Evidence map›Paper›PMID 22685299›Full record

ArticleThe Journal of biological chemistry2012

A unique sugar-binding site mediates the distinct anti-influenza activity of pig surfactant protein D.

Martin van Eijk, Michael J Rynkiewicz, Mitchell R White, Kevan L Hartshorn, Xueqing Zou, Klaus Schulten, Dong Luo, Erika C Crouch, Tanya R Cafarella, James F Head and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

14 citing papers in PubMed, 25 citations in OpenAlex.

  1. Adaptation and conservation of CL-10/11 in avian lungs: implications for their role in pulmonary innate immune protection.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Article
  2. Article
  3. Article
  4. Innate Immunity and Influenza A Virus Pathogenesis: Lessons for COVID-19.Frontiers in cellular and infection microbiology · 2020
    Review
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  6. Article
  7. Article
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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

12 authors at 4 institutions in 2 countries.

Martin van EijkDepartment of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, 3584 CL Utrecht, The Netherlands.
Michael J Rynkiewicz
Mitchell R White
Kevan L Hartshorn
Xueqing Zou
Klaus Schulten
Dong Luo
Erika C Crouch
Tanya R Cafarella
James F Head
Henk P Haagsman
Barbara A Seaton
Boston University · USUniversity of Illinois Urbana-Champaign · USUtrecht University · NLWashington University in St. Louis · US

Funding

WHOLE CELL SIMULATIONP41RR005969 · NCRR · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI STONE, JOHN H · 1990 to 2011
$19.8M
Enhancing Collectin-Mediated Defense Against InfluenzaR01HL069031 · NHLBI · BOSTON MEDICAL CENTER · PI HARTSHORN, KEVAN L · 2002 to 2018
$6.6M
Collectins and Innate Defense against Inhaled PathogensP01AI083222 · NIAID · BOSTON UNIVERSITY MEDICAL CAMPUS · PI SEATON, BARBARA A · 2009 to 2010
$4.9M
NCRR NIH HHS P41-RR005969NHLBI NIH HHS HL069031NHLBI NIH HHS R01 HL069031NIAID NIH HHS AI083222NIAID NIH HHS P01 AI083222
6 · The paper itself

Abstract

Pigs can act as intermediate hosts by which reassorted influenza A virus (IAV) strains can be transmitted to humans and cause pandemic influenza outbreaks. The innate host defense component surfactant protein D (SP-D) interacts with glycans on the hemagglutinin of IAV and contributes to protection against IAV infection in mammals. This study shows that a recombinant trimeric neck lectin fragment derived from porcine SP-D (pSP-D) exhibits profound inhibitory activity against IAV, in contrast to comparable fragments derived from human SP-D. Crystallographic analysis of the pSP-D fragment complexed with a viral sugar component shows that a unique tripeptide loop alters the lectin site conformation of pSP-D. Molecular dynamics simulations highlight the role of this flexible loop, which adopts a more stable conformation upon sugar binding and may facilitate binding to viral glycans through contact with distal portions of the branched mannoside. The combined data demonstrate that porcine-specific structural features of SP-D contribute significantly to its distinct anti-IAV activity. These findings could help explain why pigs serve as important reservoirs for newly emerging pathogenic IAV strains.

Indexed as

Carbohydrate MetabolismAnimalsAntiviral AgentsBase SequenceBinding SitesCells, CulturedCrystallizationDNA PrimersDogsInfluenza A virusMicrobial Sensitivity TestsModels, MolecularMolecular Dynamics SimulationMutagenesis, Site-DirectedPulmonary Surfactant-Associated Protein DSwineAntiviral AgentsDNA PrimersPulmonary Surfactant-Associated Protein D

Identifiers

PMID22685299
PMCPMC3411006
OpenAlexW2085536315

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.