Characterization of Underwater Silk Proteins from Caddisfly Larva, Stenopsyche marmorata

Ohkawa, Kousaku; Nomura, Toshihiro; Arai, Ryoichi; Abe, Kôji; Tsukada, Masaru; Hirabayashi, Kimio

doi:10.1007/978-94-007-7119-2_6

Cited by 6 publications

(6 citation statements)

References 34 publications

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“…1B and Table S4). The experimental analysis of the amino acid composition indicated that Smsp-4 highly contained Gly (20.3 mol%), Trp (8.9 mol%), His (7.5 mol%), and Ser (7.3 mol%) [3,6], which is roughly consistent with that deduced from the cDNA of Smsp-4 (Table S5). The molecular mass of Smsp-4 without the signal sequence is calculated to be 12.4 kDa, which is a roughly reasonable value compared to ~16-17 kDa estimated by SDS-PAGE considering experimental errors and/or potential post-translational modifications.…”

Section: Recombinant Protein Expression In Escherichia Colisupporting

confidence: 75%

“…Stenopsyche marmorata (suborder Annulipalpia, called "retreat-maker") is one of the most common large caddisflies in rivers in Japan, such as the Chikuma (Shinano) River [1]. The larvae feed, mature, and pupate underwater and spin aquatic adhesive silk to build essential structures including food capture nets and protective nests [2,3]. Research on silk proteins from caddisfly larvae could lead to novel biopolymer materials for underwater adhesive and biomedical purposes [4].…”

Section: Introductionmentioning

confidence: 99%

“…The high-molecular-mass protein (>~300 kDa) was designated as Smsp-1; the three low-molecular-mass proteins were designated as Smsp-2, Smsp-3, and Smsp-4 (~26-32 kDa, ~21-26 kDa, and ~16-17 kDa, respectively, in SDS-PAGE analysis) [3,5,6]. We also reported the biochemical characterization and amino acid sequences of Smsp-1 that are the major component of the larval net silk/adhesive precursor [3,6]. However, detailed molecular information on Smsp-2, Smsp-3, and Smsp-4 is still unknown.…”

Section: Introductionmentioning

confidence: 99%

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Molecular cloning, gene expression analysis, and recombinant protein expression of novel silk proteins from larvae of a retreat-maker caddisfly, Stenopsyche marmorata

Bai

Sakaguchi

Yamaguchi

et al. 2015

Biochemical and Biophysical Research Communications

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Section: Recombinant Protein Expression In Escherichia Colisupporting

confidence: 75%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Molecular cloning, gene expression analysis, and recombinant protein expression of novel silk proteins from larvae of a retreat-maker caddisfly, Stenopsyche marmorata

Bai

Sakaguchi

Yamaguchi

et al. 2015

Biochemical and Biophysical Research Communications

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“…Among them, the posterior silk glands secrete the gelatinous silk components -broin, which is the main silk component in the cocoons of the silk moth. Ohkawa et al (2014) puri ed a silk protein from caddis y larva Stenopsyche marmorata, and Ashton et al (2012) studied the morphology and biochemical traits of adhesive silk of aquatic caddisworms. They found that the silk glands of caddisworm form Z-type silk glands, which belong to complex glands according to the structural complexity.…”

Section: Discussionmentioning

confidence: 99%

Fine structure of the silk spinning system in the caddisworm, Hydatophylax nigrovittatus (Trichoptera: Limnephilidae)

Kim

Sun

Moon

2020

Preprint

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Silk is produced by a variety of insects, but only silk made by terrestrial arthropods has been examined in detail. To fill the gap, this study was designed to understand the silk spinning system of aquatic insect. The larvae of caddis flies, Hydatophylax nigrovittatus produce silk through a pair of labial silk glands and use raw silk to protect themselves in the aquatic environment. The result of this study clearly shows that although silk fibers are made under aquatic conditions, the cellular silk production system is quite similar to that of terrestrial arthropods. Typically, silk production in caddisworm has been achieved by two independent processes in the silk glands. This includes the synthesis of silk fibroin in the posterior region, the production of adhesive glycoproteins in the anterior region, which are ultimately accumulated into functional silk dope and converted to a silk ribbon coated with gluey substances. At the cellular level, each substance of fibroin and glycoprotein is specifically synthesized at different locations, and then transported from the rough ER to the Golgi apparatus as transport vesicles, respectively. Thereafter, the secretory vesicles gradually increase in size by vesicular fusion, forming larger secretory granules containing specific proteins. It was found that these granules eventually migrate to the apical membrane and are exocytosed into the lumen by a mechanism of merocrine secretion.

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“…honeybees, crickets, ants, hornets, lacewings, silverfish, caddis flies and chironomid midges (Weisman et al, 2008;Sehnal and Sutherland, 2008;Sutherland et al 2010;Walker et al, 2012;Sutherland et al, 2011). In the purview of aquatic silks spun underwater, the retreat maker caddisworms (Stewart and Wang 2010;Tsukada et al, 2010;Ohkawa et al, 2014;Ashton et al, 2016) and larval chironomid midges (Grossbach, 1977;Hertner et al, 1980;Wellman and Case, 1989;Case et al, 1994) have exhibited how habitats influence the nature, composition and properties of silk. This review focusses on the underexplored silk-spinning expertise and the little known physiological biochemistry of silk protein produced by Chironomus larvae.…”

Section: Introductionmentioning

confidence: 99%

Aquatic silk proteins in Chironomus: A review

Thorat

Nath

2018

J Limnol

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Silk proteins secreted by salivary glands in the dipteran insect, Chironomus play a significant role as proteinaceous adhesives for construction of underwater housing nests by larvae. To date, only three Chironomus species, C. tentans Fabricius, C. pallidivittatus Malloch and C. riparius Meigen have been explored for characterization of their aquatic silk protein. Genes coding for silk proteins are located on specific chromosomal 'puffs' called Balbiani rings as well as non-Balbiani ring regions. Expression of these genes is closely regulated by developmental and hormonal alterations and environmental factors. Furthermore, pilot studies have postulated that silk proteins probably occur in diverse size classes grouped into large (~1000 kDa), intermediate (100-200 kDa) and small (≤100 kDa). Barring few preliminary reports that date back to the 1990s, the physical and bioproperties of silk from chironomid midges remain largely unknown, leading to paucity of updated information. This review was therefore aimed to compile existing literature database and to highlight the wide possibilities for commercialization of midge larval silk as a novel biopolymer.

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Characterization of Underwater Silk Proteins from Caddisfly Larva, Stenopsyche marmorata

Cited by 6 publications

References 34 publications

Molecular cloning, gene expression analysis, and recombinant protein expression of novel silk proteins from larvae of a retreat-maker caddisfly, Stenopsyche marmorata

Molecular cloning, gene expression analysis, and recombinant protein expression of novel silk proteins from larvae of a retreat-maker caddisfly, Stenopsyche marmorata

Fine structure of the silk spinning system in the caddisworm, Hydatophylax nigrovittatus (Trichoptera: Limnephilidae)

Aquatic silk proteins in Chironomus: A review

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