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ANISERP: a new serpin from the parasite Anisakis simplex

Overview of attention for article published in Parasites & Vectors, July 2015
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Title
ANISERP: a new serpin from the parasite Anisakis simplex
Published in
Parasites & Vectors, July 2015
DOI 10.1186/s13071-015-1006-z
Pubmed ID
Authors

Elizabeth Valdivieso, Maria J. Perteguer, Carolina Hurtado, Pamela Campioli, Esperanza Rodríguez, Ana Saborido, Victoria Martínez-Sernández, Paulino Gómez-Puertas, Florencio M. Ubeira, Teresa Gárate

Abstract

Serine proteinase inhibitors (serpins) finely regulate serine proteinase activity via a suicide substrate-like inhibitory mechanism. In parasitic nematodes, some serpins interact with host physiological processes; however, little is known about these essential molecules in Anisakis. This article reports the gene sequencing, cloning, expression and preliminary biochemical and bioinformatically-based structural characterization of a new Anisakis serpin (ANISERP). The full AniSerp gene was cloned by specific RACE-PCR after screening an Anisakis simplex (L3) cDNA library. For biochemical assays, the AniSerp gene was subcloned into both prokaryotic and eukaryotic vectors, and the recombinant proteins were purified. The inhibitory properties of the proteins were tested in classical biochemical assays using human serine peptidases and AMC substrates. Immunolocalization of ANISERP, theoretical structural analysis and bioinformatically-based structural modelling of the ANISERP protein were also conducted. The AniSerp gene was found to have 1194 nucleotides, coding for a protein of 397 amino acid residues plus a putative N-terminal signal peptide. It showed significant similarity to other nematode, arthropod and mammalian serpins. The recombinant ANISERP expressed in the prokaryotic and eukaryotic systems inhibited the human serine proteases thrombin, trypsin and cathepsin G in a concentration-dependent manner. No inhibitory activity against Factor Xa, Factor XIa, Factor XIIa, elastase, plasmin or chymotrypsin was observed. ANISERP also acted on the cysteine protease cathepsin L. ANISERP was mainly localized in the nematode pseudocoelomic fluid, somatic muscle cell bodies and intestinal cells. The findings of molecular dynamics studies suggest that ANISERP inhibits thrombin via a suicide substrate-like inhibitory mechanism, similar to the mechanism of action of mammalian coagulation inhibitors. In contrast to findings concerning human antithrombin III, heparin had no effect on ANISERP anticoagulant inhibitory activity. Our findings suggest that ANISERP is an internal Anisakis regulatory serpin and that the inhibitory activity against thrombin depends on a suicide substrate-like inhibitory mechanism, similar to that described for human antithrombin (AT)-III. The fact that heparin does not modulate the anticoagulant activity of ANISERP might be explained by the absence in the latter of five of the six positively charged residues usually seen at the AT-III-heparin binding site.

X Demographics

X Demographics

The data shown below were collected from the profiles of 3 X users who shared this research output. Click here to find out more about how the information was compiled.
Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 33 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Colombia 1 3%
Unknown 32 97%

Demographic breakdown

Readers by professional status Count As %
Researcher 7 21%
Student > Master 4 12%
Student > Bachelor 3 9%
Student > Ph. D. Student 3 9%
Lecturer 2 6%
Other 4 12%
Unknown 10 30%
Readers by discipline Count As %
Agricultural and Biological Sciences 8 24%
Medicine and Dentistry 4 12%
Immunology and Microbiology 4 12%
Veterinary Science and Veterinary Medicine 2 6%
Biochemistry, Genetics and Molecular Biology 2 6%
Other 2 6%
Unknown 11 33%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 2. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 03 August 2015.
All research outputs
#13,950,934
of 22,818,766 outputs
Outputs from Parasites & Vectors
#2,652
of 5,461 outputs
Outputs of similar age
#130,513
of 263,394 outputs
Outputs of similar age from Parasites & Vectors
#45
of 104 outputs
Altmetric has tracked 22,818,766 research outputs across all sources so far. This one is in the 37th percentile – i.e., 37% of other outputs scored the same or lower than it.
So far Altmetric has tracked 5,461 research outputs from this source. They typically receive a little more attention than average, with a mean Attention Score of 5.7. This one is in the 48th percentile – i.e., 48% of its peers scored the same or lower than it.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 263,394 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 48th percentile – i.e., 48% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 104 others from the same source and published within six weeks on either side of this one. This one has gotten more attention than average, scoring higher than 54% of its contemporaries.