Evidence map›Paper›PMID 21550371›Full record

ArticleVaccine2011

Amphipols stabilize the Chlamydia major outer membrane protein and enhance its protective ability as a vaccine.

Delia F Tifrea, Guifeng Sun, Sukumar Pal, Gustavo Zardeneta, Melanie J Cocco, Jean-Luc Popot, Luis M de la Maza

Abstract read
In one paragraph

Article in Vaccine, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

37 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. A potent novel vaccine adjuvant based on straight polyacrylate.International journal of pharmaceutics: X · 2020
    Article
  10. Article
  11. Article
  12. Article
  13. Seventy Years ofFrontiers in microbiology · 2019
    Review
  14. Article
  15. Article
  16. Article
  17. TheFrontiers in immunology · 2018
    Article
  18. Article
  19. Article
  20. Cell-free production of a functional oligomeric form of aThe Journal of biological chemistry · 2017
    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

7 authors at 2 institutions in 2 countries.

Delia F TifreaDepartment of Pathology and Laboratory Medicine, Medical Sciences I, Room D440, University of California, Irvine, Irvine, CA 92697-4800, USA.
Guifeng Sun
Sukumar Pal
Gustavo Zardeneta
Melanie J Cocco
Jean-Luc Popot
Luis M de la Maza
University of California, Irvine · USInstitut de Biologie Physico-Chimique · FR

Funding

IMMUNOPATHOLOGY OF TUBAL INFERTILITYR01AI032248 · NIAID · UNIVERSITY OF CALIFORNIA-IRVINE · PI DE LA MAZA, LUIS M · 1993 to 2007
$2.6M
Recombinant C. trachomatis vaccineR01AI067888 · NIAID · UNIVERSITY OF CALIFORNIA-IRVINE · PI DE LA MAZA, LUIS M · 2007 to 2011
$1.9M
NIAID NIH HHS AI-32248NIAID NIH HHS AI-67888NIAID NIH HHS R01 AI032248NIAID NIH HHS R01 AI067888
6 · The paper itself

Abstract

The native major outer membrane protein (nMOMP) from Chlamydia was purified in its trimeric form using the zwitterionic detergent Z3-14. In aliquots from this preparation, Z3-14 was exchanged for amphipol (APol) A8-35. CD analysis showed that trapping with A8-35 improved the thermostability of nMOMP without affecting its secondary structure. Recombinant MOMP (rMOMP) was also formulated with Z3-14 or A8-35. Four groups of mice were vaccinated with nMOMP/Z3-14, nMOMP/A8-35, rMOMP/Z3-14 or rMOMP/A8-35 using CpG and Montanide as adjuvants. A positive control group was inoculated intranasally with live Chlamydia and a negative control group with culture medium. Mice were challenged intranasally with live Chlamydia and protection was assessed based on changes in body weight, the weight of the lungs and the number of chlamydial inclusion forming units recovered from the lungs 10 days after the challenge. Overall, vaccines formulated with nMOMP elicited better protection than those using rMOMP. Furthermore, the protection afforded by nMOMP/A8-35 was more robust than that achieved with nMOMP/Z3-14. In contrast, no differences in protection were observed between rMOMP/Z3-14 and rMOMP/A8-35 preparations. These findings suggest that the higher protection conferred by nMOMP/A8-35 complexes most likely results from a better preservation of the native structure of MOMP and/or from a more efficient presentation of the antigen to the immune system, rather than from an adjuvant effect of the amphipol. Thus, amphipols can be used in vaccine formulations to stabilize a membrane-protein component and enhance its immunogenicity.

Indexed as

AnimalsAntibodies, BacterialBacterial Outer Membrane ProteinsBacterial VaccinesChlamydia InfectionsChlamydia trachomatisCircular DichroismDetergentsFemaleLungMiceMice, Inbred BALB CPolymersPropylaminesProtein StabilityProtein Structure, Secondaryamphipol A8-35Antibodies, BacterialBacterial Outer Membrane ProteinsBacterial VaccinesDetergentsPolymersPropylaminesRecombinant Proteins

Identifiers

PMID21550371
PMCPMC3114171
OpenAlexW2129269993

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.