Evidence map›Paper›PMID 9658072›Full record

ArticleJournal of virology1998

Determinants of human immunodeficiency virus type 1 envelope glycoprotein activation by soluble CD4 and monoclonal antibodies.

N Sullivan, Y Sun, J Binley, J Lee, C F Barbas, P W Parren, D R Burton, J Sodroski

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

84 citing papers in PubMed, 130 citations in OpenAlex.

  1. Article
  2. Article
  3. Virus Entry Inhibitors: Past, Present, and Future.Advances in experimental medicine and biology · 2022
    Review
  4. Article
  5. Article
  6. Article
  7. Nanoparticles presenting clusters of CD4 expose a universal vulnerability of HIV-1 by mimicking target cells.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Long-Term Persistence of Anti-HIV Broadly Neutralizing Antibody-Secreting Hematopoietic Cells in Humanized Mice.Molecular therapy : the journal of the American Society of Gene Therapy · 2019
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

24 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

8 authors at 2 institutions in 1 country.

N SullivanDivision of Human Retrovirology, Dana-Farber Cancer Institute, Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115, USA.
Y Sun
J Binley
J Lee
C F Barbas
P W Parren
D R Burton
J Sodroski
Harvard University · USScripps Research Institute · US

Funding

HIV-1 ENVELOPE GLYCOPROTEINSR37AI024755 · NIAID · DANA-FARBER CANCER INSTITUTE · PI SODROSKI, JOSEPH G · 1996 to 2015
$11.6M
MOLECULAR STUDIES OF HIV1 NEUTRALIZING ANTIBODIESR01AI031783 · NIAID · DANA-FARBER CANCER INSTITUTE · PI SODROSKI, JOSEPH G · 1991 to 2007
$2.9M
ROLE OF THE HTLV-III ENVELOPE GLYCOPROTEIN IN VIRUSR01AI024755 · NIAID · DANA-FARBER CANCER INSTITUTE · PI SODROSKI, JOSEPH G · 1987 to 1995
–
NIAID NIH HHS AI 24755NIAID NIH HHS AI 31783NIAID NIH HHS R01 AI031783NIAID NIH HHS R37 AI024755
6 · The paper itself

Abstract

Infection by some human immunodeficiency virus type 1 (HIV-1) isolates is enhanced by the binding of subneutralizing concentrations of soluble receptor, soluble CD4 (sCD4), or monoclonal antibodies directed against the viral envelope glycoproteins. In this work, we studied the abilities of different antibodies to mediate activation of the envelope glycoproteins of a primary HIV-1 isolate, YU2, and identified the regions of gp120 envelope glycoprotein contributing to activation. Binding of antibodies to a variety of epitopes on gp120, including the CD4 binding site, the third variable (V3) loop, and CD4-induced epitopes, enhanced the entry of viruses containing YU2 envelope glycoproteins. Fab fragments of antibodies directed against either the CD4 binding site or V3 loop also activated YU2 virus infection. The activation phenotype was conferred on the envelope glycoproteins of a laboratory-adapted HIV-1 isolate (HXBc2) by replacing the gp120 V3 loop or V1/V2 and V3 loops with those of the YU2 virus. Infection by the YU2 virus in the presence of activating antibodies remained inhibitable by macrophage inhibitory protein 1beta, indicating dependence on the CCR5 coreceptor on the target cells. Thus, antibody enhancement of YU2 entry involves neither Fc receptor binding nor envelope glycoprotein cross-linking, is determined by the same variable loops that dictate enhancement by sCD4, and probably proceeds by a process fundamentally similar to the receptor-activated virus entry pathway.

Indexed as

AnimalsAntibodies, MonoclonalCD4 AntigensCells, CulturedChemokine CCL4COS CellsEpitopes, B-LymphocyteHIV-1HIV AntibodiesHIV Envelope Protein gp120HumansImmunoglobulin Fab FragmentsMacrophage Inflammatory ProteinsRecombinant ProteinsAntibodies, MonoclonalCD4 AntigensChemokine CCL4Epitopes, B-LymphocyteHIV AntibodiesHIV Envelope Protein gp120Immunoglobulin Fab FragmentsMacrophage Inflammatory ProteinsRecombinant Proteinsrecombinant soluble CD4

Identifiers

PMID9658072
PMCPMC109776
OpenAlexW2133017175

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.