» Articles » PMID: 19221523

Silks Produced by Insect Labial Glands

Overview
Journal Prion
Specialty Biochemistry
Date 2009 Feb 18
PMID 19221523
Citations 19
Authors
Affiliations
Soon will be listed here.
Abstract

Insect silks are secreted from diverse gland types; this chapter deals with the silks produced by labial glands of Holometabola (insects with pupa in their life cycle). Labial silk glands are composed of a few tens or hundreds of large polyploid cells that secrete polymerizing proteins which are stored in the gland lumen as a semi-liquid gel. Polymerization is based on weak molecular interactions between repetitive amino acid motifs present in one or more silk proteins; cross-linking by disulfide bonds may be important in the silks spun under water. The mechanism of long-term storage of the silk dope inside the glands and its conversion into the silk fiber during spinning is not fully understood. The conversion occurs within seconds at ambient temperature and pressure, under minimal drawing force and in some cases under water. The silk filament is largely built of proteins called fibroins and in Lepidoptera and Trichoptera coated by glue-type proteins known as sericins. Silks often contain small amounts of additional proteins of poorly known function. The silk components controlling dope storage and filament formation seem to be conserved at the level of orders, while the nature of polymerizing motifs in the fibroins, which determine the physical properties of silk, differ at the level of family and even genus. Most silks are based on fibroin beta-sheets interrupted with other structures such as alpha-helices but the silk proteins of certain sawflies have predominantly a collagen-like or polyglycine II arrangement and the silks of social Hymenoptera are formed from proteins in a coiled coil arrangement.

Citing Articles

An effective protocol to isolate and mechanically test silk fibers spun by Osmia lignaria Say (Hymenoptera: Megachilidae) fifth instar larvae.

Wasserman O, Morley J, Williams M, Bell B, Cox-Foster D, Jones J PLoS One. 2025; 20(2):e0318918.

PMID: 40009637 PMC: 11864535. DOI: 10.1371/journal.pone.0318918.


Transcriptome and Neuroendocrinome Responses to Environmental Stress in the Model and Pest Insect .

Gong W, Lubawy J, Marciniak P, Smagghe G, Slocinska M, Liu D Int J Mol Sci. 2025; 26(2).

PMID: 39859404 PMC: 11766081. DOI: 10.3390/ijms26020691.


Characterization and comparative analysis of sericin protein 150 in Bombyx mori.

Wu B, Zabelina V, Zurovcova M, Zurovec M Sci Rep. 2024; 14(1):20990.

PMID: 39251726 PMC: 11385562. DOI: 10.1038/s41598-024-71503-2.


Disentangling the Web: An Interdisciplinary Review on the Potential and Feasibility of Spider Silk Bioproduction.

Guessous G, Blake L, Bui A, Woo Y, Manzanarez G ACS Biomater Sci Eng. 2024; 10(9):5412-5438.

PMID: 39136701 PMC: 11388149. DOI: 10.1021/acsbiomaterials.4c00145.


De Novo Long-Read Genome Assembly and Annotation of the Luna Moth (Actias luna) Fully Resolves Repeat-Rich Silk Genes.

Markee A, Godfrey R, Frandsen P, Weng Y, Triant D, Kawahara A Genome Biol Evol. 2024; 16(7).

PMID: 38957923 PMC: 11258402. DOI: 10.1093/gbe/evae148.


References
1.
Craig C . Evolution of arthropod silks. Annu Rev Entomol. 1997; 42:231-67. DOI: 10.1146/annurev.ento.42.1.231. View

2.
Yonemura N, Sehnal F, Mita K, Tamura T . Protein composition of silk filaments spun under water by caddisfly larvae. Biomacromolecules. 2006; 7(12):3370-8. DOI: 10.1021/bm060663u. View

3.
Takasu Y, Yamada H, Tsubouchi K . Isolation of three main sericin components from the cocoon of the silkworm, Bombyx mori. Biosci Biotechnol Biochem. 2003; 66(12):2715-8. DOI: 10.1271/bbb.66.2715. View

4.
Mita K, Ichimura S, James T . Highly repetitive structure and its organization of the silk fibroin gene. J Mol Evol. 1994; 38(6):583-92. DOI: 10.1007/BF00175878. View

5.
Tanaka K, Mizuno S . Homologues of fibroin L-chain and P25 of Bombyx mori are present in Dendrolimus spectabilis and Papilio xuthus but not detectable in Antheraea yamamai. Insect Biochem Mol Biol. 2001; 31(6-7):665-77. DOI: 10.1016/s0965-1748(00)00173-9. View