Evidence map›Paper›PMID 35761501›Full record

ArticleCurrent neuropharmacology2023

Analysis of Interaction Between Odorant Receptors and Flexible Spike of SARS CoV-2- Key to Loss of Smell.

Firoz Anwar, Hisham Altayeb, Sultan Alhayyani, Vikas Kumar, Fahad A Al-Abbasi, Ghulam Md Ashraf

Open access · greenAbstract read
In one paragraph

Article in Current neuropharmacology, 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
0.3field-weighted citation impact, top 44% 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, 3 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

6 authors at 1 institution in 1 country.

Firoz AnwarDepartment of Biochemistry, Faculty of Sciences, King Abdulaziz University, Jeddah, Kingdom of Saudi Arabia.
Hisham AltayebDepartment of Biochemistry, Faculty of Sciences, King Abdulaziz University, Jeddah, Kingdom of Saudi Arabia.
Sultan AlhayyaniDepartment of Chemistry, College of Sciences & Arts, King Abdulaziz University, Rabigh King Abdulaziz University, Jeddah, Kingdom of Saudi Arabia.
Vikas KumarDepartment of Pharmaceutical Sciences, Natural Product Discovery Laboratory, Shalom Institute of Health and Allied Sciences. SHUATS, Naini, Prayagraj, India.
Fahad A Al-AbbasiDepartment of Biochemistry, Faculty of Sciences, King Abdulaziz University, Jeddah, Kingdom of Saudi Arabia.
Ghulam Md AshrafKing Fahd Medical Research Center, King Abdulaziz University, Jeddah, Kingdom of Saudi Arabia.
King Abdulaziz University · SA

Funding

Deanship of Scientific Research (DSR) at King Abdulaziz University, Jeddah IFPHI-285-130-2020
6 · The paper itself

Abstract

backgroundThe development of a vaccine for SARS-CoV-2 is primarily focused on the structure of the spike (S) protein. The heavy glycosylation of S with flexible hinges at the stalk shields from antibody attachment.

objectiveThis study deciphers the flexible nature of hinges responsible for binding the odorant receptor on neurons responsible for the loss of smell in COVID-19 patients.

methodsThe 3D structure via EPIK in Maestro, protein docking with ligands via Maestro protein analysis tool, and molecular dynamic simulation at 30 ns run using DESMOND was prepared.

resultsThe data of the study strongly suggest that strong and stable bond formation results from the reaction between R:14: Trp and Phe at the residue, targeting the flexible hinges of SARS-CoV-2. The difference in the conformational structure of the S protein and its binding with the odorant receptor in COVID-19 is the prime factor for the loss of smell and taste in patients, as supported by the concept of Antigen (epitope) Antibody interaction by the stable formation of a hydrogen bond among odorant receptor and the S protein. The flexibility of structural proteins determines the binding potential of antibodies or other defense proteins produced to participate in the antigen-antibody reaction.

conclusionMolecular and atomic details potentiate the design and screening of small molecules that can inhibit the fusion at entry level or odorant receptors and potentially be used in the prevention and treatment of infection, particularly when formulated as nasal drops, paving a new approach for pharmacologists in the treatment of COVID-19 infection.

Indexed as

AnosmiaCOVID-19Receptors, OdorantHumansProtein BindingSARS-CoV-2Spike Glycoprotein, CoronavirusReceptors, OdorantSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2COVID-19flexibleodorant receptorSARS-CoV-2spike protein

Identifiers

PMID35761501
PMCPMC10193757
OpenAlexW4283655400

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.