{
  "abstract": "Helicobacter pylori remains a major cause of gastric diseases, while increasing antimicrobial resistance highlights the need for novel therapeutic targets. Here, we developed a comprehensive computational target-prioritization framework integrating Rosetta Stone domain-fusion analysis, subtractive genomics, metabolic pathway mapping, structural modeling, and molecular dynamics simulations to identify pathogen-specific drug targets in H. pylori J99. Twelve conserved domain families comprising 746 proteins were identified, and domain abundance showed a weak negative correlation with versatility (r = −0.327), suggesting functional specialization through domain expansion. Sequential filtering based on essentiality, nonhomology to the human proteome and gut microbiota, subcellular localization, and druggability prioritized five candidate proteins, with the ATP-binding protein AAD06727.1 emerging as the most promising target. AlphaFold2 modeling produced a high-confidence structure containing a conserved nucleotide-binding pocket. Molecular docking identified 5′-fluorosulfonylbenzoyl-5′-adenosine (FSBA) as the highest-affinity ligand (−7.3 kcal mol–1), outperforming ATP and verapamil. Triplicate 1 μs molecular dynamics simulations of apo and halo AAD06727.1 demonstrated stable rmsd, RMSF, radius of gyration, solvent-accessible surface area, hydrogen-bond occupancy, and principal component profiles, indicating preservation of structural integrity following ATP binding. Comparative simulations with the human ABCA12 nucleotide-binding domain showed conserved global architecture while revealing distinct ligand-recognition characteristics. Together, these findings identify AAD06727.1 as a structurally stable, pathogen-specific ATP-binding protein that represents a promising candidate for future structure-guided anti-H. pylori drug development.",
  "abstract_shown": true,
  "affiliations": [
    "Nitte (Deemed to be University) , , Deralakatte , , ,",
    "Kuvempu University , , Shankaraghatta , , ,",
    "Nitte (Deemed to be University) , , Deralakatte , ,"
  ],
  "article_type": "research article",
  "arxiv": null,
  "author_total": 5,
  "authors": [
    {
      "affs": [
        0
      ],
      "name": "Manish Kumar",
      "orcid": "0009-0006-6546-8888"
    },
    {
      "affs": [
        1
      ],
      "name": "H. S. Santosh Kumar"
    },
    {
      "affs": [
        0
      ],
      "name": "Ballamoole Krishna Kumar",
      "orcid": "0000-0001-7821-7419"
    },
    {
      "affs": [
        2
      ],
      "name": "Veena A. Shetty"
    },
    {
      "affs": [
        0
      ],
      "name": "Pavan Gollapalli"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/2f873kh14bqy4.bib",
  "cited_by": 0,
  "doi": "10.1021/acsomega.6c05087",
  "fulltext_url": "https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13670296/?tool=EBI",
  "id": "2f873kh14bqy4",
  "issns": [
    "2470-1343"
  ],
  "landing_url": "https://europepmc.org/article/PMC/PMC13670296",
  "language": "eng",
  "licence": "CC-BY-NC-ND",
  "licence_label": "CC BY-NC-ND",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by-nc-nd/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "openalex",
      "1703|Computational Drug Discovery Methods"
    ]
  ],
  "openalex": "W7214712779",
  "pdf_url": "https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13670296/pdf/?tool=EBI",
  "pmcid": "PMC13670296",
  "pmid": null,
  "published": "2026-09-29",
  "publisher": "American Chemical Society (ACS)",
  "ris": "https://research.draconitic.com/paper/2f873kh14bqy4.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:18:18Z",
      "native_id": "PMC:PMC13670296",
      "source": "europepmc",
      "url": "https://europepmc.org/article/PMC/PMC13670296"
    },
    {
      "first_seen": "2026-10-30T12:18:39Z",
      "native_id": "10.1021/acsomega.6c05087",
      "source": "crossref",
      "url": "https://pubs.acs.org/acsodf/article/11/40/61003/5442047/Integrated-In-Silico-Analysis-Reveals-ABC"
    }
  ],
  "subjects": [
    {
      "field": "chemistry",
      "origin": "issn:2470-1343",
      "subfield": "general"
    }
  ],
  "title": "Integrated In Silico Analysis Reveals ABC Transporter ATP-Binding Protein as a Therapeutic Target in Helicobacter pylori",
  "title_text": "Integrated In Silico Analysis Reveals ABC Transporter ATP-Binding Protein as a Therapeutic Target in Helicobacter pylori",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:18:39Z",
  "url": "https://research.draconitic.com/paper/2f873kh14bqy4",
  "venue": "ACS omega",
  "versions": []
}