Evidence map›Paper›PMID 37458864›Full record

ArticleCurrent microbiology2023

Purification and Characterization of the Lecithin-Dependent Thermolabile Hemolysin Vhe1 from the Vibrio sp. Strain MA3 Associated with Mass Mortality of Pearl Oyster (Pinctada fucata).

Akihiro Sakatoku, Kaito Hatano, Kosei Takada, Ryota Shimizu, Takaya Suzuki, Makoto Seki, Nobuo Suzuki, Daisuke Tanaka, Shogo Nakamura, Tadashi Isshiki

Abstract read
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In one paragraph

Article in Current microbiology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.6field-weighted citation impact, top 31% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. 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

10 authors at 3 institutions in 1 country.

Akihiro SakatokuSchool of Science, Academic Assembly, University of Toyama, Toyama, 930-8555, Japan. sakatoku@sci.u-toyama.ac.jp.ORCID http://orcid.org/0000-0001-8333-1531
Kaito HatanoNoto Marine Laboratory, Institute of Nature and Environmental Technology, Kanazawa University, Ogi, Noto‑cho, Ishikawa, 927‑0553, Japan.
Kosei TakadaSchool of Science, Academic Assembly, University of Toyama, Toyama, 930-8555, Japan.
Ryota ShimizuSchool of Science, Academic Assembly, University of Toyama, Toyama, 930-8555, Japan.
Takaya SuzukiSchool of Science, Academic Assembly, University of Toyama, Toyama, 930-8555, Japan.
Makoto SekiSchool of Science, Academic Assembly, University of Toyama, Toyama, 930-8555, Japan.
Nobuo SuzukiNoto Marine Laboratory, Institute of Nature and Environmental Technology, Kanazawa University, Ogi, Noto‑cho, Ishikawa, 927‑0553, Japan.
Daisuke TanakaSchool of Science, Academic Assembly, University of Toyama, Toyama, 930-8555, Japan.
Shogo NakamuraSchool of Science, Academic Assembly, University of Toyama, Toyama, 930-8555, Japan.
Tadashi IsshikiGraduate School of Bioresources, Mie University, 1577 Kurimamachiya, Tsu, Mie, 514-8507, Japan.
University of Toyama · JPKanazawa University · JPMie University · JP

Funding

Institute of Nature and Environmental Technology, Kanazawa University 22040Institute of Nature and Environmental Technology, Kanazawa University 23029Japan Society for the Promotion of Science 20K06203Japan Society for the Promotion of Science 23H02291Japan Society for the Promotion of Science 23KJ1031Kurita Water and Environment Foundation 20E003Kurita Water and Environment Foundation 21E018Kurita Water and Environment Foundation 22K008
6 · The paper itself

Abstract

In a previous study, we isolated a Vibrio sp. strain MA3 and its virulence factor, a hemolysin encoded by vhe1. This strain is associated with mass mortalities of the pearl oyster Pinctada fucata. In the present study, the vhe1 gene from strain MA3 was cloned and its encoded product was purified and characterized. Our results show that the vhe1 gene encodes a protein of 417 amino acids with an estimated molecular mass of 47.2 kDa and a pI of 5.14. The deduced protein, Vhe1, was found to contain the conserved amino acid sequence (GDSL motif) of the hydrolase/esterase superfamily and five conserved blocks characteristic of SGNH hydrolases. A BLAST homology search indicated that Vhe1 belongs the lecithin-dependent hemolysin/thermolabile hemolysin (LDH/TLH) family. In activity analyses, the optimal temperature for both the hemolytic and phospholipase activities of Vhe1 was 50 °C. Vhe1 hemolytic activity and phospholipase activity were highest at pH 8.5 and pH 8.0, respectively. However, both enzymatic activities sharply decreased at high temperature (> 50 °C) and pH < 7.0. Compared with previously reported hemolysins, Vhe1 appeared to be more thermal- and pH-labile. Both its hemolytic activity and phospholipase activity were significantly inhibited by CuCl

Indexed as

PinctadaVibrioAnimalsCloning, MolecularHemolysin ProteinsLecithinsPhospholipasesHemolysin ProteinsLecithinsPhospholipases

Identifiers

PMID37458864
OpenAlexW4384485958

What OpenQuestion holds

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Read underepoch 390

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.