Evidence map›Paper›PMID 19955519›Full record

ArticleJournal of immunology (Baltimore, Md. : 1950)2010

A high-affinity inhibitor of human CD59 enhances complement-mediated virolysis of HIV-1: implications for treatment of HIV-1/AIDS.

Weiguo Hu, Qigui Yu, Ningjie Hu, Daniel Byrd, Tohti Amet, Cecilia Shikuma, Bruce Shiramizu, Jose A Halperin, Xuebin Qin

Open access · bronzeAbstract read
In one paragraph

Article in Journal of immunology (Baltimore, Md. : 1950), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed, 1 pooled it
1.0field-weighted citation impact, top 27% 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

31 citing papers in PubMed, 1 synthesis or guideline pooled it, 42 citations in OpenAlex.

  1. Pooled it
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  10. The role of the complement system in HIV infection and preeclampsia.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2019
    Review
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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 3 institutions in 1 country.

Weiguo HuDepartment of Medicine, Brigham and Women's Hospital, Boston, MA 02115, USA.
Qigui Yu
Ningjie Hu
Daniel Byrd
Tohti Amet
Cecilia Shikuma
Bruce Shiramizu
Jose A Halperin
Xuebin Qin
University of Hawaiʻi at Mānoa · USBrigham and Women's Hospital · USIndiana University School of Medicine

Funding

University of Washington/Fred Hutch Center for AIDS ResearchP30AI027757 · NIAID · UNIVERSITY OF WASHINGTON · PI EDWIN ROBERTO ORELLANA · 1988 to 2026
$104.9M
Towards a Mouse Model of Complement-Mediated DiseasesR01AI061174 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI QIN, XUEBIN · 2005 to 2009
$1.8M
EXTRAMURAL RESEARCH FACILITIES CONSTRUCTIONC06RR015481 · NCRR · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI FIFE, ROSE S · 2001 to 2001
$1.6M
Specific killing of latently HIV-1-infected cells after provirus reactivationR33AI104268 · NIAID · INDIANA UNIVERSITY INDIANAPOLIS · PI YU, QIGUI A. · 2015 to 2017
$1.2M
Development of Molecular Adjuvants for Therapeutic HIV-1 VaccinesR21AI073250 · NIAID · UNIVERSITY OF HAWAII AT MANOA · PI YU, QIGUI A. · 2007 to 2008
$362k
NCRR NIH HHS C06 RR015481NCRR NIH HHS C06 RR015481-01NIAID NIH HHS AI 27757NIAID NIH HHS P30 AI027757NIAID NIH HHS R01 AI061174NIAID NIH HHS R21 AI073250NIAID NIH HHS R21AI073250NIAID NIH HHS R33 AI104268
6 · The paper itself

Abstract

Many pathogenic enveloped viruses, including HIV-1, escape complement-mediated virolysis by incorporating host cell regulators of complement activation into their own viral envelope. The presence of complement regulators including CD59 on the external surface of the viral envelope confers resistance to complement-mediated virolysis, which may explain why human pathogenic viruses such as HIV-1 are not neutralized by complement in human fluids, even in the presence of high Ab titers against the viral surface proteins. In this study, we report the development of a recombinant form of the fourth domain of the bacterial toxin intermedilysin (the recombinant domain 4 of intermedilysin [rILYd4]), a 114 aa protein that inhibits human CD59 function with high affinity and specificity. In the presence of rILYd4, HIV-1 virions derived from either cell lines or peripheral blood mononuclear cells of HIV-1-infected patients became highly sensitive to complement-mediated lysis activated by either anti-HIV-1 gp120 Abs or by viral infection-induced Abs present in the plasma of HIV-1-infected individuals. We also demonstrated that rILYd4 together with serum or plasma from HIV-1-infected patients as a source of anti-HIV-1 Abs and complement did not mediate complement-mediated lysis of either erythrocytes or peripheral blood mononuclear cells. These results indicate that rILYd4 may represent a novel therapeutic agent against HIV-1/AIDS.

Indexed as

Acquired Immunodeficiency SyndromeBacteriocinsCD59 AntigensComplement ActivationComplement System ProteinsFlow CytometryHIV-1HumansRecombinant ProteinsBacteriocinsCD59 AntigensComplement System Proteinsintermedilysin protein, Streptococcus intermediusRecombinant Proteins

Identifiers

PMID19955519
PMCPMC4272871
OpenAlexW1760063727

What OpenQuestion holds

Textmetadata
LicenceTDM
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.