China
Africa
Explore chapters and articles related to this topic
Order Cirlivirales
Published in Paul Pumpens, Peter Pushko, Philippe Le Mercier, Virus-Like Particles, 2022
Paul Pumpens, Peter Pushko, Philippe Le Mercier
Li X et al. (2018) developed a bivalent PCV2 and FMDV vaccine candidate based on the chimeric E. coli-produced PCV2 Cap VLPs. Thus, the neutralizing FMDV B cell epitope region 135–160 replaced the regions aa 123–151 and aa 169–194 of the PCV2b Cap. The chimeric protein was expressed in E. coli and the purified product assembled into the VLPs through dialysis. The chimeric VLPs induced effective immune response against both FMDV and PCV2b in mice and guinea pigs, without inducing antibodies against the PCV2 decoy epitope (Li X et al. 2018).
EML4-ALK Fusion Gene and Therapy with ALK-Targeted Agents in Non-Small Cell Lung Cancer
Published in Sherry X. Yang, Janet E. Dancey, Handbook of Therapeutic Biomarkers in Cancer, 2021
Francisco E. Vera-Badillo, Janet E. Dancey
In 2007, Soda and colleagues identified a “driver mutation” in a very small subset of patients with NSCLC: the fusion between the 5’ portion of EML4 (echinoderm microtubule-associated like-protein 4) and the 3’ portion of ALK (anaplastic lymphoma kinase) [8]. The importance of this discovery is highlighted by new agents that target this unique chimeric protein. In this chapter, we will review the biology and treatment of EML4-ALK and other ALK gene rearrangements in NSCLC.
The Chemical Cross-Linking Of Peptide Chains
Published in Roger L. Lundblad, Chemical Reagents for Protein Modification, 2020
In addition to the study of protein-protein interactions, intramolecular cross-linking has been of value in increasing protein stability5-7 as well as stabilizing erythrocyte structure.8 Cross-linking between a biologically active protein and a carrier protein has been advocated for therapeutic purposes9 although this approach will likely be supplanted by the preparation of chimeric proteins. Covalent cross-linking with the reagents described in this chapter have been used to complex peptides to carrier proteins such as hemocyanin or tetanus toxin for the preparation of antipeptide antibodies.10 Care must be exercised in the screening of antibodies resulting from the use of peptide-carrier conjugates not only for cross-reactivity with the carrier protein but also for antibodies directly to coupling groups used in such procedures.11
The MICA-NKG2D axis in clear cell renal cell carcinoma bolsters MICA as target in immuno-oncology
Published in OncoImmunology, 2022
Florencia Secchiari, Sol Yanel Nuñez, Jessica Mariel Sierra, Andrea Ziblat, María Victoria Regge, Ximena Lucía Raffo Iraolagoitia, Agustín Rovegno, Carlos Ameri, Fernando Pablo Secin, Nicolás Richards, Hernando Ríos Pita, Gonzalo Vitagliano, Luis Rico, Mauro Mieggi, Florencia Frascheri, Nicolás Bonanno, Leandro Blas, Aldana Trotta, Adrián David Friedrich, Mercedes Beatriz Fuertes, Carolina Inés Domaica, Norberto Walter Zwirner
Antibody-dependent cell-mediated cytotoxicity (ADCC) is one of the major NK cell-mediated effector functions and responsible for the therapeutic efficacy of several mAbs currently used to treat cancer patients.46,47 We previously observed that cell surface MICA constitutes a druggable target because anti-MICA Abs generated by immunization with a chimeric protein significantly delayed the growth of MICA-expressing tumors in part due to the induction of ADCC.48 Complementary results were published recently using another chimeric protein as cancer vaccine that elicits anti-MICA Abs that trigger T cell- and NK cell-mediated tumor elimination.49 Targeting MICA and MICB has been also assessed using mAbs.43,44,50–52 However, to successfully trigger ADCC against NKG2DLs, these molecules should be expressed on the tumor cell surface, which should be unambiguously assessed on primary tumors by strategies such as classical FC or cytometry-time-of-flight (CYTOF). Such approaches would allow the selection of the optimal NKG2DL to be targeted and mitigate risks in clinical trials with putative anti-NKG2DL Abs because it would facilitate the selection of patients with higher chances of clinical benefit.
The potential of plant-made vaccines to fight picornavirus
Published in Expert Review of Vaccines, 2020
Omayra C. Bolaños-Martínez, Sergio Rosales-Mendoza
Plant-based vaccines are being adopted as an alternative to generate new HAV vaccines. In 2011, Chung et al. reported the expression and immunogenicity of a recombinant chimeric protein (HAV VP1-Fc) containing the VP1 viral protein and an Fc antibody fragment. The chimeric protein was detected and subsequently purified. The expression levels reached up to 0.6% TSP. The immunogenicity was assessed in mice after i.p. immunization (4 times at 2-week intervals with 30 µg of VP1). Strong IgG response to VP1-Fc in sera was obtained from the group immunized with the plant-made antigen. Furthermore, splenocytes from immunized mice showed increased INF-γ and IL-4 production upon antigenic stimuli. These results indicated the induction of Th1 and Th2-type cytokines [42]. The assessment of the protective capacity of this vaccine in appropriate animal models will provide solid evidence of its true potential.
Vaccine-induced CD8 T cells are redirected with peptide-MHC class I-IgG antibody fusion proteins to eliminate tumor cells in vivo
Published in mAbs, 2020
Cornelia Fischer, Michael W. Munks, Ann B. Hill, Richard A. Kroczek, Stefan Bissinger, Verena Brand, Martina Schmittnaegel, Sabine Imhof-Jung, Eike Hoffmann, Frank Herting, Christian Klein, Hendrik Knoetgen
An alternative method of activating T cells to eliminate tumor cells is to use only antigen-specific T cells instead of all T cells. For viral infections, potent antigens are well described and can be used as antigenic peptides in recombinant peptide MHC class I complexes to engage preexisting effector cells. For that purpose, pMHCI-IgG molecules have been designed.5–7 These chimeric proteins contain a monoclonal antibody (mAb), specific for a tumor-associated antigen, linked to a single-chain peptide-MHC I molecule (pMHCI) presenting an antigenic, mostly immunodominant viral peptide. The pMHCI-IgGs are named according to the peptide in the MHC class I complex and the antibody target (e.g., M38-αFAP). The molecules mimic an infection in the tumor cells via a viral antigen presented on MHC I, which activates virus-specific CD8 T cells. Similar to CAR-T cell and TCB immunotherapies, tumor cells are flagged for CD8 T cell killing, regardless of whether or not they process and present endogenous MHC I.