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Order Blubervirales: Surface Protein
Published in Paul Pumpens, Peter Pushko, Philippe Le Mercier, Virus-Like Particles, 2022
Paul Pumpens, Peter Pushko, Philippe Le Mercier
Since the Z domain limited the animal species and subtypes of IgGs that can be displayed on the ZZ-BNCs, Tatematsu et al. (2016) introduced into the BNCs an Ig κ light chain-binding B1 domain of Finegoldia magna protein L (protein-L B1 domain) and an Ig Fc-binding C2 domain of Streptococcus species protein G (protein-G C2 domain) to produce LG-BNCs. The LL-BNCs were constructed in a similar way using a tandem form of the protein-L B1 domain. Both LG-BNCs and LL-BNCs displayed rat IgGs, mouse IgG1, human IgG3, and human IgM—all of which were not binding to the ZZ-BNCs—and accumulated in target cells in an antibody specificity-dependent manner. Thus, when these BNCs displayed anti-CD11c IgG or anti-EGFR IgG, both of which cannot bind to the Z domain, they could bind to and then enter their respective target cells (Tatematsu et al. 2016). Li H et al. (2018, 2020) introduced the tandem form of G and L domains, as a GL domain, instead of the ZZ domain and generated both GL-BNCs and GL-virosomes, which functioned as promising macrophage-specific and phagocytosis-inducing drug delivery nanocarriers.
Animal Source Foods
Published in Chuong Pham-Huy, Bruno Pham Huy, Food and Lifestyle in Health and Disease, 2022
Chuong Pham-Huy, Bruno Pham Huy
Proteins. Milk is generally considered an important protein source in the human diet, supplying approximately 32 g protein/L (92–99). Its protein fraction can be divided into soluble and insoluble proteins. Soluble proteins, named whey proteins, represent approximatively 20% of milk protein fraction, whereas the insoluble proteins, namely caseins, represent about 80% and may vary slightly depending on the species (92–96). The casein family contains phosphorus and will coagulate at pH 4.6.
In Vivo Modulation of Lymphohemopoietic Stem Cell Populations with Cytokines
Published in Thomas F. Kresina, Immune Modulating Agents, 2020
In vivo studies have clearly demonstrated the potency of various inhibitory cytokines that reduce the percentage of cells in S phase. Treatment of mice with macrophage inflammatory protein-lα (MIP-lα) or transforming growth factor-β (TGF-β) before the injection of a cytotoxic drug has resulted in improved hematological recovery and survival [60,61]. Obviously, these inhibitors may provide a potential prophylactic treatment to prepare patients receiving chemotherapy, but, at present, the impact of these inhibitors in such clinical conditions has yet to be established. The effectiveness of inhibitory cytokines is dependent on the cycling activity of stem cells present in cancer patients. It is not unlikely that the proliferation of stem cells in these patients, particularly in those with malignant bone marrow involvement, is substantially different from that in normal, healthy individuals. Limited information on this subject is available. However, data of Broxmeyer et al. show that the cycling activity of various hemopoietic progenitors in patients with sarcoma is significantly reduced as compared to that of normal bone marrow [62]. If this situation proves to be a general finding, then pretreatment of cancer patients with inhibitory cytokines may not be very effective, since their stem cells are slowly cycling.
Correlated analytical and functional evaluation of higher order structure perturbations from oxidation of NISTmAb
Published in mAbs, 2023
Tsega L. Solomon, Frank Delaglio, John P. Giddens, John P. Marino, Yihua Bruce Yu, Marc B. Taraban, Robert G. Brinson
Met oxidation in mAbs can alter biological activity by diminishing ligand binding to both the Fc and Fab regions.18,36 Here, to correlate the NMR and stability methods to a functional change, the binding capacity of oxidized NISTmAb was assessed by three binding partners that are known to have distinct binding sites on mAbs. Two of the partners are bacterial proteins, Protein A and Protein L, which bind to the Fc domain and to the variable region of the Fab light chain, respectively.37–39 The third is a synthetic peptide, F peptide, which binds to the complementary-determining region (CDR) of the Fab heavy chain. Oxidized NISTmAb binding to Protein A, Protein L, and F peptide was measured with an SPR assay where ligands are immobilized to a sensor chip. The SPR results showed that binding to Protein A and F peptide were sensitive to Met oxidation, causing a decline in affinity with increasing oxidation time. However, the binding affinity of protein L remained mostly unaffected (Figure 7). Relative binding assessment demonstrated that within 4 h of NISTmAb oxidation, binding affinity to Protein A decreased by 50% and binding to F peptide by 30%. Although binding capacity to both ligands continued to decrease until 24 h of oxidation, the first 4 h exhibit the fastest loss in binding affinity, which directly correlates to the results of R2(1H2O), 2D NMR, and Tycho measurements.
Bacteremia and complicated parapneumonic effusion caused by Bordetella holmesii in an elderly patient
Published in Acta Clinica Belgica, 2021
Eveline Vancraeynest, Lien Cattoir, Kristien Van Vaerenbergh, Hans De Beenhouwer, Anne Vankeerberghen, An Boel
An 84-year-old Caucasian female presented at the emergency department with progressive exertional dyspnea since 15 months. Her medical history included colon cancer which had been treated successfully more than 15 years before, diabetes mellitus type 2, chronic hepatitis C virus infection, and chronic heart failure with pleural effusion for which multiple pleural punctures had been performed. Two weeks before admission she complained of a tickly, productive cough with yellow sputa. She noticed moderate throat and ear pain, but no fever. Two days before admission, a pleural puncture was performed because of recurrent bilateral pleural effusion. Aerobic and anaerobic cultures remained negative. On admission, the clinical examination revealed decreased breath sounds and bilateral crepitations. A white blood cell count (WBC) of 17640/µL (15680 neutrophils/µL) and a CRP of 281mg/L were the only divergent blood values. Chest radiography showed the known bilateral pleural effusion, with an increase at the left side for which superinfection could not be excluded. The patient was admitted, blood cultures were obtained and intravenous amoxicillin/clavulanic acid 1 g q8h was started empirically. The day after admission, pleural fluid and sputum were sent to the laboratory for microbiological evaluation. Cell count and biochemical features of the pleural fluid were: 432 WBC/µL with 65% neutrophils, 1.04 g glucose/L, 45.30 g protein/L, 18.7 g albumin/L and an LDH of 308 U/L. Corresponding values in blood were 92 g protein/L, 31 g albumin/L and an LDH of 297 U/L, all characteristically for an exudate [13].
Investigation of the effect of salt additives in Protein L affinity chromatography for the purification of tandem single-chain variable fragment bispecific antibodies
Published in mAbs, 2020
Serene W. Chen, Darryl Tan, Yuan Sheng Yang, Wei Zhang
Another alternative purification method for the purification of tandem scFv BsAb is the use of Protein L affinity chromatography,19,20 which eliminates the need for the presence of a poly-histidine tag on the target molecule. Isolated from the bacteria Peptostreptococcus magnus, Protein L is a cell surface protein that interacts with the variable region of the antibody’s kappa (К) light chain, in particular, the К1, К3, and К4 light chains, allowing it to bind to approximately 67% of human immunoglobulins and 99% of mouse immunoglobulins.21–23 So far, the use of Protein L affinity chromatography has been reported for research purposes only, with overall purity reported as 50 – 70% after a single affinity chromatographic step20 and requiring additional Protein A or Protein G chromatographic steps and SEC to achieve higher purity.19