Evidence map›Paper›PMID 26572057›Full record

ArticleBMC genomics2015

Biofilm-associated proteins: news from Acinetobacter.

Eliana De Gregorio, Mariateresa Del Franco, Marianna Martinucci, Emanuela Roscetto, Raffaele Zarrilli, Pier Paolo Di Nocera

Open access · goldAbstract read
In one paragraph

Article in BMC genomics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

73 citing papers in PubMed, 104 citations in OpenAlex.

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  20. The intricacies ofFrontiers in microbiology · 2025
    Review

13 more citing papers are in PubMed but not listed here.

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

6 authors at 1 institution in 1 country.

Eliana De GregorioDipartimento di Medicina Molecolare e Biotecnologie Mediche, Università Federico II, Via Sergio Pansini 5, Naples, 80131, Italy. edegrego@unina.it.
Mariateresa Del FrancoDipartimento di Sanità Pubblica, Università Federico II, Via Sergio Pansini 5, 80131, Naples, Italy. mariateresa.88@libero.it.
Marianna MartinucciDipartimento di Medicina Molecolare e Biotecnologie Mediche, Università Federico II, Via Sergio Pansini 5, Naples, 80131, Italy. mariannamartinucci@libero.it.
Emanuela RoscettoDipartimento di Medicina Molecolare e Biotecnologie Mediche, Università Federico II, Via Sergio Pansini 5, Naples, 80131, Italy. emanuelaroscetto@gmail.com.
Raffaele ZarrilliDipartimento di Sanità Pubblica, Università Federico II, Via Sergio Pansini 5, 80131, Naples, Italy. rafzarri@unina.it.
Pier Paolo Di NoceraDipartimento di Medicina Molecolare e Biotecnologie Mediche, Università Federico II, Via Sergio Pansini 5, Naples, 80131, Italy. dinocera@unina.it.
University of Naples Federico II · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundA giant protein called BAP (biofilm-associated protein) plays a role in biofilm formation and adhesion to host cells in A. baumannii. Most of the protein is made by arrays of 80-110 aa modules featuring immunoglobulin-like (Ig-like) motifs.

resultsThe survey of 541 A. baumannii sequenced strains belonging to 108 STs (sequence types) revealed that BAP is highly polymorphic, distinguishable in three main types for changes both in the repetitive and the COOH region. Analyzing the different STs, we found that 29 % feature type-1, 40 % type-2 BAP, 11 % type-3 BAP, 20 % lack BAP. The type-3 variant is restricted to A. baumannii, type-1 and type-2 BAP have been identified also in other species of the Acinetobacter calcoaceticus-baumannii (ACB) complex. A. calcoaceticus and A. pittii also encode BAP-like proteins in which Ig-like repeats are replaced by long tracts of alternating serine and aspartic acid residues. We have identified in species of the ACB complex two additional proteins, BLP1 and BLP2 (BAP-like proteins 1 and 2) which feature Ig-like repeats, share with BAP a sequence motif at the NH2 terminus, and are similarly expressed in stationary growth phase. The knock-out of either BLP1 or BLP2 genes of the A. baumannii ST1 AYE strain severely affected biofilm formation, as measured by comparing biofilm biomass and thickness, and adherence to epithelial cells. BLP1 is missing in the majority of type-3 BAP strains. BLP2 is largely conserved, but is frequently missing in BAP-negative cells.

conclusionsMultiple proteins sharing Ig-like repeats seem to be involved in biofilm formation. The uneven distribution of the different BAP types, BLP1, and BLP2 is highly indicative that alternative protein complexes involved in biofilm formation are assembled in different A. baumannii strains.

Indexed as

Acinetobacter baumanniiAmino Acid SequenceBacterial AdhesionBacterial ProteinsBronchiCell LineGenetic HeterogeneityGenome, BacterialHumansMolecular Sequence DataProtein Structure, TertiarySpecies SpecificityBacterial Proteins

Identifiers

PMID26572057
PMCPMC4647330
OpenAlexW2176048240

What OpenQuestion holds

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LicenceCC BY
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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.