Identification of Four Major Hornet Silk Genes with a Complex of Alanine-Rich and Serine-Rich Sequences in<i>Vespa simillima xanthoptera</i>Cameron

Sezutsu, Hideki; Kajiwara, Hideyuki; Kojima, Katsura; Mita, Kazuei; Tamura, Toshiki; Tamada, Yasushi; Kameda, Tsunenori

doi:10.1271/bbb.70326

Cited by 33 publications

(51 citation statements)

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“…15 Using coiled-coil prediction programs to search the heptad repeats of the primary structures, the location of potential coiled-coil domains in hornet silk proteins was predicted. 10 The results indicated that coiled-coil structures exist only in the Alarich domain, and not in the Ser-rich domains. From this result, we confirmed that a-helices exist in the Ala-rich domain, as the a-helix is a prerequisite for the formation of a coiled-coil structure.…”

Section: Introductionmentioning

confidence: 95%

“…[2][3][4] The structure of hornet silk has been reported in our recent studies. [5][6][7][8][9][10][11][12] The amino-acid sequences of six types of hornet silk proteins of Vespa simillima xanthoptera Cameron have been determined. 5,6,10 Of these six proteins, four are major and have similar characteristics.…”

Section: Introductionmentioning

confidence: 99%

“…[5][6][7][8][9][10][11][12] The amino-acid sequences of six types of hornet silk proteins of Vespa simillima xanthoptera Cameron have been determined. 5,6,10 Of these six proteins, four are major and have similar characteristics. These four major proteins consist of an alanine(Ala)-rich domain at the center of the chain and serine(Ser)-rich domains at both ends of the chain.…”

Section: Introductionmentioning

confidence: 99%

“…These four major proteins consist of an alanine(Ala)-rich domain at the center of the chain and serine(Ser)-rich domains at both ends of the chain. 6,10 Hornet silk proteins contain both a-helices and b-sheets. 12 In addition, hornet silk contains coiled-coil structures, 10 which are a common feature of the silks of the social Hymenoptera (bees, ants and hornets).…”

Section: Introductionmentioning

confidence: 99%

“…6,10 Hornet silk proteins contain both a-helices and b-sheets. 12 In addition, hornet silk contains coiled-coil structures, 10 which are a common feature of the silks of the social Hymenoptera (bees, ants and hornets). 3,13 The coiled-coil structure consists of several a-helices wound around each other.…”

Section: Introductionmentioning

confidence: 99%

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Quantifying the fraction of alanine residues in an α-helical conformation in hornet silk using solid-state NMR

Kameda

2012

Polym J

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Here, we demonstrate the first successful isotope labeling of Ala carbons in hornet silk produced by the larvae of Vespa (Vespinae, Vespidae) mandarinia. This labeled hornet silk was examined by high-resolution 13 C solid-state NMR, and it was found that the fraction of Ala residues in a-helical conformations compared with Ala residues in the overall conformation of hornet silk can be quantitatively determined from Ala C a NMR peaks. The value for this a-helical Ala fraction is close to that of the fraction of Ala residues in coiled-coil structures estimated in the four major hornet silk proteins by coiled-coil prediction analysis. This result indicates that most of the Ala residues in a-helices occur in those a-helices with a coiled-coil structure, and that the number of Ala residues in a-helices without a coiled-coil structure is small. Moreover, coiled-coil prediction analysis indicated that the potential coiled-coil domains are located only in the central portion of the protein chains of the major hornet silk proteins. From these results, we confirmed that the a-helical conformation mostly forms in the central portion of the hornet silk chains, whereas the ends of the protein chains are nearly devoid of a-helical structure. We deduce that the ends of the protein chains would preferentially adopt a b-sheet conformation.

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Section: Introductionmentioning

confidence: 95%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Quantifying the fraction of alanine residues in an α-helical conformation in hornet silk using solid-state NMR

Kameda

2012

Polym J

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The coiled coil silk of bees, ants, and hornets

et al. 2011

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In this article, we review current knowledge about the silk produced by the larvae of bees, ants, and hornets [Apoidea and Vespoidea: Hymenoptera]. Different species use the silk either alone or in composites for a variety of purposes including mechanical reinforcement, thermal regulation, or humidification. The characteristic molecular structure of this silk is α-helical proteins assembled into tetrameric coiled coils. Gene sequences from seven species are available, and each species possesses a copy of each of four related silk genes that encode proteins predicted to form coiled coils. The proteins are ordered at multiple length scales within the labial gland of the final larval instar before spinning. The insects control the morphology of the silk during spinning to produce either fibers or sheets. The silk proteins are small and non repetitive and have been produced artificially at high levels by fermentation in E. coli. The artificial silk proteins can be fabricated into materials with structural and mechanical properties similar to those of native silks.

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Influence of pH, temperature, and concentration on stabilization of aqueous hornet silk solution and fabrication of salt‐free materials

Kameda

2014

Biopolymers

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We found that an aqueous solution of silk from cocoons produced by hornet larvae (hornet silk) can be obtained when the solution is adjusted to basic conditions of pH > 9.2. It is known that native hornet cocoons can be dissolved in concentrated aqueous solution of salts, such as lithium bromide (LiBr) and calcium chloride (CaCl2). Upon the removal of these salts from solution by dialysis, solidification, gelation, or sedimentation of hornet silk is known to occur. In the present study, under basic conditions, however, no such solidification occurred, even after salt removal. In this study, ammonia was used for alkalization of solution because it is volatilized during the casting process and pure hornet silk materials can be obtained after drying. The effects of the concentrations of hornet silk and ammonia, as well as dialysis temperature, on preventing gelation during dialysis were investigated. Dialysis conditions that limit the degradation of hornet silk by hydrolysis in alkali solution were identified. Moreover, casting conditions to prepare flexible and transparent hornet silk film from aqueous ammonia solution were optimized. Molecular structural analysis of hornet silk in aqueous ammonia solution and cast film indicated the formation of α-helix conformations.

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Identification of Four Major Hornet Silk Genes with a Complex of Alanine-Rich and Serine-Rich Sequences inVespa simillima xanthopteraCameron

Cited by 33 publications

References 31 publications

Quantifying the fraction of alanine residues in an α-helical conformation in hornet silk using solid-state NMR

Quantifying the fraction of alanine residues in an α-helical conformation in hornet silk using solid-state NMR

The coiled coil silk of bees, ants, and hornets

Influence of pH, temperature, and concentration on stabilization of aqueous hornet silk solution and fabrication of salt‐free materials

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