Evidence map›Paper›PMID 31324000›Full record

ArticleViruses2019

Ubiquitous Carbohydrate Binding Modules Decorate 936 Lactococcal Siphophage Virions.

Stephen Hayes, Jennifer Mahony, Renaud Vincentelli, Laurie Ramond, Arjen Nauta, Douwe van Sinderen, Christian Cambillau

Abstract read
In one paragraph

Article in Viruses, 2019. 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
–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

23 citing papers in PubMed.

  1. Review
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  17. Review
  18. Genome Sequence and Characterization ofPHAGE (New Rochelle, N.Y.) · 2021
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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

7 authors.

Stephen HayesSchool of Microbiology, University College Cork, T12 YT20 Cork, Ireland.ORCID 0000-0003-4304-0953
Jennifer MahonySchool of Microbiology, University College Cork, T12 YT20 Cork, Ireland.
Renaud VincentelliArchitecture et Fonction des Macromolécules Biologiques, Aix-Marseille Université, Campus de Luminy, 12388 Marseille, France.
Laurie RamondArchitecture et Fonction des Macromolécules Biologiques, Aix-Marseille Université, Campus de Luminy, 12388 Marseille, France.
Arjen NautaFrieslandCampina, 3800 Amersfoort, The Netherlands.
Douwe van SinderenSchool of Microbiology, University College Cork, T12 YT20 Cork, Ireland. d.vansinderen@ucc.ie.
Christian CambillauSchool of Microbiology, University College Cork, T12 YT20 Cork, Ireland. ccambillau@gmail.com.ORCID 0000-0001-5502-4729

Funding

Science Foundation Ireland 13/IA/1953Science Foundation Ireland 15/SIRG/3430
6 · The paper itself

Abstract

With the availability of an increasing number of 3D structures of bacteriophage components, combined with powerful in silico predictive tools, it has become possible to decipher the structural assembly and functionality of phage adhesion devices. In the current study, we examined 113 members of the 936 group of lactococcal siphophages, and identified a number of Carbohydrate Binding Modules (CBMs) in the neck passage structure and major tail protein, on top of evolved Dit proteins, as recently reported by us. The binding ability of such CBM-containing proteins was assessed through the construction of green fluorescent protein fusion proteins and subsequent binding assays. Two CBMs, one from the phage tail and another from the neck, demonstrated definite binding to their phage-specific host. Bioinformatic analysis of the structural proteins of 936 phages reveals that they incorporate binding modules which exhibit structural homology to those found in other lactococcal phage groups and beyond, indicating that phages utilize common structural "bricks" to enhance host binding capabilities. The omnipresence of CBMs in Siphophages supports their beneficial role in the infection process, as they can be combined in various ways to form appendages with different shapes and functionalities, ensuring their success in host detection in their respective ecological niches.

Indexed as

BacteriophagesCarbohydratesComputational BiologyHost Microbial InteractionsLactococcus lactisModels, MolecularProtein BindingProtein ConformationSiphoviridaeViral Tail ProteinsVirionCarbohydratesViral Tail Proteinsbacteriophagecarbohydrate binding moduleLactococcus lactisphage–host interactionsreceptor-binding protein

Identifiers

PMID31324000
PMCPMC6669499

What OpenQuestion holds

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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.