Erratum to: Protection against human papillomavirus type 16-induced tumors in mice using non-genetically modified lactic acid bacteria displaying E7 antigen at its surface

Ribelles, Pedro; Benbouziane, Bouasria; Langella, Philippe; Súarez, Juan E.; Bermúdez‐Humarán, Luis G.

doi:10.1007/s00253-012-4662-3

Appl Microbiol Biotechnol

2013

DOI: 10.1007/s00253-012-4662-3

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Erratum to: Protection against human papillomavirus type 16-induced tumors in mice using non-genetically modified lactic acid bacteria displaying E7 antigen at its surface

Pedro Ribelles

Bouasria Benbouziane

Philippe Langella

et al.

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Cited by 3 publications

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confidence: 99%

“…Lactic acid bacteria (LAB) have been used to develop surface display systems based on phage endolysins , Ribelles et al, 2013 in large part due to their GRAS status (generally recognized as safe), which makes them more readily accepted in medical and food applications than other bacteria. Regarding the application of these systems, recently, Ribelles et al (2013) Endolysins have also been used to produce empty 'ghost' bacteria to be developed into vaccines. These bacterial 'ghosts' are produced by the controlled expression of phage PhiX174 lysis gene E. E-mediated lysis of bacteria outcomes in the formation of empty bacterial cell envelopes with essentially the same cell surface composition as their living counterparts (Eko et al, 1999;Haidinger et al, 2003).…”

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Phage lytic proteins: biotechnological applications beyond clinical antimicrobials

Rodríguez-Rubio

Gutiérrez

Donovan

et al. 2015

Critical Reviews in Biotechnology

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Most bacteriophages encode two types of cell wall lytic proteins: endolysins (lysins) and virion-associated peptidoglycan hydrolases. Both enzymes have the ability to degrade the peptidoglycan of Gram positive bacteria resulting in cell lysis when they are applied externally. Bacteriophage lytic proteins have a demonstrated potential in treating animal models of infectious diseases. There has also been an increase in the study of these lytic proteins for their application in areas such as food safety, pathogen detection/diagnosis, surfaces disinfection, vaccine development and nanotechnology.This review summarizes the more recent developments, outlines the full potential of these proteins to develop new biotechnological tools and discusses the feasibility of these proposals.3

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confidence: 99%

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confidence: 99%

Phage lytic proteins: biotechnological applications beyond clinical antimicrobials

Rodríguez-Rubio

Gutiérrez

Donovan

et al. 2015

Critical Reviews in Biotechnology

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Surface display of glycosylated Tyrosinase related protein-2 (TRP-2) tumour antigen on Lactococcus lactis

et al. 2015

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BackgroundThe exploitation of the surface display system of food and commensal lactic acid bacteria (LAB) for bacterial, viral, or protozoan antigen delivery has received strong interest recently. The Generally Regarded as Safe (GRAS) status of the Lactococcus lactis coupled with a non-recombinant strategy of in-trans surface display, provide a safe platform for therapeutic drug and vaccine development. However, production of therapeutic proteins fused with cell-wall anchoring motifs is predominantly limited to prokaryotic expression systems. This presents a major disadvantage in the surface display system particularly when glycosylation has been recently identified to significantly enhance epitope presentation. In this study, the glycosylated murine Tyrosinase related protein-2 (TRP-2) with the ability to anchor onto the L. lactis cell wall was produced in suspension adapted Chinese Hamster Ovary (CHO-S) cells by expressing TRP-2 fused with cell wall anchoring LysM motif (cA) at the C-terminus.ResultsA total amount of 33 μg of partially purified TRP-2-cA from ~6.0 g in wet weight of CHO-S cells was purified by His-tag affinity chromatography. The purified TRP-2-cA protein was shown to be N-glycosylated and successfully anchored to the L. lactis cell wall.ConclusionsThus cell surface presentation of glycosylated mammalian antigens may now permit development of novel and inexpensive vaccine platforms.

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Phage-Encoded Endolysins

Easwaran²,

et al. 2021

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Due to the global emergence of antibiotic resistance, there has been an increase in research surrounding endolysins as an alternative therapeutic. Endolysins are phage-encoded enzymes, utilized by mature phage virions to hydrolyze the cell wall from within. There is significant evidence that proves the ability of endolysins to degrade the peptidoglycan externally without the assistance of phage. Thus, their incorporation in therapeutic strategies has opened new options for therapeutic application against bacterial infections in the human and veterinary sectors, as well as within the agricultural and biotechnology sectors. While endolysins show promising results within the laboratory, it is important to document their resistance, safety, and immunogenicity for in-vivo application. This review aims to provide new insights into the synergy between endolysins and antibiotics, as well as the formulation of endolysins. Thus, it provides crucial information for clinical trials involving endolysins.

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Erratum to: Protection against human papillomavirus type 16-induced tumors in mice using non-genetically modified lactic acid bacteria displaying E7 antigen at its surface

Cited by 3 publications

References 0 publications

Phage lytic proteins: biotechnological applications beyond clinical antimicrobials

Phage lytic proteins: biotechnological applications beyond clinical antimicrobials

Surface display of glycosylated Tyrosinase related protein-2 (TRP-2) tumour antigen on Lactococcus lactis

Phage-Encoded Endolysins

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