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Analysis of the Full-Length Pyriform Spidroin Gene Sequence

Spiders often produce multiple types of silk, each with unique properties suiting them to certain tasks and biological functions. Orb-weaver spiders can generate more than six types of silk fibroins, with pyriform silk used to form attachment discs, adhering silk to other surfaces and substances. Th...

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Autores principales: Wang, Kangkang, Wen, Rui, Jia, Qiupin, Liu, Xiangqin, Xiao, Junhua, Meng, Qing
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6627382/
https://www.ncbi.nlm.nih.gov/pubmed/31163680
http://dx.doi.org/10.3390/genes10060425
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author Wang, Kangkang
Wen, Rui
Jia, Qiupin
Liu, Xiangqin
Xiao, Junhua
Meng, Qing
author_facet Wang, Kangkang
Wen, Rui
Jia, Qiupin
Liu, Xiangqin
Xiao, Junhua
Meng, Qing
author_sort Wang, Kangkang
collection PubMed
description Spiders often produce multiple types of silk, each with unique properties suiting them to certain tasks and biological functions. Orb-weaver spiders can generate more than six types of silk fibroins, with pyriform silk used to form attachment discs, adhering silk to other surfaces and substances. The unique higher-order structuring of silk fibroins has been cited as the source of their remarkable biomechanical properties. Even so, only one full-length gene sequence of pyriform silk protein 1 (PySp1) from Argiopeargentata has been reported, and studies on the mechanical properties of natural pyriform silk fibers are also lacking. To better understand the PySp1 family of genes, we used long-distance PCR (LD-PCR) to determine the sequence of PySp1 in the Araneusventricosus species. This full-length PySp1 gene is 11,931 bp in length, encoding for 3976 amino acids residues in non-repetitive N- and C-terminal domains with a central largely repetitive region made up of sixteen remarkably homogeneous units. This was similar to the previously reported A. argentata PySp1 sequence, with PySp1 from A. ventricosus also having a long repetitive N-linker that bridges the N-terminal and repetitive regions. Predictions of secondary structure and hydrophobicity of A. ventricosus PySp1 showed the pyriform silk fiber’s functional properties. The amino acid compositions of PySp1 is obviously distinct from other spidroins. Our sequence makes an important contribution to understand pyriform silk protein structure and also provides a new template for recombinant pyriform silk proteins with attractive properties.
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spelling pubmed-66273822019-07-23 Analysis of the Full-Length Pyriform Spidroin Gene Sequence Wang, Kangkang Wen, Rui Jia, Qiupin Liu, Xiangqin Xiao, Junhua Meng, Qing Genes (Basel) Article Spiders often produce multiple types of silk, each with unique properties suiting them to certain tasks and biological functions. Orb-weaver spiders can generate more than six types of silk fibroins, with pyriform silk used to form attachment discs, adhering silk to other surfaces and substances. The unique higher-order structuring of silk fibroins has been cited as the source of their remarkable biomechanical properties. Even so, only one full-length gene sequence of pyriform silk protein 1 (PySp1) from Argiopeargentata has been reported, and studies on the mechanical properties of natural pyriform silk fibers are also lacking. To better understand the PySp1 family of genes, we used long-distance PCR (LD-PCR) to determine the sequence of PySp1 in the Araneusventricosus species. This full-length PySp1 gene is 11,931 bp in length, encoding for 3976 amino acids residues in non-repetitive N- and C-terminal domains with a central largely repetitive region made up of sixteen remarkably homogeneous units. This was similar to the previously reported A. argentata PySp1 sequence, with PySp1 from A. ventricosus also having a long repetitive N-linker that bridges the N-terminal and repetitive regions. Predictions of secondary structure and hydrophobicity of A. ventricosus PySp1 showed the pyriform silk fiber’s functional properties. The amino acid compositions of PySp1 is obviously distinct from other spidroins. Our sequence makes an important contribution to understand pyriform silk protein structure and also provides a new template for recombinant pyriform silk proteins with attractive properties. MDPI 2019-06-03 /pmc/articles/PMC6627382/ /pubmed/31163680 http://dx.doi.org/10.3390/genes10060425 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Wang, Kangkang
Wen, Rui
Jia, Qiupin
Liu, Xiangqin
Xiao, Junhua
Meng, Qing
Analysis of the Full-Length Pyriform Spidroin Gene Sequence
title Analysis of the Full-Length Pyriform Spidroin Gene Sequence
title_full Analysis of the Full-Length Pyriform Spidroin Gene Sequence
title_fullStr Analysis of the Full-Length Pyriform Spidroin Gene Sequence
title_full_unstemmed Analysis of the Full-Length Pyriform Spidroin Gene Sequence
title_short Analysis of the Full-Length Pyriform Spidroin Gene Sequence
title_sort analysis of the full-length pyriform spidroin gene sequence
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6627382/
https://www.ncbi.nlm.nih.gov/pubmed/31163680
http://dx.doi.org/10.3390/genes10060425
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