Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Asp-ase Activity of the Opossum Granzyme B Supports the Role of Granzyme B as Part of Anti-Viral Immunity Already during Early Mammalian Evolution
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Chemical Biology.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Chemical Biology.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Chemical Biology.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Chemical Biology.
2016 (English)In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 11, no 5, e0154886Article in journal (Refereed) Published
Resource type
Text
Abstract [en]

Granzyme B is one of the key effector molecules in our defense against viruses and intracellular bacteria. This serine protease together with the pore forming protein perforin, induces caspase or Bid-dependent apoptosis in target cells. Here we present the first characterization of a granzyme B homolog, the grathepsodenase, in a non-placental mammal, the American opossum (Monodelphis domestica). The recombinant enzyme was produced in a human cell line and used to study its primary and extended cleavage specificity using a panel of chromogenic substrates and recombinant protein substrates. The opossum granzyme B was found to have a specificity similar to human granzyme B, although slightly less restrictive in its extended specificity. The identification of a granzyme B homolog with asp-ase (cleaving after aspartic acid) specificity in a non-placental mammal provides strong indications that caspase or Bid-dependent apoptosis by a serine protease with a conserved primary specificity has been part of anti-viral immunity since early mammalian evolution. This finding also indicates that an asp-ase together with a chymase were the first two serine protease genes to appear in the mammalian chymase locus.

Place, publisher, year, edition, pages
2016. Vol. 11, no 5, e0154886
National Category
Evolutionary Biology
Identifiers
URN: urn:nbn:se:uu:diva-297790DOI: 10.1371/journal.pone.0154886ISI: 000375677000044PubMedID: 27152961OAI: oai:DiVA.org:uu-297790DiVA: diva2:943555
Funder
Swedish Research Council, 621-2011-5007
Available from: 2016-06-28 Created: 2016-06-28 Last updated: 2017-11-28Bibliographically approved

Open Access in DiVA

fulltext(10794 kB)198 downloads
File information
File name FULLTEXT01.pdfFile size 10794 kBChecksum SHA-512
538e87679d4b1124e7f7e5eae28bb3f61e15191bede5f3114c76c4900586efa719acbb0d62c8fe23c0cef98216b01f53d2ab9fa9c0e3c5f35f8c3e4e6e78f85b
Type fulltextMimetype application/pdf

Other links

Publisher's full textPubMed

Authority records BETA

Akula, SrinivasHellman, Lars

Search in DiVA

By author/editor
Akula, SrinivasHellman, Lars
By organisation
Chemical Biology
In the same journal
PLoS ONE
Evolutionary Biology

Search outside of DiVA

GoogleGoogle Scholar
Total: 198 downloads
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 476 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf