. Entomon 31: 165-168.
  • Sahayaraj K, Sankaralinkam SK, Balasubramanian R (2007) Prey influence on the salivary gland and gut enzymes qualitative profile of Rhynocoris marginatus (Fab.) and Catamiarus brevipennis (Serville) (Heteroptera: Reduviidae). J Insect Sci 4: 331-336.
  • Santoro ML, Sousa-e-Silva MC, Gonçalves LR, Almeida-Santos SM, Cardoso DF, Laporta-Ferreira IL, Saiki M, Peres CA, Sano-Martins IS (1999) Comparison of the biological activities in venoms from three subspecies of the South American rattlesnake (Crotalus durissus terrificus, C. durissus cascavella and C. durissus collilineatus). Comp Biochem Physiol C Pharmacol 122: 61-73. 
  • Schägger H, Von Jagow G (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1-100 kDalton. Anal Biochem 166: 368-379. 
  • da Silveira RB, Chaim OM, Mangili OC, Gremski W, Dietrich CP, Nader HB, Veiga SS (2007) Hyaluronidases in Loxosceles intermedia (brown spider) venom are endo-β-N-acetyl-d-hexosaminidases hydrolases. Toxicon 49: 758-768. 
  • Soyelu OL, Akingbohungbe AE, Okonji RE (2007) Salivary glands and their digestive enzymes in pod-sucking bugs (Hemiptera: Coreoidea) associated with cowpea Vigna unguiculata ssp. ungiculata in Nigeria. Int J Tropic Insect Sci 27: 40-47.
  • Uçkan F, Sinan S, Savaşçý S, Ergin E (2004) Determination of venom components from the endoparasitoid wasp Pimpla turionellae L. (Hymenoptera: Ichneumonidae). Ann Entomol Soc Am 97: 775-780.
  • Van Asperen K (1962) A study of housefly esterases by means of a sensitive colorimetric method. 1. J Insect Physiol 8: 401-416.
  • Yoshida S, Miyazaki M, Sakai K, Takeshita M, Yuasa S, Sato A, Kobayashi T, Watanabe S, Okuyama H (1997) Fourier transform infrared spectroscopic analysis of rat brain microsomal membranes modified by dietary fatty acids: possible correlation with altered learning behavior. Biospectroscopy 3: 281-290.
  • Zeng XZ, Xiao QB, Liang SP (2003) Purification and characterization of raventoxin-I and raventoxin-III, two neurotoxic peptides from the venom of the spider Macrothele raveni. Toxicon 41: 651-656. 
  • Zeng F, Zhu YC, Cohen AC (2002) Molecular cloning and partial characterization of a trypsin-like protein in salivary glands of Lygus hesperus (Hemiptera: Miridae). Insect Biochem Mol Biol 32: 455-464. 

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Bibliografia

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