Evidence map›Paper›PMID 20714354›Full record

ArticlePLoS pathogens2010

Bacteriophage lysin mediates the binding of streptococcus mitis to human platelets through interaction with fibrinogen.

Ho Seong Seo, Yan Q Xiong, Jennifer Mitchell, Ravin Seepersaud, Arnold S Bayer, Paul M Sullam

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
6.7field-weighted citation impact, top 3% 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

35 citing papers in PubMed, 61 citations in OpenAlex.

  1. Trial
  2. Serotype-Dependent Inhibition ofJournal of microbiology and biotechnology · 2024
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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

6 authors at 4 institutions in 2 countries.

Ho Seong SeoDivision of Infectious Diseases, Veterans Affairs Medical Center and the University of California, San Francisco, California, United States of America.
Yan Q Xiong
Jennifer Mitchell
Ravin Seepersaud
Arnold S Bayer
Paul M Sullam
San Francisco VA Medical Center · USHarbor–UCLA Medical Center · USUCLA Medical Center · USUniversity College Dublin · IE

Funding

STREPTOCOCCAL PLATELET BINDING AND ENDOCARDITISR01AI041513 · NIAID · NORTHERN CALIFORNIA INSTITUTE RES &EDUC · PI SULLAM, PAUL M. · 1997 to 2019
$5.6M
Staphylococcal Adaptations to Platelet Microbicidal ProteinR01AI039108 · NIAID · LUNDQUIST INSTITUTE FOR BIOMEDICAL INNOVATION AT HARBOR-UCLA MEDICAL CENTER · PI BAYER, ARNOLD S · 1997 to 2016
$5.1M
Prophage-Encoded Binding of S. mitis to Human PlateletsR01AI057433 · NIAID · NORTHERN CALIFORNIA INSTITUTE RES &EDUC · PI SULLAM, PAUL M. · 2004 to 2008
$1.8M
NIAID NIH HHS R01 AI039108NIAID NIH HHS R01-AI039108NIAID NIH HHS R01 AI041513NIAID NIH HHS R01 AI057433NIAID NIH HHS R01-AI057433NIAID NIH HHS R01-AI41513
6 · The paper itself

Abstract

The binding of bacteria to human platelets is a likely central mechanism in the pathogenesis of infective endocarditis. We have previously found that platelet binding by Streptococcus mitis SF100 is mediated by surface components encoded by a lysogenic bacteriophage, SM1. We now demonstrate that SM1-encoded lysin contributes to platelet binding via its direct interaction with fibrinogen. Far Western blotting of platelets revealed that fibrinogen was the major membrane-associated protein bound by lysin. Analysis of lysin binding with purified fibrinogen in vitro confirmed that these proteins could bind directly, and that this interaction was both saturable and inhibitable. Lysin bound both the Aalpha and Bbeta chains of fibrinogen, but not the gamma subunit. Binding of lysin to the Bbeta chain was further localized to a region within the fibrinogen D fragment. Disruption of the SF100 lysin gene resulted in an 83+/-3.1% reduction (mean +/- SD) in binding to immobilized fibrinogen by this mutant strain (PS1006). Preincubation of this isogenic mutant with purified lysin restored fibrinogen binding to wild type levels. When tested in a co-infection model of endocarditis, loss of lysin expression resulted in a significant reduction in virulence, as measured by achievable bacterial densities (CFU/g) within vegetations, kidneys, and spleens. These results indicate that bacteriophage-encoded lysin is a multifunctional protein, representing a new class of fibrinogen-binding proteins. Lysin appears to be cell wall-associated through its interaction with choline. Once on the bacterial surface, lysin can bind fibrinogen directly, which appears to be an important interaction for the pathogenesis of endocarditis.

Indexed as

Amino Acid SequenceAnimalsBlood PlateletsBlotting, WesternEndocarditis, BacterialFibrinogenHumansMolecular Sequence DataMucoproteinsRatsStreptococcal InfectionsStreptococcus mitisStreptococcus PhagesViral ProteinsVirulenceFibrinogenlysin, gastropodaMucoproteinsViral Proteins

Identifiers

PMID20714354
PMCPMC2920869
OpenAlexW2161509463

What OpenQuestion holds

Textmetadata
LicenceCC0
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.