Evidence map›Paper›PMID 19224860›Full record

ArticleThe Journal of biological chemistry2009

Oligomerization of the macrophage mannose receptor enhances gp120-mediated binding of HIV-1.

Joey Lai, Oliver K Bernhard, Stuart G Turville, Andrew N Harman, John Wilkinson, Anthony L Cunningham

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

33 citing papers in PubMed, 64 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. The mannose receptor ligands and the macrophage glycome.Current opinion in structural biology · 2022
    Review
  6. Article
  7. Review
  8. From structure to function - Ligand recognition by myeloid C-type lectin receptors.Computational and structural biotechnology journal · 2022
    Review
  9. Article
  10. Vaginal Epithelium Transiently Harbours HIV-1 Facilitating Transmission.Frontiers in cellular and infection microbiology · 2021
    Article
  11. Impact of Protein Glycosylation on the Design of Viral Vaccines.Advances in biochemical engineering/biotechnology · 2021
    Review
  12. The Role of Dendritic Cells in TB and HIV Infection.Journal of clinical medicine · 2020
    Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Paucimannose-RichMolecular & cellular proteomics : MCP · 2017
    Article
  20. Review
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

6 authors at 3 institutions in 2 countries.

Joey LaiCentre for Virus Research, Westmead Millennium Institute, Westmead Hospital, Westmead, Sydney, New South Wales 2145, Australia.
Oliver K Bernhard
Stuart G Turville
Andrew N Harman
John Wilkinson
Anthony L Cunningham
Millennium Institute · BRWestmead Hospital · AULudwig Cancer Research · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

C-type lectin receptors expressed on the surface of dendritic cells and macrophages are able to bind glycoproteins of microbial pathogens via mannose, fucose, and N-acetylglucosamine. Langerin on Langerhans cells, dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin on dendritic cells, and mannose receptor (MR) on dendritic cells and macrophages bind the human immunodeficiency virus (HIV) envelope protein gp120 principally via high mannose oligosaccharides. These C-type lectin receptors can also oligomerize to facilitate enhanced ligand binding. This study examined the effect of oligomerization of MR on its ability to bind to mannan, monomeric gp120, native trimeric gp140, and HIV type 1 BaL. Mass spectrometry analysis of cross-linked MR showed homodimerization on the surface of primary monocyte-derived dendritic cells and macrophages. Both monomeric and dimeric MR were precipitated by mannan, but only the dimeric form was co-immunoprecipitated by gp120. These results were confirmed independently by flow cytometry analysis of soluble monomeric and trimeric HIV envelope and a cellular HIV virion capture assay. As expected, mannan bound to the carbohydrate recognition domains of MR dimers mostly in a calcium-dependent fashion. Unexpectedly, gp120-mediated binding of HIV to dimers on MR-transfected Rat-6 cells and macrophages was not calcium-dependent, was only partially blocked by mannan, and was also partially inhibited by N-acetylgalactosamine 4-sulfate. Thus gp120-mediated HIV binding occurs via the calcium-dependent, non-calcium-dependent carbohydrate recognition domains and the cysteine-rich domain at the C terminus of MR dimers, presenting a much broader target for potential inhibitors of gp120-MR binding.

Indexed as

AcetylgalactosamineAnimalsCalciumCross-Linking ReagentsCysteineDimerizationFlow CytometryHIV-1HIV Envelope Protein gp120HumansLangerhans CellsLectins, C-TypeMacrophagesMannose-Binding LectinsMannose ReceptorOligosaccharidesAcetylgalactosamineCalciumCross-Linking ReagentsCysteinegp120 protein, Human immunodeficiency virus 1HIV Envelope Protein gp120Lectins, C-TypeMannose-Binding LectinsMannose ReceptorOligosaccharidesReceptors, Cell Surface

Identifiers

PMID19224860
PMCPMC2670108
OpenAlexW1984567902

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.