A comprehensive gene expression analysis of the unique three-layered cocoon of the cecropia moth, Hyalophora cecropia
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F24%3A00587772" target="_blank" >RIV/60077344:_____/24:00587772 - isvavai.cz</a>
Alternative codes found
RIV/60076658:12310/24:43908576
Result on the web
<a href="https://www.sciencedirect.com/science/article/pii/S0965174824000833/pdfft?md5=1d7c2018e13e72767b6aaa87d808527a&pid=1-s2.0-S0965174824000833-main.pdf" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0965174824000833/pdfft?md5=1d7c2018e13e72767b6aaa87d808527a&pid=1-s2.0-S0965174824000833-main.pdf</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.ibmb.2024.104152" target="_blank" >10.1016/j.ibmb.2024.104152</a>
Alternative languages
Result language
angličtina
Original language name
A comprehensive gene expression analysis of the unique three-layered cocoon of the cecropia moth, Hyalophora cecropia
Original language description
The larvae of the moth Hyalophora cecropia spin silk cocoons with morphologically distinct layers. We investigated the expression of the individual silk protein components of these cocoons in relation to the morphology of the silk gland and its affiliation to the different layers of the cocoon. The study used transcriptomic and proteomic analyses to identify 91 proteins associated with the silk cocoons, 63 of which have a signal peptide indicating their secretory nature. We checked the specificity of their expression in different parts of the SG and the presence of the corresponding protein products in each cocoon layer. Differences were observed among less abundant proteins with unclear functions. The representation of proteins in the inner envelope and intermediate space was similar, except for a higher proportion of probable contaminating proteins, mostly originating from the gut. On the other hand, the outer envelope contains a number of putative enzymes with unclear function. However, the protein most specific to the outer layer has sequence homology to putative serine/threonine kinaselike proteins and some adhesive proteins, and its closest homolog in Bombyx mori was found in the scaffold silk. This research provides valuable insights into the silk production of the cecropia moth, highlighting both similarities and differences to other moth species.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10605 - Developmental biology
Result continuities
Project
<a href="/en/project/LM2023050" target="_blank" >LM2023050: National Infrastructure for Biological and Medical Imaging</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2024
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Insect Biochemistry and Molecular Biology
ISSN
0965-1748
e-ISSN
1879-0240
Volume of the periodical
171
Issue of the periodical within the volume
AUG 2024
Country of publishing house
GB - UNITED KINGDOM
Number of pages
13
Pages from-to
104152
UT code for WoS article
001264095200001
EID of the result in the Scopus database
2-s2.0-85197037566