Evidence map›Paper›PMID 32958885›Full record

ArticleScientific reports2020

Structure and function of bacteriophage CBA120 ORF211 (TSP2), the determinant of phage specificity towards E. coli O157:H7.

Julia Greenfield, Xiaoran Shang, Heng Luo, Yan Zhou, Sara B Linden, Ryan D Heselpoth, Petr G Leiman, Daniel C Nelson, Osnat Herzberg

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

19 citing papers in PubMed, 41 citations in OpenAlex.

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  18. Structural and functional characterization of the receptor binding proteins ofComputational and structural biotechnology journal · 2021
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  19. Subtypes of tail spike proteins predicts the host range ofComputational and structural biotechnology journal · 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

9 authors at 3 institutions in 1 country.

Julia GreenfieldInstitute for Bioscience and Biotechnology Research, University of Maryland, 9600 Gudelsky Dr, Rockville, MD, 20850, USA.
Xiaoran ShangInstitute for Bioscience and Biotechnology Research, University of Maryland, 9600 Gudelsky Dr, Rockville, MD, 20850, USA.
Heng LuoInstitute for Bioscience and Biotechnology Research, University of Maryland, 9600 Gudelsky Dr, Rockville, MD, 20850, USA.
Yan ZhouInstitute for Bioscience and Biotechnology Research, University of Maryland, 9600 Gudelsky Dr, Rockville, MD, 20850, USA.
Sara B LindenInstitute for Bioscience and Biotechnology Research, University of Maryland, 9600 Gudelsky Dr, Rockville, MD, 20850, USA.
Ryan D HeselpothInstitute for Bioscience and Biotechnology Research, University of Maryland, 9600 Gudelsky Dr, Rockville, MD, 20850, USA.
Petr G LeimanDepartment of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics, University of Texas, Medical Branch, 301 University Blvd, Galveston, TX, 77555, USA.
Daniel C NelsonInstitute for Bioscience and Biotechnology Research, University of Maryland, 9600 Gudelsky Dr, Rockville, MD, 20850, USA. nelsond@umd.edu.
Osnat HerzbergInstitute for Bioscience and Biotechnology Research, University of Maryland, 9600 Gudelsky Dr, Rockville, MD, 20850, USA. osnat@umd.edu.
Institute for Bioscience and Biotechnology ResearchThe University of Texas Medical Branch at Galveston · USUniversity of Maryland, College Park · US

Funding

Structural and functional determinants of decision-making in bacteriophage host recognitionR01GM139034 · NIGMS · UNIVERSITY OF TEXAS MED BR GALVESTON · PI LEIMAN, PETR G · 2020 to 2023
$1.7M
Structure, Function, and Engineering of Myovirus Phage CBA120 Tailspike ProteinsR01GM110202 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI NELSON, DANIEL C. · 2015 to 2019
$1.5M
NIGMS NIH HHS R01 GM110202NIGMS NIH HHS R01GM110202NIGMS NIH HHS R01 GM139034
6 · The paper itself

Abstract

The genome of Escherichia coli O157:H7 bacteriophage vB_EcoM_CBA120 encodes four distinct tailspike proteins (TSPs). The four TSPs, TSP1-4, attach to the phage baseplate forming a branched structure. We report the 1.9 Å resolution crystal structure of TSP2 (ORF211), the TSP that confers phage specificity towards E. coli O157:H7. The structure shows that the N-terminal 168 residues involved in TSPs complex assembly are disordered in the absence of partner proteins. The ensuing head domain contains only the first of two fold modules seen in other phage vB_EcoM_CBA120 TSPs. The catalytic site resides in a cleft at the interface between adjacent trimer subunits, where Asp506, Glu568, and Asp571 are located in close proximity. Replacement of Asp506 and Asp571 for alanine residues abolishes enzyme activity, thus identifying the acid/base catalytic machinery. However, activity remains intact when Asp506 and Asp571 are mutated into asparagine residues. Analysis of additional site-directed mutants in the background of the D506N:D571N mutant suggests engagement of an alternative catalytic apparatus comprising Glu568 and Tyr623. Finally, we demonstrate the catalytic role of two interacting glutamate residues of TSP1, located in a cleft between two trimer subunits, Glu456 and Glu483, underscoring the diversity of the catalytic apparatus employed by phage vB_EcoM_CBA120 TSPs.

Indexed as

BacteriophagesCatalytic DomainEscherichia coli O157Glycoside HydrolasesSpecies SpecificityViral Tail ProteinsVirionGlycoside Hydrolasestailspike protein, bacteriophageViral Tail Proteins

Identifiers

PMID32958885
PMCPMC7506556
OpenAlexW3087579739

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.