Evidence map›Paper›PMID 15601777›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

Influenza virus entry and infection require host cell N-linked glycoprotein.

Victor C Chu, Gary R Whittaker

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 122 papers.

0numbers the graph read from it
0cells of the map it votes in
122citing papers in PubMed
6.1field-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

122 citing papers in PubMed, 203 citations in OpenAlex.

  1. Review
  2. Airway macrophage specific glycocalyx expression and remodeling following viral infection.Matrix biology : journal of the International Society for Matrix Biology · 2026
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62 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

Victor C ChuDepartment of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, USA.
Gary R Whittaker
Cornell University · USIcahn School of Medicine at Mount Sinai · US

Funding

Endocytosis of Influenza VirusesR01AI048678 · NIAID · CORNELL UNIVERSITY ITHACA · PI WHITTAKER, GARY R · 2001 to 2011
$3.4M
NIAID NIH HHS R01 AI048678NIAID NIH HHS R01AI48678
6 · The paper itself

Abstract

A widely held view of influenza virus infection is that the viral receptor consists of cell surface carbohydrate sialic acid, which can be present as glycoprotein or glycolipid. Here, we examined influenza virus entry and infection in Lec1 cells, a mutant CHO cell line deficient in terminal N-linked glycosylation caused by a mutation in the N-acetylglucosaminyltransferase I (GnT1) gene. We show that influenza virus cannot infect Lec1 cells, despite having full capacity to undergo virus binding and fusion. Lec1 cells also show no virus replication defect, and infection was restored in Lec1 cells expressing wild-type GnT1. Viruses were apparently arrested at the level of internalization from the plasma membrane and were not endocytosed. Lec1 cells were refractory to infection by several strains of influenza virus, including H1 and H3 strains of influenza A, as well as influenza B virus. Finally, cleavage of N-glycans from wild-type CHO cells markedly reduced infection by influenza virus. We suggest that influenza virus specifically requires N-linked glycoprotein for entry into cells, and that sialic acid, although acting as an efficient attachment factor, is not sufficient as an influenza virus receptor in vivo.

Indexed as

AnimalsBiotinBiotinylationCarbohydratesCell LineCells, CulturedCHO CellsCricetinaeEndocytosisFlow CytometryFluorescent Antibody Technique, IndirectGlycoproteinsHeLa CellsHumansInfluenza, HumanMutationalpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase IBiotinCarbohydratesGlycoproteinsN-AcetylglucosaminyltransferasesN-Acetylneuraminic AcidPeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine AmidaseViral Fusion Proteins

Identifiers

PMID15601777
PMCPMC535801
OpenAlexW2023362879

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.