Identification and characterization of sericin5 reveals non-cocoon silk sericin components with high β-sheet content and adhesive strength

Guo, Kaiyu; Zhang, Xiaolu; Zhao, Dongfang; Qin, Lixia; Jiang, Wenchao; Liu, Xiao; Xia, Qingyou; Dong, Zhaoming; Zhao, Ping

doi:10.1016/j.actbio.2022.07.021

Cited by 34 publications

(17 citation statements)

References 65 publications

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“…The P150/Ser6 protein product of B. mori is found mainly in the inner cocoon layer formed at the end of the last instar and also in the non-cocoon silk from earlier instar larvae, as suggested by the data of Dong et al [28]. Consistently, Ser2, Ser4 and Ser5 are present in the non-cocoon silk [9][10][11]. Noncocoon silk has previously been associated with the initial stage of silk spinning and is responsible for holding the molting larva and fixing the cocoon to a suitable substrate [11].…”

Section: Discussionmentioning

confidence: 68%

“…Silkworm mutants carrying a truncated ser1 gene failed to spin or produced coarse cocoons, suggesting that it is involved in reducing friction during spinning [8]. The product of another sericin gene, sericin 2 (Ser2), and the products of two recently identified genes sericin 4 (Ser4) and sericin 5 (Ser5), have been described in non-cocoon silk and are spun by younger larvae (including early last instar larvae) [9][10][11][12]. The presence of Ser2, Ser4, and Ser5 in non-cocoon silks suggests that they may have a specific function during these developmental stages.…”

Section: Introductionmentioning

confidence: 99%

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Unravelling the complexity of silk sericins:P150/sericin 6is a new silk gene inBombyx mori

Wu,

Zabelina,

Zurovcova

et al. 2023

Preprint

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Sericins are a small family of highly divergent proteins that serve as adhesives and coatings for silk fibers and are produced in the middle part of the silk gland. So far, five genes encoding sericin proteins have been found in Bombyx mori. Sericins 1 and 3 are responsible for silk adhesion in the cocoon, while sericins 2, 4, and 5 are present in non-cocoon spun silk of younger larvae (including the early last instar). We found a new gene, which we named P150/sericin 6, which appears to be an ortholog of the sericin-like protein previously found in Galleria mellonella. The B. mori sequence of the P150/sericin 6 ORF was previously incorrectly predicted and assigned to two smaller, uncharacterized genes. We present a new P150/sericin 6 gene model and show that it encodes a large protein of 467 kDa. It is characterized by repeats with a high proportion of threonine residues and a short conserved region with a cysteine knot motif (CXCXCX) at the C-terminus. Expression analysis has shown that B. mori P150/ser6 has low transcriptional level in contrast to its G. mellonella homolog. We also discuss the synteny of homologous genes on corresponding chromosomes between moth species and possible phylogenetic relationships between P150/ser6 and cysteine knot mucins. Our results improve our understanding of the evolutionary relationships between adhesion proteins in different lepidopteran species.

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Section: Discussionmentioning

confidence: 68%

Section: Introductionmentioning

confidence: 99%

Unravelling the complexity of silk sericins:P150/sericin 6is a new silk gene inBombyx mori

Wu,

Zabelina,

Zurovcova

et al. 2023

Preprint

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“…Thirty‐four uncharacterized proteins were predicted as secreted proteins and to be putative silk proteins. Interestingly, we identified three sericin candidates (Gly/Ser‐rich protein, Ser/Gly‐rich protein and Ser/Glu‐rich protein) from these putative silk proteins based on their sericin‐like features (Dong et al, 2019; Garel et al, 1997; Guo et al, 2022; Kludkiewicz et al, 2009; Takasu et al, 2007): huge protein sizes (>80 kDa), signal peptides, rich in hydrophilic amino acids such as serine, highly repetitive motifs and present in the silk. Future studies should examine their localization in the caddisworm silk and determine their adhesion to confirm whether they are sericins.…”

Section: Discussionmentioning

confidence: 99%

The silk gland proteome of Stenopsyche angustata provides insights into the underwater silk secretion

Wang,

Liu,

Liu

et al. 2023

Insect Molecular Biology

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Caddisworms (Trichoptera) spin adhesive silks to construct a variety of underwater composite structures. Many studies have focused on the fibroin heavy chain of caddisworm silk and found that it contains heavy phosphorylation to maintain a stable secondary structure. Besides fibroins, recent studies have also identified some new silk proteins within caddisworm silk. To better understand the silk composition and its secretion process, this study reports the silk gland proteome of a retreat‐building caddisworm, Stenopsyche angustata Martynov (Trichoptera, Stenopsychidae). Using liquid chromatography tandem mass spectrometry (LC‐MS/MS), 2389 proteins were identified in the silk gland of S. angustata, among which 192 were predicted as secreted silk proteins. Twenty‐nine proteins were found to be enriched in the front silk gland, whereas 109 proteins were enriched in the caudal silk gland. The fibroin heavy chain and nine uncharacterized silk proteins were identified as phosphorylated proteins. By analysing the sequence of the fibroin heavy chain, we found that it contains 13 Gly/Thr/Pro‐rich regions, 12 Val/Ser/Arg‐rich regions and a Gly/Arg/Thr‐rich region. Three uncharacterized proteins were identified as sericin‐like proteins due to their larger molecular weights, signal peptides and repetitive motifs rich in serine. This study provides valuable information for further clarifying the secretion and adhesion of underwater caddisworm silk.

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“…Sericin’s adhesive property is significantly influenced by the presence of basic amino acids and high hydrophilicity. Sericin in its original state on the cocoon has stronger overall binding abilities due to the abundance of polar amino acid residues and a strong water affinity. , After profiling of B. mori sericin 4, sericin 5, a novel sericin that can only be found in noncocoon silk, was identified by Guo et al They discovered that the native sericin’s adhesive power steadily increases from the inner to the outside layer. By coassembling sericin protein and tannic acid, Liu et al developed self-hydrophobized sericin with strong (between 0.5 and 0.1 MPa) underwater adhesion that could be recycled (5 cycles).…”

Section: Applications Of Sericin As a Functional Biomaterialsmentioning

confidence: 99%

Waste to Wealth: Exploring the Versatile Prospects of Discarded Silk Sericin

Sabu Mathew,

Maria,

Allardyce

et al. 2024

ACS Sustainable Chem. Eng.

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Biorefinery, the process of converting biomass to valueadded materials, is gaining significant interest because of the depletion of natural resources and an increasing awareness of the need for sustainable development and material production. Silk sericin, an abundantly available byproduct of the sericulture industry, has been identified for biorefinery usage since it is biodegradable, bioavailable, pH and temperatureresponsive, naturally photoluminescent, has antioxidant properties, and is a GRAS and FDA-safe food additive. This Perspective examines the properties of sericin and its sources and discusses currently explored applications, including as a delivery system for drugs or genetic material, for wound healing, tissue engineering, media supplements, cosmetology, packaging materials, edible coating, and as bio adhesives. This Perspective examines the sources of sericin, its properties, and some of the currently explored applications. These include biomedical applications such as a delivery system for drugs or genetic material, wound healing, tissue engineering, media supplements, cosmetology, packaging materials, edible coating, and as bio adhesives. Finally, we highlight the recent developments in sericin modification to functionalize it for specific applications; this is a promising future direction that will further enhance the potential use of this valuable biomass.

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Identification and characterization of sericin5 reveals non-cocoon silk sericin components with high β-sheet content and adhesive strength

Cited by 34 publications

References 65 publications

Unravelling the complexity of silk sericins:P150/sericin 6is a new silk gene inBombyx mori

Unravelling the complexity of silk sericins:P150/sericin 6is a new silk gene inBombyx mori

The silk gland proteome of Stenopsyche angustata provides insights into the underwater silk secretion

Waste to Wealth: Exploring the Versatile Prospects of Discarded Silk Sericin

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