Evidence map›Paper›PMID 30776383›Full record

ArticleJournal of pharmaceutical sciences2019

Developability Assessment of Physicochemical Properties and Stability Profiles of HIV-1 BG505 SOSIP.664 and BG505 SOSIP.v4.1-GT1.1 gp140 Envelope Glycoprotein Trimers as Candidate Vaccine Antigens.

Neal Whitaker, John M Hickey, Kawaljit Kaur, Jian Xiong, Nishant Sawant, Albert Cupo, Wen-Hsin Lee, Gabriel Ozorowski, Max Medina-Ramírez, Andrew B Ward and 5 more

Open access · hybridAbstract read
In one paragraph

Article in Journal of pharmaceutical sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

15 citing papers in PubMed, 21 citations in OpenAlex.

  1. Under the Radar: Immune Evasion, Pathogenesis and Control of HIV Infection.International journal of molecular sciences · 2025
    Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Development of a RPLC-UV method for monitoring uncleaved HIV-1 envelope glycoprotein.Analytical methods : advancing methods and applications · 2021
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Innovations in HIV-1 Vaccine Design.Clinical therapeutics · 2020
    Review
  12. Article
  13. Review
  14. Article
  15. 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

15 authors at 5 institutions in 2 countries.

Neal WhitakerDepartment of Pharmaceutical Chemistry, Macromolecule and Vaccine Stabilization Center, University of Kansas, Lawrence, Kansas 66047.
John M HickeyDepartment of Pharmaceutical Chemistry, Macromolecule and Vaccine Stabilization Center, University of Kansas, Lawrence, Kansas 66047.
Kawaljit KaurDepartment of Pharmaceutical Chemistry, Macromolecule and Vaccine Stabilization Center, University of Kansas, Lawrence, Kansas 66047.
Jian XiongDepartment of Pharmaceutical Chemistry, Macromolecule and Vaccine Stabilization Center, University of Kansas, Lawrence, Kansas 66047.
Nishant SawantDepartment of Pharmaceutical Chemistry, Macromolecule and Vaccine Stabilization Center, University of Kansas, Lawrence, Kansas 66047.
Albert CupoDepartment of Microbiology and Immunology, Weill Medical College of Cornell University, New York, New York 10065.
Wen-Hsin LeeDepartment of Integrative Structural and Computational Biology, Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery, International AIDS Vaccine Initiative Neutralizing Antibody Center, Collaboration for AIDS Vaccine Discovery, The Scripps Research Institute, La Jolla, California 92037.
Gabriel OzorowskiDepartment of Integrative Structural and Computational Biology, Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery, International AIDS Vaccine Initiative Neutralizing Antibody Center, Collaboration for AIDS Vaccine Discovery, The Scripps Research Institute, La Jolla, California 92037.
Max Medina-RamírezDepartment of Medical Microbiology, Academic Medical Center, University of Amsterdam, Amsterdam, the Netherlands.
Andrew B WardDepartment of Integrative Structural and Computational Biology, Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery, International AIDS Vaccine Initiative Neutralizing Antibody Center, Collaboration for AIDS Vaccine Discovery, The Scripps Research Institute, La Jolla, California 92037.
Rogier W SandersDepartment of Microbiology and Immunology, Weill Medical College of Cornell University, New York, New York 10065; Department of Medical Microbiology, Academic Medical Center, University of Amsterdam, Amsterdam, the Netherlands.
John P MooreDepartment of Microbiology and Immunology, Weill Medical College of Cornell University, New York, New York 10065.
Sangeeta B JoshiDepartment of Pharmaceutical Chemistry, Macromolecule and Vaccine Stabilization Center, University of Kansas, Lawrence, Kansas 66047.
David B VolkinDepartment of Pharmaceutical Chemistry, Macromolecule and Vaccine Stabilization Center, University of Kansas, Lawrence, Kansas 66047. Electronic address: volkin@ku.edu.
Antu K DeyProduct Development Center, International AIDS Vaccine Initiative, New York, New York 10004. Electronic address: adey@iavi.org.
University of Kansas · USAcademic Medical Center · NLCornell University · USInternational AIDS Vaccine Initiative · USScripps Research Institute · US

Funding

Structural studies of native-like SOSIP trimersP01AI110657 · NIAID · WEILL MEDICAL COLL OF CORNELL UNIV · PI MOORE, JOHN P · 2015 to 2024
$35.4M
NIAID NIH HHS P01 AI110657
6 · The paper itself

Abstract

The induction of broadly neutralizing antibodies (bNAbs) is a major goal in the development of an effective vaccine against HIV-1. A soluble, trimeric, germline (gI) bNAb-targeting variant of the HIV-1 envelope glycoprotein (termed BG505 SOSIP.v4.1-GT1.1 gp140, abbreviated to GT1.1) has recently been developed. Here, we have compared this new immunogen with the parental trimer from which it was derived, BG505 SOSIP.664 gp140. We used a comprehensive suite of biochemical and biophysical methods to determine physicochemical similarities and differences between the 2 trimers, and thereby assessed whether additional formulation development efforts were needed for the GT1.1 vaccine candidate. The overall higher order structure and oligomeric states of the 2 vaccine antigens were quite similar, as were their thermal, chemical, and colloidal stability profiles, as evaluated during accelerated stability studies. Overall, we conclude that the primary sequence changes made to create the gl bNAb-targeting GT1.1 trimer did not detrimentally affect its physicochemical properties or stability profiles from a pharmaceutical perspective. This developability assessment of the BG505 GT1.1 vaccine antigen supports using the formulation and storage conditions previously identified for the parental SOSIP.664 trimer and enables the development of GT1.1 for phase I clinical studies.

Indexed as

Antibodies, NeutralizingAntigens, Viralenv Gene Products, Human Immunodeficiency VirusEpitopesGlycoproteinsHIV-1HIV AntibodiesHumansProtein MultimerizationAntibodies, NeutralizingAntigens, Viralenv Gene Products, Human Immunodeficiency VirusEpitopesGlycoproteinsGP 140HIV AntibodiesBG505developability assessmentformulationgp140HIV-1 Envstabilitytrimersvaccine

Identifiers

PMID30776383
PMCPMC6595180
OpenAlexW2913184223

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.