Literature DB >> 28739800

Cell-free production of a functional oligomeric form of a Chlamydia major outer-membrane protein (MOMP) for vaccine development.

Wei He1, Martina Felderman2, Angela C Evans1, Jia Geng1,3, David Homan1, Feliza Bourguet1, Nicholas O Fischer1, Yuanpei Li4, Kit S Lam4, Aleksandr Noy1,3, Li Xing5, R Holland Cheng5, Amy Rasley1, Craig D Blanchette1, Kurt Kamrud2, Nathaniel Wang2, Heather Gouvis2, Todd C Peterson2, Bolyn Hubby2, Matthew A Coleman6,7.   

Abstract

Chlamydia is a prevalent sexually transmitted disease that infects more than 100 million people worldwide. Although most individuals infected with Chlamydia trachomatis are initially asymptomatic, symptoms can arise if left undiagnosed. Long-term infection can result in debilitating conditions such as pelvic inflammatory disease, infertility, and blindness. Chlamydia infection, therefore, constitutes a significant public health threat, underscoring the need for a Chlamydia-specific vaccine. Chlamydia strains express a major outer-membrane protein (MOMP) that has been shown to be an effective vaccine antigen. However, approaches to produce a functional recombinant MOMP protein for vaccine development are limited by poor solubility, low yield, and protein misfolding. Here, we used an Escherichia coli-based cell-free system to express a MOMP protein from the mouse-specific species Chlamydia muridarum (MoPn-MOMP or mMOMP). The codon-optimized mMOMP gene was co-translated with Δ49apolipoprotein A1 (Δ49ApoA1), a truncated version of mouse ApoA1 in which the N-terminal 49 amino acids were removed. This co-translation process produced mMOMP supported within a telodendrimer nanolipoprotein particle (mMOMP-tNLP). The cell-free expressed mMOMP-tNLPs contain mMOMP multimers similar to the native MOMP protein. This cell-free process produced on average 1.5 mg of purified, water-soluble mMOMP-tNLP complex in a 1-ml cell-free reaction. The mMOMP-tNLP particle also accommodated the co-localization of CpG oligodeoxynucleotide 1826, a single-stranded synthetic DNA adjuvant, eliciting an enhanced humoral immune response in vaccinated mice. Using our mMOMP-tNLP formulation, we demonstrate a unique approach to solubilizing and administering membrane-bound proteins for future vaccine development. This method can be applied to other previously difficult-to-obtain antigens while maintaining full functionality and immunogenicity.

Entities:  

Keywords:  Chlamydia; apolipoprotein; cell-free expression; major outer membrane protein; membrane protein; nanolipoproteins; nanotechnology; oligomer; telodendrimer

Mesh:

Substances:

Year:  2017        PMID: 28739800      PMCID: PMC5592686          DOI: 10.1074/jbc.M117.784561

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  60 in total

Review 1.  Molecular basis of bacterial outer membrane permeability revisited.

Authors:  Hiroshi Nikaido
Journal:  Microbiol Mol Biol Rev       Date:  2003-12       Impact factor: 11.056

2.  Cell-free co-expression of functional membrane proteins and apolipoprotein, forming soluble nanolipoprotein particles.

Authors:  Jenny A Cappuccio; Craig D Blanchette; Todd A Sulchek; Erin S Arroyo; Joel M Kralj; Angela K Hinz; Edward A Kuhn; Brett A Chromy; Brent W Segelke; Kenneth J Rothschild; Julia E Fletcher; Federico Katzen; Todd C Peterson; Wieslaw A Kudlicki; Graham Bench; Paul D Hoeprich; Matthew A Coleman
Journal:  Mol Cell Proteomics       Date:  2008-07-04       Impact factor: 5.911

3.  Stability of trimeric OmpF porin: the contributions of the latching loop L2.

Authors:  P S Phale; A Philippsen; T Kiefhaber; R Koebnik; V P Phale; T Schirmer; J P Rosenbusch
Journal:  Biochemistry       Date:  1998-11-10       Impact factor: 3.162

4.  Three dimensional structure of the anthrax toxin translocon-lethal factor complex by cryo-electron microscopy.

Authors:  E P Gogol; N Akkaladevi; L Szerszen; S Mukherjee; L Chollet-Hinton; H Katayama; B L Pentelute; R J Collier; M T Fisher
Journal:  Protein Sci       Date:  2013-03-18       Impact factor: 6.725

5.  Immunization with the Chlamydia trachomatis mouse pneumonitis major outer membrane protein can elicit a protective immune response against a genital challenge.

Authors:  S Pal; I Theodor; E M Peterson; L M de la Maza
Journal:  Infect Immun       Date:  2001-10       Impact factor: 3.441

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

Authors:  Delia F Tifrea; Guifeng Sun; Sukumar Pal; Gustavo Zardeneta; Melanie J Cocco; Jean-Luc Popot; Luis M de la Maza
Journal:  Vaccine       Date:  2011-05-06       Impact factor: 3.641

7.  Immobilization of His-tagged proteins on nickel-chelating nanolipoprotein particles.

Authors:  Nicholas O Fischer; Craig D Blanchette; Brett A Chromy; Edward A Kuhn; Brent W Segelke; Michele Corzett; Graham Bench; Peter W Mason; Paul D Hoeprich
Journal:  Bioconjug Chem       Date:  2009-03-18       Impact factor: 4.774

8.  Discoidal complexes of A and C apolipoproteins with lipids and their reactions with lecithin: cholesterol acyltransferase.

Authors:  A Jonas; S A Sweeny; P N Herbert
Journal:  J Biol Chem       Date:  1984-05-25       Impact factor: 5.157

Review 9.  Development status and future prospects for a vaccine against Chlamydia trachomatis infection.

Authors:  Louise M Hafner; David P Wilson; Peter Timms
Journal:  Vaccine       Date:  2013-08-22       Impact factor: 3.641

10.  Expression and Association of the Yersinia pestis Translocon Proteins, YopB and YopD, Are Facilitated by Nanolipoprotein Particles.

Authors:  Matthew A Coleman; Jenny A Cappuccio; Craig D Blanchette; Tingjuan Gao; Erin S Arroyo; Angela K Hinz; Feliza A Bourguet; Brent Segelke; Paul D Hoeprich; Thomas Huser; Ted A Laurence; Vladimir L Motin; Brett A Chromy
Journal:  PLoS One       Date:  2016-03-25       Impact factor: 3.240

View more
  15 in total

1.  Chlamydia-Specific IgA Secretion in the Female Reproductive Tract Induced via Per-Oral Immunization Confers Protection against Primary Chlamydia Challenge.

Authors:  Nita Shillova; Savannah E Howe; Besmir Hyseni; Deahneece Ridgell; Derek J Fisher; Vjollca Konjufca
Journal:  Infect Immun       Date:  2020-12-15       Impact factor: 3.441

2.  Small-angle X-ray and neutron scattering demonstrates that cell-free expression produces properly formed disc-shaped nanolipoprotein particles.

Authors:  Thomas E Cleveland; Wei He; Angela C Evans; Nicholas O Fischer; Edmond Y Lau; Matthew A Coleman; Paul Butler
Journal:  Protein Sci       Date:  2018-02-13       Impact factor: 6.725

3.  Overexpression of the Bam Complex Improves the Production of Chlamydia trachomatis MOMP in the E. coli Outer Membrane.

Authors:  Dung T Huynh; Wouter S P Jong; Gregory M Koningstein; Peter van Ulsen; Joen Luirink
Journal:  Int J Mol Sci       Date:  2022-07-02       Impact factor: 6.208

4.  Epitope-Based Vaccines against the Chlamydia trachomatis Major Outer Membrane Protein Variable Domain 4 Elicit Protection in Mice.

Authors:  Amanda L Collar; Alexandria C Linville; Susan B Core; Kathryn M Frietze
Journal:  Vaccines (Basel)       Date:  2022-05-30

5.  Cell-free Scaled Production and Adjuvant Addition to a Recombinant Major Outer Membrane Protein from Chlamydia muridarum for Vaccine Development.

Authors:  Sean F Gilmore; Wei He; Angela C Evans; Delia F Tifrea; Sukumar Pal; Brent Segelke; Sandra K G Peters; B Dillon Vannest; Nicholas O Fischer; Amy Rasley; Luis M de la Maza; Matthew A Coleman
Journal:  J Vis Exp       Date:  2022-03-16       Impact factor: 1.424

6.  Cell-free expression of the outer membrane protein OprF of Pseudomonas aeruginosa for vaccine purposes.

Authors:  Géraldine Mayeux; Landry Gayet; Lavinia Liguori; Marine Odier; Donald K Martin; Sandra Cortès; Béatrice Schaack; Jean-Luc Lenormand
Journal:  Life Sci Alliance       Date:  2021-05-10

7.  High-yield production of "difficult-to-express" proteins in a continuous exchange cell-free system based on CHO cell lysates.

Authors:  Lena Thoring; Srujan K Dondapati; Marlitt Stech; Doreen A Wüstenhagen; Stefan Kubick
Journal:  Sci Rep       Date:  2017-09-15       Impact factor: 4.379

Review 8.  Cell-Free Co-Translational Approaches for Producing Mammalian Receptors: Expanding the Cell-Free Expression Toolbox Using Nanolipoproteins.

Authors:  Megan L Shelby; Wei He; Amanda T Dang; Tonya L Kuhl; Matthew A Coleman
Journal:  Front Pharmacol       Date:  2019-07-03       Impact factor: 5.810

Review 9.  Telodendrimers: Promising Architectural Polymers for Drug Delivery.

Authors:  Søren Mejlsøe; Ashok Kakkar
Journal:  Molecules       Date:  2020-09-02       Impact factor: 4.411

Review 10.  Cell-Free Protein Synthesis: A Promising Option for Future Drug Development.

Authors:  Srujan Kumar Dondapati; Marlitt Stech; Anne Zemella; Stefan Kubick
Journal:  BioDrugs       Date:  2020-06       Impact factor: 5.807

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.