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Isolation, N-glycosylations and Function of a Hyaluronidase-Like Enzyme from the Venom of the Spider Cupiennius salei.

التفاصيل البيبلوغرافية
العنوان: Isolation, N-glycosylations and Function of a Hyaluronidase-Like Enzyme from the Venom of the Spider Cupiennius salei.
المؤلفون: Biner O; Department of Chemistry and Biochemistry, University of Bern, Bern, Switzerland., Trachsel C; Functional Genomics Center Zürich, University of Zürich/ETH Zürich, Zürich, Switzerland., Moser A; Institute of Ecology and Evolution, University of Bern, Bern, Switzerland., Kopp L; Department of Chemistry and Biochemistry, University of Bern, Bern, Switzerland., Langenegger N; Department of Chemistry and Biochemistry, University of Bern, Bern, Switzerland., Kämpfer U; Department of Chemistry and Biochemistry, University of Bern, Bern, Switzerland., von Ballmoos C; Department of Chemistry and Biochemistry, University of Bern, Bern, Switzerland., Nentwig W; Institute of Ecology and Evolution, University of Bern, Bern, Switzerland., Schürch S; Department of Chemistry and Biochemistry, University of Bern, Bern, Switzerland., Schaller J; Department of Chemistry and Biochemistry, University of Bern, Bern, Switzerland., Kuhn-Nentwig L; Institute of Ecology and Evolution, University of Bern, Bern, Switzerland.
المصدر: PloS one [PLoS One] 2015 Dec 02; Vol. 10 (12), pp. e0143963. Date of Electronic Publication: 2015 Dec 02 (Print Publication: 2015).
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Public Library of Science Country of Publication: United States NLM ID: 101285081 Publication Model: eCollection Cited Medium: Internet ISSN: 1932-6203 (Electronic) Linking ISSN: 19326203 NLM ISO Abbreviation: PLoS One Subsets: MEDLINE
أسماء مطبوعة: Original Publication: San Francisco, CA : Public Library of Science
مواضيع طبية MeSH: Hyaluronoglucosaminidase/*metabolism , Spider Venoms/*enzymology, Amino Acid Sequence ; Animals ; Base Sequence ; Glycosylation ; Hyaluronoglucosaminidase/chemistry ; Molecular Sequence Data ; Recombinant Proteins/chemistry ; Recombinant Proteins/metabolism ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Spiders ; Tandem Mass Spectrometry
مستخلص: Structure of Cupiennius Salei Venom Hyaluronidase: Hyaluronidases are important venom components acting as spreading factor of toxic compounds. In several studies this spreading effect was tested on vertebrate tissue. However, data about the spreading activity on invertebrates, the main prey organisms of spiders, are lacking. Here, a hyaluronidase-like enzyme was isolated from the venom of the spider Cupiennius salei. The amino acid sequence of the enzyme was determined by cDNA analysis of the venom gland transcriptome and confirmed by protein analysis. Two complex N-linked glycans akin to honey bee hyaluronidase glycosylations, were identified by tandem mass spectrometry. A C-terminal EGF-like domain was identified in spider hyaluronidase using InterPro. The spider hyaluronidase-like enzyme showed maximal activity at acidic pH, between 40-60°C, and 0.2 M KCl. Divalent ions did not enhance HA degradation activity, indicating that they are not recruited for catalysis.
Function of Venom Hyaluronidases: Besides hyaluronan, the enzyme degrades chondroitin sulfate A, whereas heparan sulfate and dermatan sulfate are not affected. The end products of hyaluronan degradation are tetramers, whereas chondroitin sulfate A is mainly degraded to hexamers. Identification of terminal N-acetylglucosamine or N-acetylgalactosamine at the reducing end of the oligomers identified the enzyme as an endo-β-N-acetyl-D-hexosaminidase hydrolase. The spreading effect of the hyaluronidase-like enzyme on invertebrate tissue was studied by coinjection of the enzyme with the Cupiennius salei main neurotoxin CsTx-1 into Drosophila flies. The enzyme significantly enhances the neurotoxic activity of CsTx-1. Comparative substrate degradation tests with hyaluronan, chondroitin sulfate A, dermatan sulfate, and heparan sulfate with venoms from 39 spider species from 21 families identified some spider families (Atypidae, Eresidae, Araneidae and Nephilidae) without activity of hyaluronidase-like enzymes. This is interpreted as a loss of this enzyme and fits quite well the current phylogenetic idea on a more isolated position of these families and can perhaps be explained by specialized prey catching techniques.
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المشرفين على المادة: 0 (Recombinant Proteins)
0 (Spider Venoms)
EC 3.2.1.35 (Hyaluronoglucosaminidase)
تواريخ الأحداث: Date Created: 20151203 Date Completed: 20160624 Latest Revision: 20181113
رمز التحديث: 20231215
مُعرف محوري في PubMed: PMC4667920
DOI: 10.1371/journal.pone.0143963
PMID: 26630650
قاعدة البيانات: MEDLINE
الوصف
تدمد:1932-6203
DOI:10.1371/journal.pone.0143963