Comparison of Silks from Pseudoips prasinana and Bombyx mori Shows Molecular Convergence in Fibroin Heavy Chains but Large Differences in Other Silk Components
Autor: | Hana Sehadova, Michal Zurovec, Lenka Rouhova, Michal Rindoš, Peter Konik, Miluše Hradilová, Lucie Kucerova, Michal Sery |
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Jazyk: | angličtina |
Rok vydání: | 2021 |
Předmět: |
QH301-705.5
Nolidae Fibroin 02 engineering and technology macromolecular substances phylogeny Catalysis Inorganic Chemistry Lepidoptera genitalia 03 medical and health sciences transcriptomics Bombyx mori Bena prasinana Physical and Theoretical Chemistry Biology (General) Molecular Biology QD1-999 Spectroscopy 030304 developmental biology 0303 health sciences Heavy chain biology Fibrohexamerin Chemistry Organic Chemistry fungi technology industry and agriculture General Medicine fibrohexamerins 021001 nanoscience & nanotechnology biology.organism_classification equipment and supplies Bombycidae Computer Science Applications Pupa Phylogenetic distance SILK Biochemistry 0210 nano-technology |
Zdroj: | International Journal of Molecular Sciences Volume 22 Issue 15 International Journal of Molecular Sciences, Vol 22, Iss 8246, p 8246 (2021) |
ISSN: | 1422-0067 |
DOI: | 10.3390/ijms22158246 |
Popis: | Many lepidopteran larvae produce silk feeding shelters and cocoons to protect themselves and the developing pupa. As caterpillars evolved, the quality of the silk, shape of the cocoon, and techniques in forming and leaving the cocoon underwent a number of changes. The silk of Pseudoips prasinana has previously been studied using X-ray analysis and classified in the same category as that of Bombyx mori, suggesting that silks of both species have similar properties despite their considerable phylogenetic distance. In the present study, we examined P. prasinana silk using ‘omics’ technology, including silk gland RNA sequencing (RNA-seq) and a mass spectrometry-based proteomic analysis of cocoon proteins. We found that although the central repetitive amino acid sequences encoding crystalline domains of fibroin heavy chain molecules are almost identical in both species, the resulting fibers exhibit quite different mechanical properties. Our results suggest that these differences are most probably due to the higher content of fibrohexamerin and fibrohexamerin-like molecules in P. prasinana silk. Furthermore, we show that whilst P. prasinana cocoons are predominantly made of silk similar to that of other Lepidoptera, they also contain a second, minor silk type, which is present only at the escape valve. |
Databáze: | OpenAIRE |
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