Evidence map›Paper›PMID 16842982›Full record

ArticleBiochimica et biophysica acta2006

Peptides derived from HIV-1, HIV-2, Ebola virus, SARS coronavirus and coronavirus 229E exhibit high affinity binding to the formyl peptide receptor.

John S Mills

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2006. 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
1.4field-weighted citation impact, top 18% 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, 22 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Chemotactic Ligands that Activate G-Protein-Coupled Formylpeptide Receptors.International journal of molecular sciences · 2019
    Review
  8. Therapeutic Potential of Annexin A1 in Ischemia Reperfusion Injury.International journal of molecular sciences · 2018
    Review
  9. Review
  10. Review
  11. Review
  12. Article
  13. Review
  14. Article
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

1 author at 1 institution in 1 country.

John S Mills109 Lewis Hall, Montana State University, Bozeman, MT 59717-3520, USA. umbmj@montana.edu
Montana State University · US

Funding

MT INBRE RESEARCH COREP20RR016455 · NCRR · MONTANA STATE UNIVERSITY - BOZEMAN · PI HARMSEN, ALLEN G · 2001 to 2011
$34.4M
Effects of Formyl Peptide Receptor variants on functionR21DE016114 · NIDCR · MONTANA STATE UNIVERSITY (BOZEMAN) · PI MILLS, JOHN S · 2004 to 2005
$389k
NCRR NIH HHS P20 RR016455NCRR NIH HHS P20 RR-16455-01NIDCR NIH HHS 1R21DE016114-01NIDCR NIH HHS R21 DE016114
6 · The paper itself

Abstract

Peptides derived from the membrane proximal region of fusion proteins of human immunodeficiency viruses 1 and 2, Coronavirus 229 E, severe acute respiratory syndrome coronavirus and Ebola virus were all potent antagonists of the formyl peptide receptor expressed in Chinese hamster ovary cells. Binding of viral peptides was affected by the naturally occurring polymorphisms at residues 190 and 192, which are located at second extracellular loop-transmembrane helix 5 interface. Substitution of R190 with W190 enhanced the affinity for a severe acute respiratory syndrome coronavirus peptide 6 fold but reduced the affinity for N-formyl-Nle-Leu-Phe by 2.5 fold. A 12 mer peptide derived from coronavirus 229E (ETYIKPWWVWL) was the most potent antagonist of the formyl peptide receptor W190 with a K(i) of 230 nM. Fluorescently labeled ETYIKPWWVWL was effectively internalized by all three variants with EC(50) of approximately 25 nM. An HKU-1 coronavirus peptide, MYVKWPWYVWL, was a potent antagonist but N-formyl-MYVKWPWYVWL was a potent agonist. ETYIKPWWVWL did not stimulate GTPgammaS binding but inhibited the stimulation by formyl-NleLeuPhe. It also blocked beta arrestin translocation and receptor downregulation induced by formyl-Nle-Leu-Phe. This indicates that formyl peptide receptor may be important in viral infections and that variations in its sequence among individuals may affect their likelihood of viral and bacterial infections.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCHO CellsCoronavirus 229E, HumanCricetinaeEbolavirusGuanosine 5'-O-(3-Thiotriphosphate)HIV-1HIV-2HumansKineticsModels, MolecularMolecular Sequence DataPeptide FragmentsProtein BindingGuanosine 5'-O-(3-Thiotriphosphate)Peptide FragmentsReceptors, Formyl PeptideViral Proteins

Identifiers

PMID16842982
PMCPMC2075610
OpenAlexW2148819068

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.