Biochemical properties of the major proteins from Rhodnius prolixus eggshell
| Autor: | Luciano Neves de Medeiros, Narcisa L. Cunha-e-Silva, Heloisa S.L. Coelho, Lilian Soares da Cunha Gomes, Eleonora Kurtenbach, Sonia Rozental, Gabriela O. Paiva-Silva, Mário A.C. Silva-Neto, Adriano Penha Furtado, Marcos Henrique Ferreira Sorgine, Ana C.A. Melo, Wanderley de Souza, Hatisaburo Masuda, Adriana Lyn Hunter Andrade, Denise Marie Delgado Bouts, Eduardo Corrêa Martins de Aguiar |
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| Rok vydání: | 2007 |
| Předmět: |
Antifungal Agents
Molecular Sequence Data Embryonic Development Microbial Sensitivity Tests Biochemistry Cell wall Sequence Analysis Protein Protein biosynthesis Animals Amino Acid Sequence Cloning Molecular Eggshell Rhodnius prolixus Molecular Biology Peptide sequence Ovum chemistry.chemical_classification biology Egg Proteins Vitellogenesis biology.organism_classification Amino acid Secretory protein chemistry Rhodnius Insect Science Insect Proteins Aspergillus niger Sequence Alignment |
| Zdroj: | Insect Biochemistry and Molecular Biology. 37:1207-1221 |
| ISSN: | 0965-1748 |
| DOI: | 10.1016/j.ibmb.2007.07.010 |
| Popis: | Two proteins from the eggshell of Rhodnius prolixus were isolated, characterized and named Rp30 and Rp45 according to their molecular masses. Purified proteins were used to obtain specific antiserum which was later used for immunolocalization. The antiserum against Rp30 and Rp45 detected their presence inside the follicle cells, their secretion and their association with oocyte microvilli. Both proteins are expressed during the final stage of vitellogenesis, preserved during embryogenesis and discarded together with the eggshell. The amino terminals were sequenced and both proteins were further cloned using degenerated primers. The amino acid sequences appear to have a tripartite arrangement with a highly conserved central domain which presents a repetitive motif of valine-proline-valine (VPV) at intervals of 15 amino acid residues. Their amino acid sequence showed no similarity to any known eggshell protein. The expression of these proteins was also investigated; the results demonstrated that this occurred strictly in choriogenic follicles. Antifungal activity against Aspergillus niger was found to be associated with Rp45 but not with Rp30. A. niger exposed to Rp45 protein induced growth inhibition and several morphological changes such as large vacuoles, swollen mitochondria, multi-lamellar structures and a disorganized cell wall as demonstrated by electron microscopy analysis. |
| Databáze: | OpenAIRE |
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