Evidence map›Paper›PMID 20015992›Full record

ArticleJournal of virology2010

The potent anti-HIV activity of CXCL12gamma correlates with efficient CXCR4 binding and internalization.

Jeffrey D Altenburg, Qingwen Jin, Bashar Alkhatib, Ghalib Alkhatib

Abstract read
In one paragraph

Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.5field-weighted citation impact, top 35% 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

15 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. Article
  3. Endogenous Peptide Inhibitors of HIV Entry.Advances in experimental medicine and biology · 2022
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
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  11. The role of tyrosine sulfation in the dimerization of the CXCR4:SDF-1 complex.Protein science : a publication of the Protein Society · 2013
    Article
  12. Article
  13. Article
  14. Article
  15. 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

4 authors at 2 institutions in 1 country.

Jeffrey D AltenburgDepartment of Microbiology and Immunology, Indiana University School of Medicine, Indianapolis, Indiana, USA.
Qingwen Jin
Bashar Alkhatib
Ghalib Alkhatib
Indiana University School of MedicineIndiana University – Purdue University Indianapolis · US

Funding

Host Cell Factors and AIDS PathogenesisR01AI052019 · NIAID · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI ALKHATIB, GHALIB ABBAS · 2002 to 2013
$4.0M
NIAID NIH HHS R01 AI052019NIMHD NIH HHS L60 MD003100PHS HHS R01 A152019-01
6 · The paper itself

Abstract

We previously demonstrated that the naturally occurring splice variant stromal cell-derived factor 1gamma/CXCL12gamma is the most potent CXCL12 isoform in blocking X4 HIV-1, with weak chemotactic activity. A conserved BBXB domain (B for basic and X for any residue) located in the N terminus ((24)KHLK(27)) is found in all six isoforms of CXCL12. To determine whether the potent antiviral activity of CXCL12gamma is due to the presence of the extra C-terminal BBXB domains, we mutated each domain individually as well as in combination. Although binding of CXCL12gamma to heparan sulfate proteoglycan (HSPG) was 10-fold higher than that observed with CXCL12alpha, the results did not demonstrate a direct correlation between HSPG binding and the potent antiviral activity. CXCL12gamma mutants lacking the conserved BBXB domain (designated gammaB1) showed increased binding to HSPG but reduced anti-HIV activity. In contrast, the mutants lacking the C-terminal second and/or third BBXB domain but retaining the conserved domain (designated B2, B3, and B23) showed decreased binding to HSPG but increased anti-HIV activity. The B2, B3, and B23 mutants were associated with enhanced CXCR4 binding, receptor internalization, and restored chemotaxis. Internalization of CXCR4 was more potent with CXCL12gamma than with CXCL12alpha and was significantly reduced when the conserved BBXB domain was mutated. We concluded that the observed potent anti-HIV-1 activity of CXCL12gamma is due to increased affinity for CXCR4 and to efficient receptor internalization.

Indexed as

Amino Acid SequenceAnimalsCell LineChemokine CXCL12HIV-1HumansMolecular Sequence DataMutationProtein IsoformsProtein Structure, TertiaryReceptors, CXCR4Sequence AlignmentChemokine CXCL12Protein IsoformsReceptors, CXCR4

Identifiers

PMID20015992
PMCPMC2820898
OpenAlexW2092851520

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.