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A Proteomic Analysis of Sarcoptes scabiei (Acari: Sarcoptidae).
Morgan, Marjorie S; Arlian, Larry G; Rider, S Dean; Grunwald, William C; Cool, David R.
Afiliación
  • Morgan MS; Department of Biological Sciences, Wright State University, Dayton, OH 45435 (marjorie.morgan@wright.edu; larry.arlian@wright.edu; s.dean.rider@wright.edu).
  • Arlian LG; Department of Biological Sciences, Wright State University, Dayton, OH 45435 (marjorie.morgan@wright.edu; larry.arlian@wright.edu; s.dean.rider@wright.edu), larry.arlian@wright.edu.
  • Rider SD; Department of Biological Sciences, Wright State University, Dayton, OH 45435 (marjorie.morgan@wright.edu; larry.arlian@wright.edu; s.dean.rider@wright.edu).
  • Grunwald WC; Department of Pharmacology & Toxicology, Boonshoft School of Medicine, Wright State University, Dayton, OH 45435 (william.grunwald@wright.edu; david.cool@wright.edu).
  • Cool DR; Department of Pharmacology & Toxicology, Boonshoft School of Medicine, Wright State University, Dayton, OH 45435 (william.grunwald@wright.edu; david.cool@wright.edu).
J Med Entomol ; 53(3): 553-561, 2016 05.
Article en En | MEDLINE | ID: mdl-26792847
The pruritic skin disease scabies is caused by the burrowing of the itch mite Sarcoptes scabiei (De Geer). It is difficult to diagnose this disease because its symptoms often resemble those of other skin diseases. No reliable blood or molecular diagnostic test is available. The aim of this project was to begin to characterize the scabies proteome to identify scabies mite proteins, including those that may be useful in the development of a diagnostic test or vaccine. Various scabies mite extracts were separated by two-dimensional electrophoresis, and 844 Coomassie Blue-stained protein spots were excised, subjected to trypsin digestion, and analyzed by Matrix Assisted Laser Desorption/Ionization Time-Of-Flight/Time-Of-Flight (MALDI-TOF/TOF) mass spectrometry (MS). Tryptic fragment sequences determined by MS were searched against the recently completed S. scabiei annotated genome, leading to the identification of >150 proteins. Only 10 proteins hit to previously identified scabies proteins including actin, tropomyosin, and several ABC transporters. Thirteen proteins had homology to dust mite allergens (members of groups 8, 10, 13, 17, 20, 25, and 28). Most other sequences showed some homology to proteins in other mites and ticks including homologs of calmodulin, calreticulin, lipocalin, and glutathione-S-transferase. These data will now allow the identification of the proteins to which scabies patients produce antibodies, including those that may be good candidates for inclusion in a diagnostic test and vaccine.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Sarcoptes scabiei / Escabiosis / Proteínas de Artrópodos Límite: Animals Idioma: En Revista: J Med Entomol Año: 2016 Tipo del documento: Article Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Sarcoptes scabiei / Escabiosis / Proteínas de Artrópodos Límite: Animals Idioma: En Revista: J Med Entomol Año: 2016 Tipo del documento: Article Pais de publicación: Reino Unido