Evidence map›Paper›PMID 32326128›Full record

ReviewCells2020

Role of Protein Glycosylation in Host-Pathogen Interaction.

Borong Lin, Xue Qing, Jinling Liao, Kan Zhuo

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers.

0numbers the graph read from it
0cells of the map it votes in
94citing papers in PubMed
7.8field-weighted citation impact, top 2% 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

94 citing papers in PubMed, 170 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Carbohydrate-based biosensors for enhanced pathogen detection.Analytical and bioanalytical chemistry · 2026
    Review
  7. Review
  8. Review
  9. Review
  10. Raman signatures ofFrontiers in microbiology · 2026
    Article
  11. Article
  12. Review
  13. Emerging Mechanistic Links Between Fucosylation and Senescence in Lung Diseases.Journal of respiratory biology and translational medicine · 2026
    Article
  14. Review
  15. Article
  16. Review
  17. Review
  18. Article
  19. Review
  20. Review

34 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

4 authors at 3 institutions in 1 country.

Borong LinLaboratory of Plant Nematology, South China Agricultural University, Guangzhou 510642, China.
Xue QingCollege of Plant Protection, Nanjing Agricultural University, Nanjing 210095, China.
Jinling LiaoLaboratory of Plant Nematology, South China Agricultural University, Guangzhou 510642, China.
Kan ZhuoLaboratory of Plant Nematology, South China Agricultural University, Guangzhou 510642, China.
South China Agricultural University · CNGuangdong Polytechnic Normal University · CNNanjing Agricultural University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Host-pathogen interactions are fundamental to our understanding of infectious diseases. Protein glycosylation is one kind of common post-translational modification, forming glycoproteins and modulating numerous important biological processes. It also occurs in host-pathogen interaction, affecting host resistance or pathogen virulence often because glycans regulate protein conformation, activity, and stability, etc. This review summarizes various roles of different glycoproteins during the interaction, which include: host glycoproteins prevent pathogens as barriers; pathogen glycoproteins promote pathogens to attack host proteins as weapons; pathogens glycosylate proteins of the host to enhance virulence; and hosts sense pathogen glycoproteins to induce resistance. In addition, this review also intends to summarize the roles of lectin (a class of protein entangled with glycoprotein) in host-pathogen interactions, including bacterial adhesins, viral lectins or host lectins. Although these studies show the importance of protein glycosylation in host-pathogen interaction, much remains to be discovered about the interaction mechanism.

Indexed as

AnimalsGlycoproteinsGlycosylationHost-Pathogen InteractionsHumansLectinsPolysaccharidesProtein Processing, Post-TranslationalGlycoproteinsLectinsPolysaccharidesglycoproteinhostinteractionpathogenresistancevirulence

Identifiers

PMID32326128
PMCPMC7226260
OpenAlexW3016742691

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.