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Immunogenicity of a malaria parasite antigen displayed by Lactococcus lactis in oral immunisations

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Ramasamy, R., Yasawardena, S., Zomer, A., Venema, G., Kok, J., Leenhouts, K.·2006·Vaccine
DOI 10.1016/j.vaccine.2006.02.040PMC PMC7115539
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Abstract

A putative protective protein from Plasmodium falciparum merozoites, MSA2, was expressed in two different ways on the cell surface of the Gram-positive food-grade bacterium, Lactococcus lactis. The first display format exploits an LPXTG-type anchoring motif of the lactococcal proteinase PrtP to covalently anchor MSA2 to the genetically modified producer cells. In a second display format, MSA2 was fused to the peptidoglycan-binding domain (Protein Anchor) of the lactococcal cell wall hydrolase AcmA and was non-covalently rebound to the surface of non-genetically modified, non-living high-binder L. lactis cells, termed Gram-positive enhancer matrix (GEM) particles. The L. lactis recombinants carrying covalently bound MSA2 were used to immunise rabbits through nasal and oral routes. The highest levels of IgG antibodies reacting with near-native MSA2 on merozoites was elicited by oral administration. Intestinal antibodies to MSA2 were produced only after oral immunisation. MSA2-specific T(h)-cell activation could be demonstrated. Based on these results, the immunogenicity in oral immunisations of MSA2, bound non-covalently to non-genetically modified L. lactis GEM particles, was compared with MSA2 that was bound covalently to genetically modified L. lactis. These two forms elicited similar titres of serum antibodies. The results illustrate the potential of using non-genetically modified L. lactis as a safe vaccine delivery vehicle to elicit systemic antibodies, thereby avoiding the dissemination of recombinant DNA into the environment.

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  • Fusion of the C-terminal LPXTG containing domain of PrtP with several reporter proteins resulted in the surface exposure of the fusion proteins.

    “Fusion of the C-terminal LPXTG containing domain of PrtP with several reporter proteins resulted in the surface exposure of the fusion proteins [28,29].”

    From Positive role of cell wall anchored proteinase PrtP in adhesion of lactococci (2007) · cites this paper as [28]

    The Materials and methods section describes fusing the PrtP C-terminal anchoring sequence to MSA2, and the Results section confirms that this fusion protein was exposed on the Lactococcus lactis surface. This paper demonstrates the result for MSA2, a malaria antigen, but does not establish it for several reporter proteins. Page numbers are not available in our copy. (LLM, conf=0.88)

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Authors
Ramasamy, R., Yasawardena, S., Zomer, A., Venema, G., Kok, J., & Leenhouts, K.
Affiliations
  • National Science Foundation of Sri Lanka (LK)
  • National Institute of Fundamental Studies (LK)
  • University of Groningen (NL)
Corresponding author
Leenhouts, K.
ORCID
Venue
Vaccine
Publisher
Elsevier BV
Published
2006-05
Volume
24
Issue
18
Pages
3900-3908
ISSN
0264-410X (ISSN-L)
DOI
10.1016/j.vaccine.2006.02.040
PMC
PMC7115539
OpenAlex
W2135685789
Cited by
102
References
37
Citations by year
2025: 2 · 2024: 1 · 2023: 4 · 2022: 2 · 2021: 4 · 2020: 6 · 2019: 8 · 2018: 6 · 2017: 2 · 2016: 5 · 2015: 9 · 2014: 7 · 2013: 7 · 2012: 4
FWCI
9.13
Type
journal article
Language
en
Open access
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Vaccine (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • University of Groningen research database (University of Groningen / Centre for Information Technology) (publishedVersion, other-oa)
  • University of Groningen research database (University of Groningen / Centre for Information Technology) (submittedVersion, other-oa)
Topics
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Probiotics and Fermented Foods
  • Health Sciences › Medicine › Public Health, Environmental and Occupational Health › Malaria Research and Control
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Cancer Research and Treatments
Keywords
malaria vaccine, Plasmodium falciparum, Lactococcus lactis, oral immunization, PrtP, ACMA, peptidoglycan-binding domain, merozoites, IgG
MeSH terms
Administration, Intranasal, Administration, Oral, Animals, Antibodies, Protozoan, Antigens, Protozoan, Antigens, Surface, Feces, Immunoglobulin G, Muramidase, Plasmodium falciparum, Rabbits, Recombinant Fusion Proteins, Lactococcus lactis, T-Lymphocytes, Vaccines, Synthetic, Protozoan Proteins, Microscopy, Immunoelectron, Malaria Vaccines, Fluorescent Antibody Technique, Indirect, Protein Sorting Signals, Models, Animal, Organisms, Genetically Modified

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