Evidence map›Paper›PMID 7543140›Full record

ArticleThe Journal of experimental medicine1995

Role of virion-associated glycosylphosphatidylinositol-linked proteins CD55 and CD59 in complement resistance of cell line-derived and primary isolates of HIV-1.

M Saifuddin, C J Parker, M E Peeples, M K Gorny, S Zolla-Pazner, M Ghassemi, I A Rooney, J P Atkinson, G T Spear

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of experimental medicine, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
106citing papers in PubMed, 1 pooled it
3.1field-weighted citation impact, top 6% 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

106 citing papers in PubMed, 1 synthesis or guideline pooled it, 246 citations in OpenAlex.

  1. Pooled it
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  12. Complement contributes to antibody-mediated protection against repeated SHIV challenge.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  13. Article
  14. Review
  15. Article
  16. Innate Immune Response Against HIV-1.Advances in experimental medicine and biology · 2021
    Article
  17. Article
  18. Article
  19. Review
  20. Article

46 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

9 authors at 1 institution in 1 country.

M SaifuddinDepartment of Immunology/Microbiology, Rush University, Chicago, Illinois 60612, USA.
C J Parker
M E Peeples
M K Gorny
S Zolla-Pazner
M Ghassemi
I A Rooney
J P Atkinson
G T Spear
Rush University · US

Funding

COMPLEMENT INTERACTION WITH HIV AND HIV-INFECTED CELLSR01AI029661 · NIAID · RUSH UNIVERSITY MEDICAL CENTER · PI SPEAR, GREGORY T · 1992 to 1995
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INTERACTION OF HIV-1 WITH COMPLEMENTR01AI031812 · NIAID · RUSH UNIVERSITY MEDICAL CENTER · PI SPEAR, GREGORY T · 1996 to 1998
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INTERACTION OF HIV-1 WITH COMPLEMENTR29AI031812 · NIAID · RUSH UNIVERSITY MEDICAL CENTER · PI SPEAR, GREGORY T · 1991 to 1995
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NIAID NIH HHS AI 29661NIAID NIH HHS AI 31812
6 · The paper itself

Abstract

This study investigates whether cell-derived glycosylphosphatidylinositol-linked complement control proteins CD55 and CD59 can be incorporated into HIV-1 virions and contribute to complement resistance. Virus was prepared by transfection of cell lines with pNL4-3, and primary isolates of HIV-1 were derived from patients' PBMCs. Virus was tested for sensitivity to complement-mediated virolysis in the presence of anti-gp160 antibody. Viral preparations from JY33 cells, which lack CD55 and CD59, were highly sensitive to complement. HIV-1 preparations from H9 and U937 cells, which express low levels of CD55 and CD59, had intermediate to high sensitivity while other cell line-derived viruses and primary isolates of HIV-1 were resistant to complement-mediated virolysis. Although the primary isolates were not lysed, they activated complement as measured by binding to a complement receptor positive cell line. While the primary isolates were resistant to lysis in the presence of HIV-specific antibody, antibody to CD59 induced lysis. Likewise, antibody to CD55 and CD59 induced lysis of cell line-derived virus. Western blot analysis of purified virus showed bands corresponding to CD55 and CD59. Phosphatidylinositol-specific phospholipase C treatment of either cell line-derived or primary isolates of HIV-1 increased sensitivity to complement while incubation of sensitive virus with purified CD55 and CD59 increased resistance to complement. These results show that CD55 and CD59 are incorporated into HIV-1 particles and function to protect virions from complement-mediated destruction, and they are the first report of host cell proteins functioning in protection of HIV-1 from immune effector mechanisms.

Indexed as

GlycosylphosphatidylinositolsAntigens, CDBlotting, WesternCD55 AntigensCD59 AntigensCell LineComplement ActivationComplement System ProteinsHIV-1HumansIn Vitro TechniquesMembrane GlycoproteinsPhosphatidylinositol Diacylglycerol-LyasePhosphoinositide Phospholipase CPhosphoric Diester HydrolasesAntigens, CDCD55 AntigensCD59 AntigensComplement System ProteinsGlycosylphosphatidylinositolsMembrane GlycoproteinsPhosphatidylinositol Diacylglycerol-LyasePhosphoinositide Phospholipase CPhosphoric Diester Hydrolases

Identifiers

PMID7543140
PMCPMC2192116
OpenAlexW2168101800

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.