Evidence map›Paper›PMID 23658744›Full record

ArticlePloS one2013

Tryptogalinin is a tick Kunitz serine protease inhibitor with a unique intrinsic disorder.

James J Valdés, Alexandra Schwarz, Israel Cabeza de Vaca, Eric Calvo, Joao H F Pedra, Victor Guallar, Michalis Kotsyfakis

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.5field-weighted citation impact, top 8% 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

21 citing papers in PubMed, 34 citations in OpenAlex.

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  13. Gene Duplication and Protein Evolution in Tick-Host Interactions.Frontiers in cellular and infection microbiology · 2017
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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

7 authors at 5 institutions in 3 countries.

James J ValdésInstitute of Parasitology, Biology Centre of the Academy of Sciences of the Czech Republic, České Budějovice, Czech Republic. valdjj@gmail.com
Alexandra Schwarz
Israel Cabeza de Vaca
Eric Calvo
Joao H F Pedra
Victor Guallar
Michalis Kotsyfakis
Institute for Research in Biomedicine · ESInstitute of Parasitology · CZCzech Academy of Sciences, Biology Centre · CZUniversity of California, Riverside · USVector (United States) · US

Funding

Rickettsial Immunity During Tick TransmissionR01AI093653 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI PEDRA, JOAO · 2011 to 2015
$1.8M
NIAID NIH HHS R01 AI093653
6 · The paper itself

Abstract

backgroundA salivary proteome-transcriptome project on the hard tick Ixodes scapularis revealed that Kunitz peptides are the most abundant salivary proteins. Ticks use Kunitz peptides (among other salivary proteins) to combat host defense mechanisms and to obtain a blood meal. Most of these Kunitz peptides, however, remain functionally uncharacterized, thus limiting our knowledge about their biochemical interactions.

resultsWe discovered an unusual cysteine motif in a Kunitz peptide. This peptide inhibits several serine proteases with high affinity and was named tryptogalinin due to its high affinity for β-tryptase. Compared with other functionally described peptides from the Acari subclass, we showed that tryptogalinin is phylogenetically related to a Kunitz peptide from Rhipicephalus appendiculatus, also reported to have a high affinity for β-tryptase. Using homology-based modeling (and other protein prediction programs) we were able to model and explain the multifaceted function of tryptogalinin. The N-terminus of the modeled tryptogalinin is detached from the rest of the peptide and exhibits intrinsic disorder allowing an increased flexibility for its high affinity with its inhibiting partners (i.e., serine proteases).

conclusionsBy incorporating experimental and computational methods our data not only describes the function of a Kunitz peptide from Ixodes scapularis, but also allows us to hypothesize about the molecular basis of this function at the atomic level.

Indexed as

Amino Acid MotifsAnimalsArthropod ProteinsCysteineHumansIxodesModels, MolecularMolecular Sequence DataPhylogenyProtein Structure, TertiaryRecombinant ProteinsRhipicephalusSalivary Proteins and PeptidesSequence Homology, Amino AcidSerine Proteinase InhibitorsTryptasesArthropod ProteinsCysteineRecombinant ProteinsSalivary Proteins and PeptidesSerine Proteinase InhibitorsTryptases

Identifiers

PMID23658744
PMCPMC3643938
OpenAlexW2006593248

What OpenQuestion holds

Textmetadata
LicenceCC0
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.