Evidence map›Paper›PMID 35562647›Full record

ReviewCellular & molecular biology letters2022

Lectins and lectibodies: potential promising antiviral agents.

Mohsen Nabi-Afjadi, Morteza Heydari, Hamidreza Zalpoor, Ibrahim Arman, Arezoo Sadoughi, Parisa Sahami, Safiyeh Aghazadeh

Open access · goldAbstract readLetterReview
In one paragraph

Review in Cellular & molecular biology letters, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
7.8field-weighted citation impact, top 2% 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

29 citing papers in PubMed, 57 citations in OpenAlex.

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  18. A Complex-TypeInternational journal of molecular sciences · 2024
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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 7 institutions in 3 countries.

Mohsen Nabi-Afjadi *Department of Biochemistry, Faculty of Biological Science, Tarbiat Modares University, Tehran, Iran.
Morteza Heydari *Institute of Biochemistry and Biophysics, University of Tehran, Tehran, 13145-1384, Iran.
Hamidreza ZalpoorShiraz Neuroscience Research Center, Shiraz University of Medical Sciences, Shiraz, Iran.
Ibrahim ArmanDepartment of Molecular Biology and Genetics, Faculty of Sciences and Arts, Zonguldak Bulent Ecevit University, Zonguldak, Turkey.
Arezoo SadoughiDepartment of Immunology, International Campus, Shahid Sadoughi University of Medical Sciences, Yazd, Iran.
Parisa SahamiMedical Biology Research Center, Health Technologies Institute, Kermanshah University of Medical Sciences (KUMS), Kermanshah, Iran.
Safiyeh AghazadehDivision of Biochemistry, Department of Basic Sciences, Faculty of Veterinary Medicine, Urmia University, Urmia, 5756151818, Iran. s.aghazadeh@urmia.ac.ir.
American Association of Kidney Patients · USBülent Ecevit University · TRKermanshah University of Medical Sciences · IRShahid Sadoughi University of Medical Sciences and Health Services · IRTarbiat Modares University · IRUniversity of Tehran · IRUrmia University · IR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In nature, lectins are widely dispersed proteins that selectively recognize and bind to carbohydrates and glycoconjugates via reversible bonds at specific binding sites. Many viral diseases have been treated with lectins due to their wide range of structures, specificity for carbohydrates, and ability to bind carbohydrates. Through hemagglutination assays, these proteins can be detected interacting with various carbohydrates on the surface of cells and viral envelopes. This review discusses the most robust lectins and their rationally engineered versions, such as lectibodies, as antiviral proteins. Fusion of lectin and antibody's crystallizable fragment (Fc) of immunoglobulin G (IgG) produces a molecule called a "lectibody" that can act as a carbohydrate-targeting antibody. Lectibodies can not only bind to the surface glycoproteins via their lectins and neutralize and clear viruses or infected cells by viruses but also perform Fc-mediated antibody effector functions. These functions include complement-dependent cytotoxicity (CDC), antibody-dependent cell-mediated cytotoxicity (ADCC), and antibody-dependent cell-mediated phagocytosis (ADCP). In addition to entering host cells, the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein S1 binds to angiotensin-converting enzyme 2 (ACE2) and downregulates it and type I interferons in a way that may lead to lung disease. The SARS-CoV-2 spike protein S1 and human immunodeficiency virus (HIV) envelope are heavily glycosylated, which could make them a major target for developing vaccines, diagnostic tests, and therapeutic drugs. Lectibodies can lead to neutralization and clearance of viruses and cells infected by viruses by binding to glycans located on the envelope surface (e.g., the heavily glycosylated SARS-CoV-2 spike protein).

Indexed as

SARS-CoV-2Antiviral AgentsCarbohydratesLectinsSpike Glycoprotein, CoronavirusAntiviral AgentsCarbohydratesLectinsSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2CarbohydratesEBVHCVHIVLectibodyLectinsSARS-CoV-2Virus envelope

Identifiers

PMID35562647
PMCPMC9100318
OpenAlexW4280612035

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.