Evidence map›Paper›PMID 38132935›Full record

ReviewMarine drugs2023

Taxonomic Distribution and Molecular Evolution of Mytilectins.

Marco Gerdol, Daniela Eugenia Nerelli, Nicola Martelossi, Yukiko Ogawa, Yuki Fujii, Alberto Pallavicini, Yasuhiro Ozeki

Abstract readReview
In one paragraph

Review in Marine drugs, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. 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

7 authors.

Marco GerdolDepartment of Life Sciences, University of Trieste, Via Licio Giorgieri 5, 34127 Trieste, Italy.ORCID 0000-0001-6411-0813
Daniela Eugenia NerelliDepartment of Life Sciences, University of Trieste, Via Licio Giorgieri 5, 34127 Trieste, Italy.ORCID 0009-0008-1065-0927
Nicola MartelossiDepartment of Life Sciences, University of Trieste, Via Licio Giorgieri 5, 34127 Trieste, Italy.
Yukiko OgawaGraduate School of Pharmaceutical Sciences, Nagasaki International University, 2825-7 Huis Ten Bosch, Sasebo 859-3298, Japan.
Yuki FujiiGraduate School of Pharmaceutical Sciences, Nagasaki International University, 2825-7 Huis Ten Bosch, Sasebo 859-3298, Japan.ORCID 0000-0001-6408-9620
Alberto PallaviciniDepartment of Life Sciences, University of Trieste, Via Licio Giorgieri 5, 34127 Trieste, Italy.ORCID 0000-0001-7174-4603
Yasuhiro OzekiGraduate School of NanoBio Sciences, Yokohama City University, 22-2 Seto, Kanazawa-ku, Yokohama 236-0027, Japan.ORCID 0000-0002-2782-6158

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

R-type lectins are a widespread group of sugar-binding proteins found in nearly all domains of life, characterized by the presence of a carbohydrate-binding domain that adopts a β-trefoil fold. Mytilectins represent a recently described subgroup of β-trefoil lectins, which have been functionally characterized in a few mussel species (Mollusca, Bivalvia) and display attractive properties, which may fuel the development of artificial lectins with different biotechnological applications. The detection of different paralogous genes in mussels, together with the description of orthologous sequences in brachiopods, supports the formal description of mytilectins as a gene family. However, to date, an investigation of the taxonomic distribution of these lectins and their molecular diversification and evolution was still lacking. Here, we provide a comprehensive overview of the evolutionary history of mytilectins, revealing an ancient monophyletic evolutionary origin and a very broad but highly discontinuous taxonomic distribution, ranging from heteroscleromorphan sponges to ophiuroid and crinoid echinoderms. Moreover, the overwhelming majority of mytilectins display a chimera-like architecture, which combines the β-trefoil carbohydrate recognition domain with a C-terminal pore-forming domain, suggesting that the simpler structure of most functionally characterized mytilectins derives from a secondary domain loss.

Indexed as

BivalviaLectinsAnimalsCarbohydratesEvolution, MolecularCarbohydratesLectinsglycan-bindinginnate immunitylectinsmarine invertebratespore-formingβ-trefoil

Identifiers

PMID38132935
PMCPMC10744619

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Registered trials

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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.