Ana Oleaga1, Prosper Obolo-Mvoulouga2, Raúl Manzano-Román3, Ricardo Pérez-Sánchez4. 1. Parasitology Laboratory, Instituto de Recursos Naturales y Agrobiología de Salamanca (IRNASA, CSIC), Cordel de Merinas, 40-52, 37008, Salamanca, Spain. ana.oleaga@irnasa.csic.es. 2. Parasitology Laboratory, Instituto de Recursos Naturales y Agrobiología de Salamanca (IRNASA, CSIC), Cordel de Merinas, 40-52, 37008, Salamanca, Spain. prosper.obolo@irnasa.csic.es. 3. Parasitology Laboratory, Instituto de Recursos Naturales y Agrobiología de Salamanca (IRNASA, CSIC), Cordel de Merinas, 40-52, 37008, Salamanca, Spain. raul.manzano@irnasa.csic.es. 4. Parasitology Laboratory, Instituto de Recursos Naturales y Agrobiología de Salamanca (IRNASA, CSIC), Cordel de Merinas, 40-52, 37008, Salamanca, Spain. ricardo.perez@irnasa.csic.es.
Abstract
BACKGROUND: The argasid tick Ornithodoros erraticus is the vector of African swine fever virus and of several Borrelia species that cause human relapsing fever in the Iberian Peninsula. The tick midgut is part of the ectoparasite-host interface and expresses proteins that are vital for the survival of the tick. Midgut proteins are therefore potential targets for drug and/or vaccine design aimed at the development of new strategies for tick control. Thus, the aim of this work was the characterization of the proteome of the O. erraticus midgut before and after a blood meal trying to elucidate the induced changes upon blood feeding. METHODS: Midgut tissues from unfed and engorged O. erraticus females were dissected and proteins were fractionated by centrifugation and SDS-PAGE, and the corresponding gel pieces analysed by LC-MS/MS. The identified proteins were classified according to their Protein Class and Molecular Function and the differences between fed and unfed specimens were analysed. RESULTS: Overall 555 tick proteins were identified: 414 in the midgut of the unfed specimens and 376 in the fed specimens, of which 235 were present in both groups. The proteins with catalytic, binding and structural functions were the most numerous and abundant, consistent with their role in the intracellular processing of the blood meal. The analysis of some groups of proteins putatively involved directly in blood meal digestion, including protein digestion (peptidase activity), iron metabolism, enzymes involved in oxidative stress and detoxification and membrane traffic and transport proteins, detected some differences between the fed and unfed ticks CONCLUSIONS: This work reports for the first time the collection and analysis of the midgut proteome of an argasid tick species and provides molecular information about the argasid machinery involved in blood digestion. This information represents a starting point for the identification and selection of new targets for the development of alternative control strategies.
BACKGROUND: The argasid tick Ornithodoros erraticus is the vector of African swine fever virus and of several Borrelia species that cause human relapsing fever in the Iberian Peninsula. The tick midgut is part of the ectoparasite-host interface and expresses proteins that are vital for the survival of the tick. Midgut proteins are therefore potential targets for drug and/or vaccine design aimed at the development of new strategies for tick control. Thus, the aim of this work was the characterization of the proteome of the O. erraticus midgut before and after a blood meal trying to elucidate the induced changes upon blood feeding. METHODS: Midgut tissues from unfed and engorged O. erraticus females were dissected and proteins were fractionated by centrifugation and SDS-PAGE, and the corresponding gel pieces analysed by LC-MS/MS. The identified proteins were classified according to their Protein Class and Molecular Function and the differences between fed and unfed specimens were analysed. RESULTS: Overall 555 tick proteins were identified: 414 in the midgut of the unfed specimens and 376 in the fed specimens, of which 235 were present in both groups. The proteins with catalytic, binding and structural functions were the most numerous and abundant, consistent with their role in the intracellular processing of the blood meal. The analysis of some groups of proteins putatively involved directly in blood meal digestion, including protein digestion (peptidase activity), iron metabolism, enzymes involved in oxidative stress and detoxification and membrane traffic and transport proteins, detected some differences between the fed and unfed ticks CONCLUSIONS: This work reports for the first time the collection and analysis of the midgut proteome of an argasid tick species and provides molecular information about the argasid machinery involved in blood digestion. This information represents a starting point for the identification and selection of new targets for the development of alternative control strategies.
Authors: Lenka Grunclová; Martin Horn; Marie Vancová; Daniel Sojka; Zdenek Franta; Michael Mares; Petr Kopácek Journal: Biol Chem Date: 2006-12 Impact factor: 3.915
Authors: M Canales; A Enríquez; E Ramos; D Cabrera; H Dandie; A Soto; V Falcón; M Rodríguez; J de la Fuente Journal: Vaccine Date: 1997-03 Impact factor: 3.641
Authors: K Sohn; L Orci; M Ravazzola; M Amherdt; M Bremser; F Lottspeich; K Fiedler; J B Helms; F T Wieland Journal: J Cell Biol Date: 1996-12 Impact factor: 10.539
Authors: Ricardo N Araujo; Naylene C S Silva; Antonio Mendes-Sousa; Rafaela Paim; Gabriel C A Costa; Luciana R Dias; Karla Oliveira; Mauricio R V Sant'Anna; Nelder F Gontijo; Marcos H Pereira; Grasielle D Pessoa; Jesus G Valenzuela; Leonardo B Koerich; Fabiano Oliveira Journal: Sci Rep Date: 2019-05-01 Impact factor: 4.379
Authors: Travis J Bourret; William K Boyle; Amanda K Zalud; Jesus G Valenzuela; Fabiano Oliveira; Job E Lopez Journal: Cell Microbiol Date: 2019-01-04 Impact factor: 3.715