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dc.contributor.author
Biner, Olivier
dc.contributor.author
Trachsel, Christian
dc.contributor.author
Moser, Aline
dc.contributor.author
Kopp, Lukas
dc.contributor.author
Langenegger, Nicolas
dc.contributor.author
Kämpfer, Urs
dc.contributor.author
von Ballmoos, Christoph
dc.contributor.author
Nentwig, Wolfgang
dc.contributor.author
Schürch, Stefan
dc.contributor.author
Schaller, Johann
dc.contributor.author
Kuhn-Nentwig, Lucia
dc.date.accessioned
2018-08-02T10:50:07Z
dc.date.available
2017-06-11T22:11:11Z
dc.date.available
2018-08-02T10:50:07Z
dc.date.issued
2015-12-02
dc.identifier.issn
1932-6203
dc.identifier.other
10.1371/journal.pone.0143963
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/108826
dc.identifier.doi
10.3929/ethz-b-000108826
dc.description.abstract
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.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
Public Library of Science
en_US
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.title
Isolation, N-glycosylations and Function of a Hyaluronidase-Like Enzyme from the Venom of the Spider Cupiennius salei
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 4.0 International
ethz.journal.title
PLoS ONE
ethz.journal.volume
10
en_US
ethz.journal.issue
12
en_US
ethz.journal.abbreviated
PLoS ONE
ethz.pages.start
e0143963
en_US
ethz.size
32 p.
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.identifier.wos
ethz.identifier.scopus
ethz.identifier.nebis
006206116
ethz.publication.place
San Francisco, CA
en_US
ethz.publication.status
published
en_US
ethz.leitzahl
ETH Zürich::00002 - ETH Zürich::00003 - Schulleitung und Dienste::00022 - Bereich VP Forschung & Wirtschaftsbez. / Domain VP Research & Corporate Relations::02207 - Functional Genomics Center Zürich / Functional Genomics Center Zürich
en_US
ethz.leitzahl.certified
ETH Zürich::00002 - ETH Zürich::00003 - Schulleitung und Dienste::00022 - Bereich VP Forschung & Wirtschaftsbez. / Domain VP Research & Corporate Relations::02207 - Functional Genomics Center Zürich / Functional Genomics Center Zürich
ethz.date.deposited
2017-06-11T22:12:03Z
ethz.source
ECIT
ethz.identifier.importid
imp593653d65ccbf94997
ethz.ecitpid
pub:169843
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2017-08-03T08:22:23Z
ethz.rosetta.lastUpdated
2018-11-07T17:41:11Z
ethz.rosetta.versionExported
true
ethz.COinS
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