Evidence map›Paper›PMID 38016962›Full record

ArticleNature communications2023

Ongoing shuffling of protein fragments diversifies core viral functions linked to interactions with bacterial hosts.

Bogna J Smug, Krzysztof Szczepaniak, Eduardo P C Rocha, Stanislaw Dunin-Horkawicz, Rafał J Mostowy

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
9.7field-weighted citation impact, top 1% 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

23 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
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  14. Gene co-occurrence and its association with phage infectivity in bacterial pangenomes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Article
  15. Evolutionarily conserved grammar rules viral factories of amoeba-infecting members of the hyperdiverseProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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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 at 3 institutions in 3 countries.

Bogna J SmugMalopolska Centre of Biotechnology, Jagiellonian University, Krakow, Poland.ORCID 0000-0001-9364-163X
Krzysztof SzczepaniakMalopolska Centre of Biotechnology, Jagiellonian University, Krakow, Poland.
Eduardo P C RochaInstitut Pasteur, Université Paris Cité, CNRS UMR3525, Microbial Evolutionary Genomics, Paris, France.
Stanislaw Dunin-HorkawiczInstitute of Evolutionary Biology, Faculty of Biology & Biological and Chemical Research Centre, University of Warsaw, Żwirki i Wigury 101, 02-089, Warsaw, Poland.
Rafał J MostowyMalopolska Centre of Biotechnology, Jagiellonian University, Krakow, Poland. rafal.mostowy@uj.edu.pl.ORCID 0000-0002-4557-3748
Jagiellonian University · PLCentre National de la Recherche Scientifique · FRMax Planck Institute for Developmental Biology · DE

Funding

Fundacja na rzecz Nauki Polskiej (Foundation for Polish Science) POIR.04.04.00-00-5CF1/18-00Narodowe Centrum Nauki (National Science Centre) 2020/37/B/NZ8/03492
6 · The paper itself

Abstract

Biological modularity enhances evolutionary adaptability. This principle is vividly exemplified by bacterial viruses (phages), which display extensive genomic modularity. Phage genomes are composed of independent functional modules that evolve separately and recombine in various configurations. While genomic modularity in phages has been extensively studied, less attention has been paid to protein modularity-proteins consisting of distinct building blocks that can evolve and recombine, enhancing functional and genetic diversity. Here, we use a set of 133,574 representative phage proteins and highly sensitive homology detection to capture instances of domain mosaicism, defined as fragment sharing between two otherwise unrelated proteins, and to understand its relationship with functional diversity in phage genomes. We discover that unrelated proteins from diverse functional classes frequently share homologous domains. This phenomenon is particularly pronounced within receptor-binding proteins, endolysins, and DNA polymerases. We also identify multiple instances of recent diversification via domain shuffling in receptor-binding proteins, neck passage structures, endolysins and some members of the core replication machinery, often transcending distant taxonomic and ecological boundaries. Our findings suggest that ongoing diversification via domain shuffling is reflective of a co-evolutionary arms race, driven by the need to overcome various bacterial resistance mechanisms against phages.

Indexed as

BacteriophagesEvolution, MolecularBacteriaBiological EvolutionGenome, ViralGenomicsPhylogeny

Identifiers

PMID38016962
PMCPMC10684548
OpenAlexW4389088427

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.