Evidence map›Paper›PMID 41303692›Full record

ArticleInternational journal of molecular sciences2025

Modeling Human Protein Physical Interactions Involved in HIV Attachment In Silico.

Vladimir S Davydenko, Alexander N Shchemelev, Yulia V Ostankova, Ekaterina V Anufrieva, Areg A Totolian

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

5 authors.

Vladimir S DavydenkoSaint Petersburg Pasteur Institute, 197101 St. Petersburg, Russia.ORCID 0000-0003-0078-9681
Alexander N ShchemelevSaint Petersburg Pasteur Institute, 197101 St. Petersburg, Russia.ORCID 0000-0002-3139-3674
Yulia V OstankovaSaint Petersburg Pasteur Institute, 197101 St. Petersburg, Russia.ORCID 0000-0003-2270-8897
Ekaterina V AnufrievaSaint Petersburg Pasteur Institute, 197101 St. Petersburg, Russia.ORCID 0009-0002-1882-529X
Areg A TotolianSaint Petersburg Pasteur Institute, 197101 St. Petersburg, Russia.ORCID 0000-0003-4571-8799

Funding

Russian Science Foundation 24-25-00479
6 · The paper itself

Abstract

The human immunodeficiency virus (HIV) remains a major global health challenge. A promising therapeutic strategy involves identifying human proteins capable of physically blocking viral entry by interacting with key components of the HIV attachment system. To address this challenge systematically, we developed a computational pipeline for prioritizing protein-protein interaction and applied it to identify host proteins interacting with the viral glycoprotein gp120 and cellular receptors (CD4, CCR5, CXCR4, CCR2). Our approach combined large-scale interaction modeling using AlphaFold 3 with a comprehensive comparative analysis framework. We screened a panel of 55 candidate human proteins selected through integrated bioinformatics analysis. The pipeline incorporated model confidence assessment, quantitative contact analysis, and normalization against reference interactions to generate a robust ranking of candidates. Key findings reveal several important patterns. Chemokine CCL27 uniquely demonstrated high binding potential to both CCR5 co-receptor and viral gp120, suggesting its potential for dual-blockade capability. Analysis of natural ligand interactions with chemokine receptors showed marked disparity: CC-chemokine family members exhibited significantly greater binding capacity for CCR5 and CCR2 receptors compared to CXC-family ligand interactions with CXCR4. This binding imbalance may potentially drive selective viral pressure and influence tropism evolution during disease progression. We also identified potential interactions between HIV entry components and neuropeptides including PNOC and NPY, as well as various membrane receptors beyond classical coreceptors. Furthermore, cluster analysis revealed clear separation between receptor-type and ligand-type interactors, supporting the biological plausibility of our predictions. While acknowledging limitations related to model refinement, this study provides a systematically ranked set of candidate targets for HIV therapeutic development. Beyond identifying specific HIV interaction candidates, this study establishes a generalizable computational pipeline for the prioritization of protein-protein interaction in pathogen-host systems, effectively bridging large-scale modeling.

Indexed as

HIV-1HIV Envelope Protein gp120HIV InfectionsVirus AttachmentComputational BiologyComputer SimulationHumansProtein BindingReceptors, CCR5Receptors, CXCR4Virus InternalizationHIV Envelope Protein gp120Receptors, CCR5Receptors, CXCR4AlphaFoldcandidate genesCCR2CCR5CD4ChimeraXcomputer modelingCXCR4human immunodeficiency virusin silicoprotein-protein interactionsvirus–host interaction

Identifiers

PMID41303692
PMCPMC12652853

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LicenceCC BY
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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.