Evidence map›Paper›PMID 38762620›Full record

ArticleArchives of microbiology2024

Exploring the evolutionary and pathogenic role of Acinetobacter baumannii biofilm-associated protein (Bap) through in silico structural modeling.

Kirti Upmanyu, Rakesh Kumar, Qazi Mohd Rizwanul Haque, Ruchi Singh

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Article in Archives of microbiology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

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3 · Its place in the literature

Who cites it

3 citing papers in PubMed.

  1. Synergistic Inhibition ofMicroorganisms · 2026
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4 · The record

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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

4 authors.

Kirti UpmanyuICMR-National Institute of Pathology, Safdarjung Hospital Campus, New Delhi, 110029, India.
Rakesh KumarICMR-National Institute of Pathology, Safdarjung Hospital Campus, New Delhi, 110029, India.
Qazi Mohd Rizwanul HaqueDepartment of Biosciences, Jamia Millia Islamia, New Delhi, India.
Ruchi SinghICMR-National Institute of Pathology, Safdarjung Hospital Campus, New Delhi, 110029, India. ruchisp@gmail.com.ORCID http://orcid.org/0000-0001-8094-4703

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Acinetobacter species encode for extracellularly secreted Biofilm-associated protein (Bap), a multi-domain protein with variable molecular weights reaching several hundred kilodaltons. Bap is crucial for the development of multi-dimensional structures of mature biofilms. In our investigation, we analyzed 7338 sequences of A. baumannii from the NCBI database and found that Bap or Bap-like protein (BLP) was present in 6422 (87.52%) isolates. Further classification revealed that 12.12% carried Type-1 Bap, 68.44% had Type-2, 6.91% had Type-3, 0.05% had Type-6 or SDF-Type, and 12.51% lacked Bap or BLP. The majority of isolates with Type-1, Type-2, and Type-3 Bap belonged to ST1, ST2, and ST25, respectively. Phylogenetic analysis suggested that Type-1 Bap is the most ancient, while Type-3 and SDF-Type have evolved recently. Studying the interaction of predicted Bap structures with human CEACAM-1 and PIgR showed that Bap with its BIg13 and BIg6 domains interact with the N-terminal domain of CEACAM-1, involving Arg

Indexed as

Acinetobacter baumanniiBacterial ProteinsBiofilmsPhylogenyAcinetobacter InfectionsComputer SimulationEvolution, MolecularHumansModels, MolecularBacterial ProteinsA. BaumanniiBiofilmBiofilm associated protein (Bap)CEACAM-1Host pathogen interactionPathogenesisPIgRVirulence

Identifiers

PMID38762620

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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.