Evidence map›Paper›PMID 17242138›Full record

ArticleAntimicrobial agents and chemotherapy2007

The second extracellular loop of CCR5 contains the dominant epitopes for highly potent anti-human immunodeficiency virus monoclonal antibodies.

Jun Zhang, Eileen Rao, Marianna Dioszegi, Rama Kondru, Andre DeRosier, Eva Chan, Stephan Schwoerer, Nick Cammack, Michael Brandt, Surya Sankuratri and 1 more

Open access · greenAbstract read
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2007. 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
0.9field-weighted citation impact, top 30% 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, 24 citations in OpenAlex.

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  11. Natural anti-CCR5 antibodies in HIV-infection and -exposure.Journal of translational medicine · 2011
    Review
  12. Article
  13. Atomic-level mapping of antibody epitopes on a GPCR.Journal of the American Chemical Society · 2009
    Article
  14. CCR5 monoclonal antibodies for HIV-1 therapy.Current opinion in HIV and AIDS · 2009
    Review
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

11 authors at 2 institutions in 1 country.

Jun ZhangViral Diseases, Roche Palo Alto, 3431 Hillview Avenue, Palo Alto, CA 94304, USA.
Eileen Rao
Marianna Dioszegi
Rama Kondru
Andre DeRosier
Eva Chan
Stephan Schwoerer
Nick Cammack
Michael Brandt
Surya Sankuratri
Changhua Ji
Global Viral · USRoche (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Six mouse anti-human CCR5 monoclonal antibodies (mAbs) that showed potent antiviral activities were identified from over 26,000 mouse hybridomas. The epitopes for these mAbs were determined by using various CCR5 mutants, including CCR5/CCR2B chimeras. One mAb, ROAb13, was found to bind to a linear epitope in the N terminus of CCR5. Strikingly, the other five mAbs bind to epitopes derived from extracellular loop 2 (ECL2). The three most potent mAbs, ROAb12, ROAb14, and ROAb18, require residues from both the N-terminal (Lys171 and Glu172) and C-terminal (Trp190) halves of ECL2 for binding; two other mAbs, ROAb10 and ROAb51, which also showed potent antiviral activities, require Lys171 and Glu172 but not Trp190 for binding. Binding of the control mAb 2D7 completely relies on Lys171 and Glu172. Unlike 2D7, the novel mAbs ROAb12, ROAb14, and ROAb18 do not bind to the linear peptide 2D7-2SK. In addition, all three mAbs bind to monkey CCR5 (with Arg at position 171 instead of Lys); however, 2D7 does not. Since five of the six most potent CCR5 mAbs derived from the same pool of immunized mice require ECL2 as epitopes, we hypothesize that CCR5 ECL2 contains the dominant epitopes for mAbs with potent antiviral activities. These dominant epitopes were found in CCR5 from multiple species and were detected in large proportions of the total cell surface CCR5. mAbs recognizing these epitopes also showed high binding affinity. A homology model of CCR5 was generated to aid in the interpretation of these dominant epitopes in ECL2.

Indexed as

CCR5 Receptor AntagonistsAntibodies, MonoclonalEpitope MappingEpitopesHIV-1HIV AntibodiesHumansReceptors, CCR5Structure-Activity RelationshipAntibodies, MonoclonalCCR5 Receptor AntagonistsEpitopesHIV AntibodiesReceptors, CCR5

Identifiers

PMID17242138
PMCPMC1855447
OpenAlexW2097958885

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.