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Spider minor ampullate silk proteins are constituents of prey wrapping silk in the cob weaver Latrodectus hesperus.
Biochemistry 2008; 47(16):4692-700B

Abstract

Spiders spin high performance fibers with diverse biological functions and mechanical properties. Molecular and biochemical studies of spider prey wrapping silks have revealed the presence of the aciniform silk fibroin AcSp1-like. In our studies we demonstrate the presence of a second distinct polypeptide present within prey wrapping silk. Combining matrix-assisted laser desorption ionization tandem time-of-flight mass spectrometry and reverse genetics, we have isolated a novel gene called MiSp1-like and demonstrate that its protein product is a constituent of prey wrap silks from the black widow spider, Latrodectus hesperus. BLAST searches of the NCBInr protein database using the amino acid sequence of MiSp1-like revealed similarity to the conserved C-terminal domain of silk family members. In particular, MiSp1-like showed the highest degree of sequence similarity to the nonrepetitive C-termini of published orb-weaver minor ampullate fibroin molecules. Analysis of the internal amino acid sequence of the black widow MiSp1-like revealed polyalanine stretches interrupted by glycine residues and glycine-alanine couplets within MiSp1-like as well as repeats of the heptameric sequence AGGYGQG. Real-time quantitative PCR analysis demonstrates that the MiSp1-like gene displays a minor ampullate gland-restricted pattern of expression. Furthermore, amino acid composition analysis, coupled with scanning electron microscopy of raw wrapping silk, supports the assertion that minor ampullate silks are important constituents of black widow spider prey wrap silk. Collectively, our findings provide direct molecular evidence for the involvement of minor ampullate fibroins in swathing silks and suggest composite materials play an important role in the wrap attack process for cob-weavers.

Authors+Show Affiliations

Department of Biology, University of the Pacific, Stockton, CA 95211, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, Non-P.H.S.

Language

eng

PubMed ID

18376847

Citation

La Mattina, Coby, et al. "Spider Minor Ampullate Silk Proteins Are Constituents of Prey Wrapping Silk in the Cob Weaver Latrodectus Hesperus." Biochemistry, vol. 47, no. 16, 2008, pp. 4692-700.
La Mattina C, Reza R, Hu X, et al. Spider minor ampullate silk proteins are constituents of prey wrapping silk in the cob weaver Latrodectus hesperus. Biochemistry. 2008;47(16):4692-700.
La Mattina, C., Reza, R., Hu, X., Falick, A. M., Vasanthavada, K., McNary, S., ... Vierra, C. A. (2008). Spider minor ampullate silk proteins are constituents of prey wrapping silk in the cob weaver Latrodectus hesperus. Biochemistry, 47(16), pp. 4692-700. doi:10.1021/bi800140q.
La Mattina C, et al. Spider Minor Ampullate Silk Proteins Are Constituents of Prey Wrapping Silk in the Cob Weaver Latrodectus Hesperus. Biochemistry. 2008 Apr 22;47(16):4692-700. PubMed PMID: 18376847.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Spider minor ampullate silk proteins are constituents of prey wrapping silk in the cob weaver Latrodectus hesperus. AU - La Mattina,Coby, AU - Reza,Ryan, AU - Hu,Xiaoyi, AU - Falick,Arnold M, AU - Vasanthavada,Keshav, AU - McNary,Shannon, AU - Yee,Russell, AU - Vierra,Craig A, Y1 - 2008/04/01/ PY - 2008/4/2/pubmed PY - 2008/6/11/medline PY - 2008/4/2/entrez SP - 4692 EP - 700 JF - Biochemistry JO - Biochemistry VL - 47 IS - 16 N2 - Spiders spin high performance fibers with diverse biological functions and mechanical properties. Molecular and biochemical studies of spider prey wrapping silks have revealed the presence of the aciniform silk fibroin AcSp1-like. In our studies we demonstrate the presence of a second distinct polypeptide present within prey wrapping silk. Combining matrix-assisted laser desorption ionization tandem time-of-flight mass spectrometry and reverse genetics, we have isolated a novel gene called MiSp1-like and demonstrate that its protein product is a constituent of prey wrap silks from the black widow spider, Latrodectus hesperus. BLAST searches of the NCBInr protein database using the amino acid sequence of MiSp1-like revealed similarity to the conserved C-terminal domain of silk family members. In particular, MiSp1-like showed the highest degree of sequence similarity to the nonrepetitive C-termini of published orb-weaver minor ampullate fibroin molecules. Analysis of the internal amino acid sequence of the black widow MiSp1-like revealed polyalanine stretches interrupted by glycine residues and glycine-alanine couplets within MiSp1-like as well as repeats of the heptameric sequence AGGYGQG. Real-time quantitative PCR analysis demonstrates that the MiSp1-like gene displays a minor ampullate gland-restricted pattern of expression. Furthermore, amino acid composition analysis, coupled with scanning electron microscopy of raw wrapping silk, supports the assertion that minor ampullate silks are important constituents of black widow spider prey wrap silk. Collectively, our findings provide direct molecular evidence for the involvement of minor ampullate fibroins in swathing silks and suggest composite materials play an important role in the wrap attack process for cob-weavers. SN - 0006-2960 UR - https://www.unboundmedicine.com/medline/citation/18376847/Spider_minor_ampullate_silk_proteins_are_constituents_of_prey_wrapping_silk_in_the_cob_weaver_Latrodectus_hesperus_ L2 - https://dx.doi.org/10.1021/bi800140q DB - PRIME DP - Unbound Medicine ER -