The expansion of genes encoding soluble silk components in the greater wax moth, Galleria mellonella
| Autor: | Hana Sehadova, Peter Konik, Miluše Hradilová, Barbara Kludkiewicz, Lucie Kucerova, Anna Zaloudikova, František Sehnal, Tereza Konikova, Hynek Strnad, Michal Zurovec |
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| Rok vydání: | 2019 |
| Předmět: |
0106 biological sciences
Proteome Silk Fibroin macromolecular substances Moths Proteomics 01 natural sciences Biochemistry Sericin Lepidoptera genitalia 03 medical and health sciences Labial glands Animals Amino Acid Sequence Sericins Molecular Biology Phylogeny Glycoproteins 030304 developmental biology 0303 health sciences Base Sequence biology fungi Mucins technology industry and agriculture equipment and supplies biology.organism_classification Galleria mellonella 010602 entomology SILK Secretory protein Larva Insect Science Insect Proteins Sequence Alignment |
| Zdroj: | Insect Biochemistry and Molecular Biology. 106:28-38 |
| ISSN: | 0965-1748 |
| DOI: | 10.1016/j.ibmb.2018.11.003 |
| Popis: | Lepidopteran silk is a complex assembly of proteins produced by a pair of highly specialized labial glands called silk glands. Silk composition has been examined only in a handful of species. Here we report on the analysis of silk gland-specific transcriptomes from three developmental stages of the greater wax moth, Galleria mellonella, combined with proteomics, Edman microsequencing and northern blot analysis. In addition to the genes known earlier, we identified twenty seven candidate cDNAs predicted to encode secretory proteins, which may represent novel silk components. Eight were verified by proteomic analysis or microsequencing, and several others were confirmed by similarity with known silk genes and their expression patterns. Our results revealed that most candidates encode abundant secreted proteins produced by middle silk glands including ten sericins, two seroins, one or more mucins, and several sequences without apparent similarity to known proteins. We did not detect any novel PSG-specific protein, confirming that there are only three fibroin subunits. Our data not only show that the number of sericin genes in the greater wax moth is higher than in other species thus far examined, but also the total content of soluble proteins in silk is twice as high in G. mellonella than in B. mori or A. yamamai. Our data will serve as a foundation for future identification and evolutionary analysis of silk proteins in the Lepidoptera. |
| Databáze: | OpenAIRE |
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