Evidence map›Paper›PMID 33688632›Full record

ArticleCurrent research in structural biology2020

One-step sequence and structure-guided optimization of HIV-1 envelope gp140.

Sameer Kumar Malladi, David Schreiber, Ishika Pramanick, Malavika Abhineshababu Sridevi, Adi Goldenzweig, Somnath Dutta, Sarel Jacob Fleishman, Raghavan Varadarajan

Open access · goldAbstract read
In one paragraph

Article in Current research in structural biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

6 citing papers in PubMed, 13 citations in OpenAlex.

  1. One-shot design elevates functional expression levels of a voltage-gated potassium channel.Protein science : a publication of the Protein Society · 2024
    Article
  2. Article
  3. Article
  4. Improving the secretion of designed protein assemblies through negative design of cryptic transmembrane domains.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  5. Review
  6. Harnessing Conformational Plasticity to Generate Designer Enzymes.Journal of the American Chemical Society · 2020
    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

8 authors at 3 institutions in 2 countries.

Sameer Kumar MalladiMolecular Biophysics Unit (MBU), Indian Institute of Science, Bengaluru, India.
David SchreiberDepartment of BioMolecular Sciences, Weizmann Institute of Science, Rehovot, Israel.
Ishika PramanickMolecular Biophysics Unit (MBU), Indian Institute of Science, Bengaluru, India.
Malavika Abhineshababu SrideviMolecular Biophysics Unit (MBU), Indian Institute of Science, Bengaluru, India.
Adi GoldenzweigDepartment of BioMolecular Sciences, Weizmann Institute of Science, Rehovot, Israel.
Somnath DuttaMolecular Biophysics Unit (MBU), Indian Institute of Science, Bengaluru, India.
Sarel Jacob FleishmanDepartment of BioMolecular Sciences, Weizmann Institute of Science, Rehovot, Israel.
Raghavan VaradarajanMolecular Biophysics Unit (MBU), Indian Institute of Science, Bengaluru, India.
Indian Institute of Science Bangalore · INWeizmann Institute of Science · ILJawaharlal Nehru Centre for Advanced Scientific Research · IN

Funding

HIV-1 envelope structure, stability and dynamics probed by saturation mutagenesisR01AI118366 · NIAID · INDIAN INSTITUTE OF SCIENCE · PI VARADARAJAN, RAGHAVAN · 2015 to 2019
$607k
NIAID NIH HHS R01 AI118366
6 · The paper itself

Abstract

Stabilization of the metastable envelope glycoprotein (Env) of HIV-1 is hypothesized to improve induction of broadly neutralizing antibodies. We improved the expression yield and stability of the HIV-1 envelope glycoprotein BG505SOSIP.664 gp140 by means of a previously described automated sequence and structure-guided computational thermostabilization approach, PROSS. This combines sequence conservation information with computational assessment of mutant stabilization, thus taking advantage of the extensive natural sequence variation present in HIV-1 Env. PROSS is used to design three gp140 variants with 17-45 mutations relative to the parental construct. One of the designs is experimentally observed to have a fourfold improvement in yield and a 4 °C increment in thermostability. In addition, the designed immunogens have similar antigenicity profiles to the native flexible linker version of wild type, BG505SOSIP.664 gp140 (NFL Wt) to major epitopes targeted by broadly neutralizing antibodies. PROSS eliminates the laborious process of screening many variants for stability and functionality, providing a proof of principle of the method for stabilization and improvement of yield without compromising antigenicity for next generation complex, highly glycosylated vaccine candidates.

Indexed as

AutomatedImmunogenProtein designProtein stabilityRosettaVaccineVirus

Identifiers

PMID33688632
PMCPMC7939140
OpenAlexW3021975097

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.