Evidence map›Paper›PMID 37097521›Full record

ArticleMolecular biotechnology2024

Characterization of a Molecularly Engineered Banlec-Type Lectin (rBTL).

Laura Junqueira de Camargo, Mara Andrade Colares Maia, Rafael Dos Santos Woloski, Caroline Rizzi, Gustavo Marçal Schmidt Garcia Moreira, Claus Tröger Pich, Luciano da Silva Pinto

Abstract read
PubMed Publisher
In one paragraph

Article in Molecular biotechnology, 2024. 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
0.3field-weighted citation impact, top 37% 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

7 authors at 4 institutions in 2 countries.

Laura Junqueira de CamargoLaboratório de Bioinformática E Proteômica, Programa de Pós-Graduação Em Biotecnologia, Centro de Desenvolvimento Tecnológico, Universidade Federal de Pelotas, Pelotas, RS, Brazil. laurajcamargo@gmail.com.ORCID http://orcid.org/0000-0003-1120-2882
Mara Andrade Colares MaiaLaboratório de Vacinologia - Centro de Desenvolvimento Tecnológico, Universidade Federal de Pelotas, Pelotas, RS, Brazil.
Rafael Dos Santos WoloskiLaboratório de Bioinformática E Proteômica, Programa de Pós-Graduação Em Biotecnologia, Centro de Desenvolvimento Tecnológico, Universidade Federal de Pelotas, Pelotas, RS, Brazil.
Caroline RizziLaboratório de Vacinologia - Centro de Desenvolvimento Tecnológico, Universidade Federal de Pelotas, Pelotas, RS, Brazil.
Gustavo Marçal Schmidt Garcia MoreiraInstituto Für Biochemie, Biotechnologie Und Bioinformatik, Technische Universität Braunschweig, Brunswick, Germany.
Claus Tröger PichUniversidade Federal de Santa Catarina - UFSC, Campus Araranguá, Rua Pedro João Pereira, 150. Bairro Mato Alto, CEP 88905120, Araranguá, SC, Brazil.
Luciano da Silva PintoLaboratório de Bioinformática E Proteômica, Programa de Pós-Graduação Em Biotecnologia, Centro de Desenvolvimento Tecnológico, Universidade Federal de Pelotas, Pelotas, RS, Brazil. dmpluc@gmail.com.
Universidade Federal de Pelotas · BRTechnische Universität Braunschweig · DEUniversidade Federal de Santa Catarina · BRUniversidade Federal do Rio Grande do Sul · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lectins are proteins that reversibly bind to carbohydrates and are commonly found across many species. The Banana Lectin (BanLec) is a member of the Jacalin-related Lectins, heavily studied for its immunomodulatory, antiproliferative, and antiviral activity. In this study, a novel sequence was generated in silico considering the native BanLec amino acid sequence and 9 other lectins belonging to JRL. Based on multiple alignment of these proteins, 11 amino acids of the BanLec sequence were modified because of their potential for interference in active binding site properties resulting in a new lectin named recombinant BanLec-type Lectin (rBTL). rBTL was expressed in E. coli and was able to keep biological activity in hemagglutination assay (rat erythrocytes), maintaining similar structure with the native lectin. Antiproliferative activity was demonstrated on human melanoma lineage (A375), evaluated by 3-(4,5-Dimethylthiazol-2-yl)-2,5-Diphenyltetrazolium Bromide (MTT). rBTL was able to inhibit cellular growth in a concentration-dependent manner, in an 8-h incubation, 12 µg/mL of rBTL led to a 28.94% of cell survival compared to cell control with 100%. Through a nonlinear fit out log-concentration versus biological response, an IC50% of 3.649 µg/mL of rBTL was determined. In conclusion, it is possible to state that the changes made to the rBTL sequence maintained the structure of the carbohydrate-binding site without changing specificity. The new lectin is biologically active, with an improved carbohydrate recognition spectrum compared to nBanLec, and can also be considered cytotoxic for A375 cells.

Indexed as

Escherichia coliLectinsAmino Acid SequenceAnimalsCarbohydratesHumansPlant LectinsRatsCarbohydratesLectinsPlant LectinsBanlecJacalin-related lectinsMelanomaRecombinant lectinStructure prediction

Identifiers

PMID37097521
OpenAlexW4366992518

What OpenQuestion holds

Textmetadata
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.