Oral immunization with live Lactococcus lactis expressing rotavirus VP8* subunit induces specific immune response in mice

Marelli, Belkis Ester; Pérez, Ana Rosa; Banchio, Claudia; Mendoza, Diego de; Magni, Christian

doi:10.1016/j.jviromet.2011.04.011

Cited by 62 publications

(38 citation statements)

References 40 publications

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“…It has been shown that L. lactis with surface displayed rotavirus VP8 antigen using the M6 cell wall anchor, induced secretion of antigen specific antibodies in mice, both in the intestine and at the systemic level. L. lactis producing VP8* intracellularly induced only mucosal secretion of IgA [103], suggesting that surface exposed localization of the antigen is most efficient. In another study, it was shown that L. lactis strain secreting VP7 elicited production of neutralizing antibodies after oral administration of the recombinant bacteria to mice.…”

Section: Lab Displaying Antigensmentioning

confidence: 99%

Display of recombinant proteins at the surface of lactic acid bacteria: strategies and applications

et al. 2016

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Lactic acid bacteria (LAB) are promising vectors of choice to deliver active molecules to mucosal tissues. They are recognized as safe by the World Health Organization and some strains have probiotic properties. The wide range of potential applications of LAB-driven mucosal delivery includes control of inflammatory bowel disease, vaccine delivery, and management of auto-immune diseases. Because of this potential, strategies for the display of proteins at the surface of LAB are gaining interest. To display a protein at the surface of LAB, a signal peptide and an anchor domain are necessary. The recombinant protein can be attached to the membrane layer, using a transmembrane anchor or a lipoprotein-anchor, or to the cell wall, by a covalent link using sortase mediated anchoring via the LPXTG motif, or by non-covalent liaisons employing binding domains such as LysM or WxL. Both the stability and functionality of the displayed proteins will be affected by the kind of anchor used. The most commonly surfaced exposed recombinant proteins produced in LAB are antigens and antibodies and the most commonly used LAB are lactococci and lactobacilli. Although it is not necessarily so that surface-display is the preferred localization in all cases, it has been shown that for certain applications, such as delivery of the human papillomavirus E7 antigen, surface-display elicits better biological responses, compared to cytosolic expression or secretion. Recent developments include the display of peptides and proteins targeting host cell receptors, for the purpose of enhancing the interactions between LAB and host. Surface-display technologies have other potential applications, such as degradation of biomass, which is of importance for some potential industrial applications of LAB.

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Section: Lab Displaying Antigensmentioning

confidence: 99%

Display of recombinant proteins at the surface of lactic acid bacteria: strategies and applications

et al. 2016

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“…Oral administration of recombinant LL expressing bovine β -lactoglobulin (BLG), a major cow's milk allergen, partially prevents BALB/c mice from intranasal BLG-sensitization [31]. The development of a mucosal live vaccine using LL as an antigen vehicle has been reported as an attractive and safe vaccination strategy [32]. Recently, LL strains without genetic modification have been shown to possess Th1/Th2 modulatory activity.…”

Section: Discussionmentioning

confidence: 99%

Immunomodulatory Activity ofLactococcus lactisA17 from Taiwan Fermented Cabbage in OVA-Sensitized BALB/c Mice

Mei

Liu²,

Chiang

et al. 2013

Evidence-Based Complementary and Alternative Medicine

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From fermented Taiwan foods, we have isolated numerous lactic acid bacteria (LAB) of plant origin and investigated their biological activities. This study aimed to investigate the immunomodulatory effect and mechanism of Lactococcus lactis A17 (A17), isolated from Taiwan fermented cabbage, on ovalbumin (OVA)-sensitized mice. Human peripheral blood mononuclear cells were used to verify immune responses of A17 by IFN-γ production. Live (A17-A) and heat-killed A17 (A17-H) were orally administered to OVA-sensitized BALB/c mice to investigate their effects on immunoglobulin (Ig) and cytokine production. The mRNA expression of Toll-like receptors (TLR) and nucleotide binding oligomerization domain (NOD)-like protein receptors in spleen cells was analyzed by real-time RT-PCR. Both live and heat-killed A17 modulate OVA-induced allergic effects. B-cell response was modulated by diminishing IgE production and raising OVA-specific IgG2a production, while T-cell response was modulated by increasing IFN-γ production and decreasing IL-4 production. The mRNA expression of NOD-1, NOD-2, and TLR-4 was down-regulated by A17 as well. This is the first report to describe a naïve Lactococcus lactis A17 strain as a promising candidate for prophylactic and therapeutic treatments of allergic diseases via oral administration. Our results suggest the ameliorative effects of A17 may be caused by modulating NOD-1 NOD-2, and TLR-4 expression.

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“…Rotavirus protein expression in L. lactis was previously reported by Perez et al [8] (VP7 protein), Marelli et al [9], Rodríguez-Díaz et al [10] (VP8* protein), Li et al [11] (VP4 protein), and Enouf et al (NSP4 protein) [12]. However, among rotavirus structural proteins, the intermediate layer protein VP6 is the most immunogenic and determines group specificity since it is highly conserved among strains belonging to the same group [13].…”

Section: Introductionmentioning

confidence: 88%

Antigenicity and Immunogenicity of Rotavirus VP6 Protein Expressed on the Surface ofLactococcus lactis

Esteban

Temprana

Argüelles

et al. 2013

BioMed Research International

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Group A rotaviruses are the major etiologic agents of acute gastroenteritis worldwide in children and young animals. Among its structural proteins, VP6 is the most immunogenic and is highly conserved within this group. Lactococcus lactis is a food-grade, Gram-positive, and nonpathogenic lactic acid bacteria that has already been explored as a mucosal delivery system of heterologous antigens. In this work, the nisin-controlled expression system was used to display the VP6 protein at the cell surface of L. lactis. Conditions for optimal gene expression were established by testing different nisin concentrations, cell density at induction, and incubation times after induction. Cytoplasmic and cell wall protein extracts were analyzed by Western blot and surface expression was confirmed by flow cytometry. Both analysis provided evidence that VP6 was efficiently expressed and displayed on the cell surface of L. lactis. Furthermore, the humoral response of mice immunized with recombinant L. lactis was evaluated and the displayed recombinant VP6 protein proved to be immunogenic. In conclusion, this is the first report of displaying VP6 protein on the surface of L. lactis to induce a specific immune response against rotavirus. These results provide the basis for further evaluation of this VP6-displaying L. lactis as a mucosal delivery vector in a mouse model of rotavirus infection.

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Oral immunization with live Lactococcus lactis expressing rotavirus VP8* subunit induces specific immune response in mice

Cited by 62 publications

References 40 publications

Display of recombinant proteins at the surface of lactic acid bacteria: strategies and applications

Display of recombinant proteins at the surface of lactic acid bacteria: strategies and applications

Immunomodulatory Activity ofLactococcus lactisA17 from Taiwan Fermented Cabbage in OVA-Sensitized BALB/c Mice

Antigenicity and Immunogenicity of Rotavirus VP6 Protein Expressed on the Surface ofLactococcus lactis

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