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1.
FEBS J ; 289(14): 4251-4303, 2022 07.
Article in English | MEDLINE | ID: mdl-33934527

ABSTRACT

Vaccination is one of the greatest achievements in biomedical research preventing death and morbidity in many infectious diseases through the induction of pathogen-specific humoral and cellular immune responses. Currently, no effective vaccines are available for pathogens with a highly variable antigenic load, such as the human immunodeficiency virus or to induce cellular T-cell immunity in the fight against cancer. The recent SARS-CoV-2 outbreak has reinforced the relevance of designing smart therapeutic vaccine modalities to ensure public health. Indeed, academic and private companies have ongoing joint efforts to develop novel vaccine prototypes for this virus. Many pathogens are covered by a dense glycan-coat, which form an attractive target for vaccine development. Moreover, many tumor types are characterized by altered glycosylation profiles that are known as "tumor-associated carbohydrate antigens". Unfortunately, glycans do not provoke a vigorous immune response and generally serve as T-cell-independent antigens, not eliciting protective immunoglobulin G responses nor inducing immunological memory. A close and continuous crosstalk between glycochemists and glycoimmunologists is essential for the successful development of efficient immune modulators. It is clear that this is a key point for the discovery of novel approaches, which could significantly improve our understanding of the immune system. In this review, we discuss the latest advancements in development of vaccines against glycan epitopes to gain selective immune responses and to provide an overview on the role of different immunogenic constructs in improving glycovaccine efficacy.


Subject(s)
COVID-19 , Neoplasms , Vaccines , COVID-19/prevention & control , Glycoconjugates/therapeutic use , Humans , Neoplasms/prevention & control , Polysaccharides/therapeutic use , SARS-CoV-2
2.
FEBS J ; 288(16): 4746-4772, 2021 08.
Article in English | MEDLINE | ID: mdl-33752265

ABSTRACT

Glycan structures are common posttranslational modifications of proteins, which serve multiple important structural roles (for instance in protein folding), but also are crucial participants in cell-cell communications and in the regulation of immune responses. Through the interaction with glycan-binding receptors, glycans are able to affect the activation status of antigen-presenting cells, leading either to induction of pro-inflammatory responses or to suppression of immunity and instigation of immune tolerance. This unique feature of glycans has attracted the interest and spurred collaborations of glyco-chemists and glyco-immunologists to develop glycan-based tools as potential therapeutic approaches in the fight against diseases such as cancer and autoimmune conditions. In this review, we highlight emerging advances in this field, and in particular, we discuss on how glycan-modified conjugates or glycoengineered cells can be employed as targeting devices to direct tumor antigens to lectin receptors on antigen-presenting cells, like dendritic cells. In addition, we address how glycan-based nanoparticles can act as delivery platforms to enhance immune responses. Finally, we discuss some of the latest developments in glycan-based therapies, including chimeric antigen receptor (CAR)-T cells to achieve targeting of tumor-associated glycan-specific epitopes, as well as the use of glycan moieties to suppress ongoing immune responses, especially in the context of autoimmunity.


Subject(s)
Autoimmunity/immunology , Polysaccharides/immunology , Receptors, Chimeric Antigen/immunology , T-Lymphocytes/immunology , Animals , Cell Communication/immunology , Humans , Nanoparticles/chemistry , Polysaccharides/chemistry , Protein Processing, Post-Translational
3.
Methods Mol Biol ; 2021: 217-230, 2019.
Article in English | MEDLINE | ID: mdl-31309508

ABSTRACT

Methods of lipopolysaccharide extraction, purification, and sample validation are presented. Based on serological reaction in ELISA, immunoblotting, and infrared spectra, identities of two LPS preparations from smooth P. mirabilis (O18) PrK 34/57 are presented.


Subject(s)
Antibodies, Bacterial/metabolism , Lipopolysaccharides/isolation & purification , Proteus mirabilis/metabolism , Enzyme-Linked Immunosorbent Assay , Lipopolysaccharides/immunology , Proteus mirabilis/immunology , Serology , Spectrophotometry, Infrared
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