Mucosal vaccine delivery of antigens tightly bound to an adjuvant particle made from food-grade bacteria

Roosmalen, Maarten L. van; Kanninga, Rolf; Khattabi, Mohamed El; Neef, Jolanda; Audouy, Sandrine; Bosma, Tjibbe; Kuipers, Anneke; Post, Eduard; Steen, Anton; Kok, Jan; Buist, Girbe; Kuipers, Oscar P.; Robillard, George T.; Leenhouts, Kees

doi:10.1016/j.ymeth.2005.09.015

Cited by 106 publications

(105 citation statements)

References 31 publications

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“…41,42 GEM particles were made from non-living L. lactis cells (cells were treated with a 1M hot acid solution for 30 min and washed thoroughly with PBS) free of DNA and cytoplasmic material that retained their bacterial size and surface display of antigens of the original bacterial cells. Heterologous antigens were anchored to the GEM particles by means of a lactococcal peptidoglycan binding domain called the protein anchor (PA).…”

Section: Lactococcus Lactis Nasally Administered As An Adjuvant and Dmentioning

confidence: 99%

Lactococcus lactisas an adjuvant and delivery vehicle of antigens against pneumococcal respiratory infections

et al. 2010

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Section: Lactococcus Lactis Nasally Administered As An Adjuvant and Dmentioning

confidence: 99%

Lactococcus lactisas an adjuvant and delivery vehicle of antigens against pneumococcal respiratory infections

et al. 2010

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“…Construction of the plasmids is described elsewhere (Audouy, manuscript in preparation). Lactococcal GEM particles were produced as described before [20,21]. Culture supernatants containing the fusion recombinant proteins were concentrated with a VivaFlow (Vivascience VivaFlow200, 10,000 Da cut-off).…”

Section: Vaccine Preparationmentioning

confidence: 99%

“…In order to develop a safe and affordable mucosal vaccine delivery system we used a system that exploits killed non-recombinant L. lactis particles obtained by chemical pretreatment of whole bacteria with hot acid [19,20] (van Roosmalen et al, in press). These particles are referred to as Gram-positive enhancer matrix (GEM) and they constitute mainly of bacterial shaped peptidoglycan spheres that lack other intact cell wall components and intracellular material.…”

Section: Introductionmentioning

confidence: 99%

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Lactococcus lactis GEM particles displaying pneumococcal antigens induce local and systemic immune responses following intranasal immunization

Audouy¹,

Roosmalen²,

Neef³

et al. 2006

Vaccine

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Take-down policy If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim.Downloaded from the University of Groningen/UMCG research database (Pure): http://www.rug.nl/research/portal. For technical reasons the number of authors shown on this cover page is limited to 10 maximum. AbstractThe present work reports the use of non-living non-recombinant bacteria as a delivery system for mucosal vaccination. Antigens are bound to the cell-wall of pretreated Lactococcus lactis, designated as Gram-positive enhancer matrix (GEM), by means of a peptidoglycan binding domain. The influence of the GEM particles on the antigen-specific serum antibody response was studied. Following nasal immunization with the GEM-based vaccines, antibody responses were induced at systemic and local levels. Furthermore, different GEM-based vaccines could be used consecutively in the same mice without adverse effects or loss of activity. Taken together, the results evidence the adjuvant properties of the GEM particles and indicate that GEM-based vaccines can be used repeatedly and are particularly suitable for nasal immunization purposes.

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“…However, heterologous proteins have been anchored to the producer cells, and the use of genetically modified organisms is less desirable or at least still being debated. Surface display of heterologous proteins on genetically unmodified Gram-positive bacteria has been successfully carried out using the peptidoglycan binding lysin motif (LysM) domain of the major autolysin AcmA of Lactococcus lactis (1,2,4,18,28).…”

mentioning

confidence: 99%

Characterization of a Novel LysM Domain from Lactobacillus fermentum Bacteriophage Endolysin and Its Use as an Anchor To Display Heterologous Proteins on the Surfaces of Lactic Acid Bacteria

Kong

et al. 2010

Appl Environ Microbiol

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The endolysin Lyb5, from Lactobacillus fermentum temperate bacteriophage PYB5, showed a broad lytic spectrum against Gram-positive as well as Gram-negative bacteria. Sequence analysis revealed that the C terminus of the endolysin Lyb5 (Ly5C) contained three putative lysin motif (LysM) repeat regions, implying that Ly5C was involved in bacterial cell wall binding. To investigate the potential of Ly5C for surface display, green fluorescent protein (GFP) was fused to Ly5C at its N or C terminus and the resulting fusion proteins were expressed in Escherichia coli. After being mixed with various cells in vitro, GFP was successfully displayed on the surfaces of Lactococcus lactis, Lactobacillus casei, Lb. brevis, Lb. plantarum, Lb. fermentum, Lb. delbrueckii, Lb. helveticus, and Streptococcus thermophilus cells. Increases in the fluorescence intensities of chemically pretreated L. lactis and Lb. casei cells compared to those of nonpretreated cells suggested that the peptidoglycan was the binding ligand for Ly5C. Moreover, the pH and concentration of sodium chloride were optimized to enhance the binding capacity of GFP-Ly5C, and high-intensity fluorescence of cells was observed under optimal conditions. All results suggested that Ly5C was a novel anchor for constructing a surface display system for lactic acid bacteria (LAB). To demonstrate the applicability of the Ly5C-mediated surface display system, ␤-galactosidase (␤-Gal) from Paenibacillus sp. strain K1, replacing GFP, was functionally displayed on the surfaces of LAB cells via Ly5C. The success in surface display of GFP and ␤-Gal opened up the feasibility of employing the cell wall anchor of bacteriophage endolysin for surface display in LAB.

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Mucosal vaccine delivery of antigens tightly bound to an adjuvant particle made from food-grade bacteria

Cited by 106 publications

References 31 publications

Lactococcus lactisas an adjuvant and delivery vehicle of antigens against pneumococcal respiratory infections

Lactococcus lactisas an adjuvant and delivery vehicle of antigens against pneumococcal respiratory infections

Lactococcus lactis GEM particles displaying pneumococcal antigens induce local and systemic immune responses following intranasal immunization

Characterization of a Novel LysM Domain from Lactobacillus fermentum Bacteriophage Endolysin and Its Use as an Anchor To Display Heterologous Proteins on the Surfaces of Lactic Acid Bacteria

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