Evidence map›Paper›PMID 33144377›Full record

ArticlemBio2020

The Nontypeable Haemophilus influenzae Major Adhesin Hia Is a Dual-Function Lectin That Binds to Human-Specific Respiratory Tract Sialic Acid Glycan Receptors.

John M Atack, Christopher J Day, Jessica Poole, Kenneth L Brockman, Jamie R L Timms, Linda E Winter, Thomas Haselhorst, Lauren O Bakaletz, Stephen J Barenkamp, Michael P Jennings

Open access · goldAbstract read
In one paragraph

Article in mBio, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

12 citing papers in PubMed, 18 citations in OpenAlex.

  1. ThemBio · 2026
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  12. CEACAM1 Activation by CbpF-ExpressingFrontiers in cellular and infection microbiology · 2021
    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

10 authors at 3 institutions in 2 countries.

John M AtackInstitute for Glycomics, Griffith University, Gold Coast, Queensland, Australia j.atack@griffith.edu.au m.jennings@griffith.edu.au.ORCID 0000-0002-7994-6995
Christopher J DayInstitute for Glycomics, Griffith University, Gold Coast, Queensland, Australia.
Jessica PooleInstitute for Glycomics, Griffith University, Gold Coast, Queensland, Australia.
Kenneth L BrockmanCenter for Microbial Pathogenesis, The Research Institute at Nationwide Children's Hospital and The Ohio State University College of Medicine, Columbus, Ohio, USA.
Jamie R L TimmsInstitute for Glycomics, Griffith University, Gold Coast, Queensland, Australia.
Linda E WinterDepartment of Pediatrics, Saint Louis University School of Medicine, and the Pediatric Research Institute, Cardinal Glennon Children's Medical Center, Saint Louis, Missouri, USA.
Thomas HaselhorstInstitute for Glycomics, Griffith University, Gold Coast, Queensland, Australia.
Lauren O BakaletzCenter for Microbial Pathogenesis, The Research Institute at Nationwide Children's Hospital and The Ohio State University College of Medicine, Columbus, Ohio, USA.ORCID 0000-0002-0017-1710
Stephen J BarenkampDepartment of Pediatrics, Saint Louis University School of Medicine, and the Pediatric Research Institute, Cardinal Glennon Children's Medical Center, Saint Louis, Missouri, USA.
Michael P JenningsInstitute for Glycomics, Griffith University, Gold Coast, Queensland, Australia j.atack@griffith.edu.au m.jennings@griffith.edu.au.ORCID 0000-0002-1027-4684
Griffith University · AUCardinal Glennon Children’s Medical Center · USNationwide Children's Hospital · US

Funding

Otitis media: role of epigenetic regulation on NTHI pathogenesis and optimal vaccine designR01DC015688 · NIDCD · RESEARCH INST NATIONWIDE CHILDREN'S HOSP · PI BAKALETZ, LAUREN O, JENNINGS, MICHAEL PAUL · 2016 to 2020
$2.2M
NIDCD NIH HHS R01 DC015688
6 · The paper itself

Abstract

NTHi is a human-adapted pathogen that colonizes the human respiratory tract. Strains of NTHi express multiple adhesins; however, there is a unique, mutually exclusive relationship between the major adhesins Hia and HMW1 and HMW2 (HMW1/2). Approximately 25% of NTHi strains express Hia, a phase-variable autotransporter protein that has a critical role in colonization of the host nasopharynx. The remaining 75% of strains express HMW1/2. Previous work has shown that the HMW1 and HMW2 proteins mediate binding to 2-3- and 2-6-linked sialic acid glycans found in the human respiratory tract. Here, we show that the high-affinity binding domain of Hia, binding domain 1 (BD1), is responsible for binding to α2-6-sialyllactosamine (2-6 SLN) glycans. BD1 is highly specific for glycans that incorporate the form of sialic acid expressed by humans,

Indexed as

Adhesins, BacterialAmino Acid SequenceBinding SitesBiofilmsHaemophilus InfectionsHaemophilus influenzaeHost-Pathogen InteractionsHumansModels, MolecularMolecular ConformationMolecular StructureProtein BindingReceptors, Cell SurfaceRespiratory MucosaAdhesins, BacterialHia adhesinReceptors, Cell Surfacesialic acid receptoradhesinautotransporter proteinsbacterial pathogenCOPDglycanhost cellmiddle ear infectionNTHi

Identifiers

PMID33144377
PMCPMC7642680
OpenAlexW3096862384

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.