Evidence map›Paper›PMID 25760931›Full record

ReviewCurrent opinion in HIV and AIDS2015

Antibody engineering for increased potency, breadth and half-life.

Stuart A Sievers, Louise Scharf, Anthony P West, Pamela J Bjorkman

Abstract readReview
In one paragraph

Review in Current opinion in HIV and AIDS, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
–field-weighted citation impact
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

38 citing papers in PubMed.

  1. Trial
  2. Article
  3. Review
  4. Bispecific antibodies against the hepatitis C virus E1E2 envelope glycoprotein.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. The reduced form of the antibody CH2 domain.Protein science : a publication of the Protein Society · 2021
    Article
  15. Therapeutic potential of HIV-1 entry inhibitor peptidomimetics.Experimental biology and medicine (Maywood, N.J.) · 2021
    Review
  16. Article
  17. Review
  18. Article
  19. Review
  20. 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.

Stuart A SieversaDivision of Biology and Biological Engineering, California Institute of Technology, 1200 East California Boulevard, Pasadena, CA 91125, USA bHoward Hughes Medical Institute, Chevy Chase, MD 20815-6789, USA.
Louise Scharf
Anthony P West
Pamela J Bjorkman

Funding

Stuctural basis of bNab activityP01AI100148 · NIAID · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI Pamela J Bjorkman · 2013 to 2026
$43.3M
Thwarting HIV evasion of antibody avidity with novel antibody architecturesDP1OD006961 · OD · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI BJORKMAN, PAMELA J · 2010 to 2012
$1.7M
NIAID NIH HHS P01 AI100148NIH HHS DP1 OD006961NIH HHS DP1OD006961
6 · The paper itself

Abstract

purpose of reviewThis review highlights recent developments in HIV-1 antibody engineering and discusses the effects of increased polyreactivity on serum half-lives of engineered antibodies. RECENT

findingsRecent studies have uncovered a wealth of information about the relationship between the sequences and efficacies of anti-HIV-1 antibodies through a combination of bioinformatics, structural characterization and in vivo studies. This knowledge has stimulated efforts to enhance antibody breadth and potency for therapeutic use. Although some engineered antibodies have shown increased polyreactivity and short half-lives, promising efforts are circumventing these problems. SUMMARY: Antibodies are desirable as therapeutics due to their ability to recognize targets with both specificity and high affinity. Furthermore, the ability of antibodies to stimulate Fc-mediated effector functions can increase their utility. Thus, mAbs have become central to strategies for the treatment of various diseases. Using both targeted and library-based approaches, antibodies can be engineered to improve their therapeutic properties. This article will discuss recent antibody engineering efforts to improve the breadth and potency of anti-HIV-1 antibodies. The polyreactivity of engineered HIV-1 bNAbs and the effect on serum half-life will be explored along with strategies to overcome problems introduced by engineering antibodies. Finally, advances in creating bispecific anti-HIV-1 reagents are discussed.

Indexed as

Antibodies, BispecificHIV AntibodiesAnimalsBinding SitesHumansMiceModels, MolecularProtein EngineeringAntibodies, BispecificHIV Antibodies

Identifiers

PMID25760931
PMCPMC4465343

What OpenQuestion holds

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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.