Evidence map›Paper›PMID 29947943›Full record

ArticleImmunogenetics2018

Identification and annotation of bovine granzyme genes reveals a novel granzyme encoded within the trypsin-like locus.

Jie Yang, Christina Vrettou, Tim Connelley, W Ivan Morrison

Open access · hybridAbstract read
In one paragraph

Article in Immunogenetics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.7field-weighted citation impact, top 33% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

5 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Granzymes: The Molecular Executors of Immune-Mediated Cytotoxicity.International journal of molecular sciences · 2022
    Review
  3. Article
  4. Article
  5. Granzyme B Is an Essential Mediator in CD8Infection and immunity · 2019
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 2 countries.

Jie YangThe Roslin Institute, Royal (Dick) School of Veterinary Studies, University of Edinburgh, Edinburgh, EH8 9YL, UK.
Christina VrettouThe Roslin Institute, Royal (Dick) School of Veterinary Studies, University of Edinburgh, Edinburgh, EH8 9YL, UK.
Tim ConnelleyThe Roslin Institute, Royal (Dick) School of Veterinary Studies, University of Edinburgh, Edinburgh, EH8 9YL, UK.
W Ivan MorrisonThe Roslin Institute, Royal (Dick) School of Veterinary Studies, University of Edinburgh, Edinburgh, EH8 9YL, UK. Ivan.morrison@roslin.ed.ac.uk.
Roslin Institute · GBUniversity of Edinburgh · GB

Funding

Biotechnology and Biological Sciences Research Council BB/H009515/1Biotechnology and Biological Sciences Research Council BB/J004227/1Biotechnology and Biological Sciences Research Council BBS/E/D/05201234
6 · The paper itself

Abstract

Granzymes are a family of serine proteases found in the lytic granules of cytotoxic T lymphocytes and natural killer (NK) cells, which are involved in killing of susceptible target cells. Most information on granzymes and their enzymatic specificities derive from studies in humans and mice. Although granzymes shared by both species show a high level of conservation, the complement of granzyme genes differs between the species. The aim of this study was to identify granzyme genes expressed in cattle, determine their genomic locations and analyse their sequences to predict likely functional specificities. Orthologues of the five granzyme genes found in humans (A, B, H, K and M) were identified, as well a novel gene designated granzyme O, most closely related to granzyme A. An orthologue of granzyme O was found in pigs and a non-function version was detected in the human genome. Use of specific PCRs demonstrated that all of these genes, including granzyme O, are expressed in activated subsets of bovine lymphocytes, with particularly high levels in CD8 T cells. Consistent with findings in humans and mice, the granzyme-encoding genes were located on three distinct genomic loci, which correspond to different proteolytic enzymatic activities, namely trypsin-like, chymotrypsin-like and metase-like. Analysis of amino acid sequences indicated that the granzyme proteins have broadly similar enzymatic specificities to their human and murine counterparts but indicated that granzyme B has a different secondary specificity. These findings provide the basis for further work to examine their role in the cytotoxic activity of bovine CD8 T cells.

Indexed as

PhylogenyAnimalsCattleChromosome MappingGranzymesLymphocyte ActivationLymphocytesMolecular Sequence AnnotationPerforinReproducibility of ResultsReverse Transcriptase Polymerase Chain ReactionTrypsinGranzymesPerforinTrypsinCattleEnzymatic specificityGenome lociGranzymeLymphocyte subsets

Identifiers

PMID29947943
PMCPMC6096847
OpenAlexW2806951722

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.