Evidence map›Paper›PMID 21937438›Full record

ArticleThe Journal of biological chemistry2011

Functional characterization of the interaction between bacterial adhesin multivalent adhesion molecule 7 (MAM7) protein and its host cell ligands.

Anne Marie Krachler, Kim Orth

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. 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
5.0field-weighted citation impact, top 5% 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, 77 citations in OpenAlex.

  1. The role of adhesins ofGut microbes · 2026
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  11. Review
  12. Type III Secretion 1 Effector Gene Diversity AmongFrontiers in cellular and infection microbiology · 2020
    Article
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  16. Infection and immunity · 2019
    Article
  17. Article
  18. Article
  19. Exploring the Genomic Traits of Non-toxigenicFrontiers in microbiology · 2018
    Article
  20. 3-Sulfogalactosyl-dependent adhesion ofThe Journal of biological chemistry · 2017
    Article
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

2 authors at 1 institution in 1 country.

Anne Marie KrachlerDepartment of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA.
Kim Orth
The University of Texas Southwestern Medical Center · US

Funding

Biochemical Characterization of Yersinia Effector YopJ.R01AI056404 · NIAID · UT SOUTHWESTERN MEDICAL CENTER · PI ORTH, KIM · 2003 to 2012
$2.8M
Analysis of an orchestrated cell death mediated by Vibrio parahaemolytics T3SS1R01AI087808 · NIAID · UT SOUTHWESTERN MEDICAL CENTER · PI ORTH, KIM · 2010 to 2014
$1.9M
NIAID NIH HHS R01 AI056404NIAID NIH HHS R01-AI056404NIAID NIH HHS R01 AI087808NIAID NIH HHS R01-AI087808
6 · The paper itself

Abstract

The ability of a pathogen to rapidly form a stable interaction with the host cell surface is key to its success. Bacterial pathogens use a repertoire of virulence factors, but their efficient use relies on close contact between the host and the pathogen. We have recently identified a constitutively expressed MAM7 (multivalent adhesion molecule 7), which is widely distributed in gram-negative pathogens and enables them to establish initial contact with the host cell. Here, we describe the dissection of the MAM7 interaction with the host cell surface into two distinct binding events, involving the host protein fibronectin and the membrane phospholipid phosphatidic acid. We analyzed which domains within MAM7 and fibronectin are necessary for complex formation. We further studied phosphatidic acid binding by MAM7 using site-directed mutagenesis and liposome association assays and demonstrated that a specific distribution of basic charge on MAM7 is required for high affinity binding. Finally, we showed that fibronectin and phosphatidic acid binding to MAM7 are not mutually exclusive and that the three molecules likely assemble into a tripartite complex on the host cell surface.

Indexed as

Adhesins, BacterialCell LineFibronectinsHumansLigandsPhosphatidic AcidsProtein BindingVibrio parahaemolyticusAdhesins, BacterialFibronectinsLigandsPhosphatidic Acids

Identifiers

PMID21937438
PMCPMC3234719
OpenAlexW2005361382

What OpenQuestion holds

Textmetadata
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.