Evidence map›Paper›PMID 41614910›Full record

ArticleCurrent issues in molecular biology2026

SARS-CoV-2 Helicase (NSP13) Interacts with Mammalian Polyamine and HSP Partners in Promoting Viral Replication.

Zingisa Sitobo, Liberty T Navhaya, Ntombekhaya Nqumla, Madipoane Masenya, Matsheliso Molapo, Yamkela Mthembu, Sesethu Godlo, Xolani H Makhoba

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Article in Current issues in molecular biology, 2026. 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
–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

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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.

  1. Review
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

8 authors.

Zingisa SitoboDepartment of Biochemistry and Microbiology, University of Fort Hare, Alice Campus, Alice 5700, South Africa.
Liberty T NavhayaDepartment of Biochemistry, Microbiology and Biotechnology, University of Limpopo, Turfloop Campus, Sovenga 0727, South Africa.ORCID 0000-0003-1815-1272
Ntombekhaya NqumlaDepartment of Biochemistry and Microbiology, University of Fort Hare, Alice Campus, Alice 5700, South Africa.
Madipoane MasenyaDepartment of Life and Consumer Sciences, College of Agriculture and Environmental Sciences, University of South Africa (UNISA), Florida Campus, Roodepoort 1709, South Africa.
Matsheliso MolapoDepartment of Life and Consumer Sciences, College of Agriculture and Environmental Sciences, University of South Africa (UNISA), Florida Campus, Roodepoort 1709, South Africa.
Yamkela MthembuHuman Genetics Department, Computational Biology Division, Faculty of Health Sciences, University of Cape Town, Barnard Fuller Building, Anzio Rd, Observatory, Cape Town 7935, South Africa.ORCID 0000-0002-6939-1199
Sesethu GodloDepartment of Life and Consumer Sciences, College of Agriculture and Environmental Sciences, University of South Africa (UNISA), Florida Campus, Roodepoort 1709, South Africa.ORCID 0000-0002-8076-3096
Xolani H MakhobaDepartment of Life and Consumer Sciences, College of Agriculture and Environmental Sciences, University of South Africa (UNISA), Florida Campus, Roodepoort 1709, South Africa.ORCID 0000-0002-7238-4619

Funding

National Research Foundation RA22102665148
6 · The paper itself

Abstract

We present a computational study that precedes the potential interactions between SARS-CoV-2 helicase (NSP13) and selected host proteins implicated in chaperone-assisted folding and polyamine metabolism. Using structure-based modelling and protein-protein docking (BioLuminate v4.6), followed by all-atom molecular dynamics (MD) simulations (GROMACS v2018.6), and comparative MM-GBSA scoring (HawkDock v2), we evaluated the stability and interface properties of NSP13 complexes with cytosolic heat shock proteins; heat shock protein 40 (HSP40), heat shock protein 70 (HSP70), heat shock protein 90 (HSP90) and the polyamine biosynthesis enzyme ornithine decarboxylase (ODC). Docking, MD, and interface analyses indicate distinct complex behaviours: HSP70-NSP13 complexes sampled compact conformations, HSP90-NSP13 ensembles displayed greater conformational heterogeneity but more favourable comparative MM-GBSA estimates, and ODC-NSP13 interfaces were comparatively well packed. Per-residue contact mapping identified a small set of recurrent NSP13 residues, Lys22 and Asn51, as putative interaction hotspots. The reported findings herein generate testable hypotheses about NSP13 recruitment of host chaperones and modulation of polyamine metabolism that may inform downstream experimental studies.

Indexed as

COVID-19heat shock proteinsMD stimulationsNSP13ODCpolyaminesSARS-CoV-2

Identifiers

PMID41614910
PMCPMC12840268

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