Evidence map›Paper›PMID 21060797›Full record

ArticlePloS one2010

Determinants of glycan receptor specificity of H2N2 influenza A virus hemagglutinin.

Karthik Viswanathan, Xiaoying Koh, Aarthi Chandrasekaran, Claudia Pappas, Rahul Raman, Aravind Srinivasan, Zachary Shriver, Terrence M Tumpey, Ram Sasisekharan

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
4.4field-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

27 citing papers in PubMed, 42 citations in OpenAlex.

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  10. Shotgun glycomics of pig lung identifies natural endogenous receptors for influenza viruses.Proceedings of the National Academy of Sciences of the United States of America · 2014
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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 4 institutions in 2 countries.

Karthik ViswanathanHarvard-MIT Division of Health Sciences and Technology, Singapore-MIT Alliance for Research and Technology, Department of Biological Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts, United States of America.
Xiaoying Koh
Aarthi Chandrasekaran
Claudia Pappas
Rahul Raman
Aravind Srinivasan
Zachary Shriver
Terrence M Tumpey
Ram Sasisekharan
Singapore-MIT Alliance for Research and Technology · SGCenters for Disease Control and Prevention · USHarvard–MIT Division of Health Sciences and Technology · USMassachusetts Institute of Technology · US

Funding

Structural Basis of Immune Recognition of Glycosylated AntigensU54GM062116 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI BLIXT, OLA KLAS · 2001 to 2010
$80.3M
Structure-Function Relationship of GlycosaminoglycansR37GM057073 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SASISEKHARAN, RAM · 2010 to 2019
$3.9M
Sequence Analysis of GlycosaminoglycansR01GM057073 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SASISEKHARAN, RAM · 1998 to 2010
$3.1M
NIGMS NIH HHS GM57073NIGMS NIH HHS R01 GM057073NIGMS NIH HHS R37 GM057073NIGMS NIH HHS U54 GM062116NIGMS NIH HHS U54 GM62116
6 · The paper itself

Abstract

The H2N2 subtype of influenza A virus was responsible for the Asian pandemic of 1957-58. However, unlike other subtypes that have caused pandemics such as H1N1 and H3N2, which continue to circulate among humans, H2N2 stopped circulating in the human population in 1968. Strains of H2 subtype still continue to circulate in birds and occasionally pigs and could be reintroduced into the human population through antigenic drift or shift. Such an event is a potential global health concern because of the waning population immunity to H2 hemagglutinin (HA). The first step in such a cross-species transmission and human adaptation of influenza A virus is the ability for its surface glycoprotein HA to bind to glycan receptors expressed in the human upper respiratory epithelia. Recent structural and biochemical studies have focused on understanding the glycan receptor binding specificity of the 1957-58 pandemic H2N2 HA. However, there has been considerable HA sequence divergence in the recent avian-adapted H2 strains from the pandemic H2N2 strain. Using a combination of structural modeling, quantitative glycan binding and human respiratory tissue binding methods, we systematically identify mutations in the HA from a recent avian-adapted H2N2 strain (A/Chicken/PA/2004) that make its quantitative glycan receptor binding affinity (defined using an apparent binding constant) comparable to that of a prototypic pandemic H2N2 (A/Albany/6/58) HA.

Indexed as

Binding SitesHemagglutinin Glycoproteins, Influenza VirusInfluenza A Virus, H2N2 SubtypeMutationReceptors, Cell SurfaceHemagglutinin Glycoproteins, Influenza VirusReceptors, Cell Surface

Identifiers

PMID21060797
PMCPMC2966429
OpenAlexW2108565584

What OpenQuestion holds

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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.