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Biology subjects

Ballegeer, M.

Publications and source records attributed to Ballegeer, M..

4 recordsLinked to original sources

ENGINEERING AND PRECLINICAL EVALUATION OF DRIED FOOD-FORMULATED YEAST-SECRETED ANTIBODIES AS PERI-EXPOSURE PROPHYLAXIS AGAINST CLOSTRIDIOIDES DIFFICILE DISEASE.

Clostridioides difficile gastrointestinal infection (CDI) causes significant disease burden, often following gut dysbiosis induced by antibiotic treatment in at-risk individuals. A non-invasive, easy to use targeted prophylaxis in such cases of acute elevated CDI risk, especially in those with a history of recurrent CDI, would prevent much suffering. In this study, we envisioned a simple prophylactic intervention for CDI enabled by the oral administration of yeast-secreted dried food-formulated C. difficile toxin A (TcdA)-and B (TcdB)-neutralizing VHH-based antibodies. We engineered two antibody versions: a previously reported tetravalent VHH (VHH4) comprising dual specificities for TcdA and TcdB, and its murine IgA Fc fusion counterpart (VHH4-mIgA Fc). We explored Generally Recognized as Safe (GRAS) Komagataella phaffii yeast as a low-cost, highly scalable production platform. In a first experiment, we produced the antibodies at small scale in shake flask yeast cultivations and formulated the secreted antibody-containing growth medium into standard-composition dried mouse feed pellets. The antibody food pellet-administration intervention was tested in a C. difficile spore-challenged mouse model in which CDI leads to 50% mortality of untreated animals. We started the antibody-feed prophylaxis dosed at 10 nmol/g pellet one day prior to C. difficile challenge and continued until the infection was cleared with ad libitum feeding. We found that the VHH4 feed almost completely prevented mortality and reduced disease-related weight loss. Despite its higher in vitro potency against TcdA and equipotent potency against TcdB, the VHH4-mIgA Fc fusion did not confer additional in vivo benefit, and further work focused on the simpler VHH4 format. Scalable high-cell-density bioreactor production of VHH4 yielded equally effective prophylactic formulations at the same dose of 10 nmol/g pellet, achieving complete survival and reduced disease burden. Our findings suggest that, with further antibody- and process development, oral prophylaxis with scalable, cost-effective, yeast-produced, dried food-formulated anti-toxin VHHs could offer a simple non-invasive, non-antibiotic prophylaxis option for the high-risk (r)CDI patient population.

molecular biology↗

Fc-dependent protective efficacy of non-inhibitory antibodies targeting influenza A virus neuraminidase is limited by epitope availability

Antibodies targeting hemagglutinin and neuraminidase (NA) are key components of the adaptive immune response against influenza A virus (IAV). However, antigenic drift allows the virus to escape inhibition by such antibodies. In this study, we aimed to isolate antibodies with cross-subtype reactivity against human H1N1 and H3N2 IAVs from transgenic mice bearing genes encoding the human immunoglobulin variable regions. We immunized these mice with recombinant N1 and N2 NA proteins, presenting them either as unconjugated soluble proteins or conjugated to self-assembling protein nanoparticles. This approach yielded a panel of NA-specific monoclonal antibodies (mAbs) with various levels of intra-and inter-subtype reactivity for N1 and N2 NA. Three of these mAbs, which collectively recognize two distinct epitopes, were cross-reactive against N1 and N2 NAs in ELISA, but did not inhibit NA enzymatic activity. Two of these mAbs, 21H8 and 45D9, were selected for further characterization. These recognized different epitopes and induced Fc-mediated effector functions to varying extents. Prophylactic administration of 21H8, but not 45D9, protected mice against challenge with H1N1 IAV, while neither mAb protected against a H3N2 challenge. The observed protective efficacy correlated with the mAbs capacity, or lack thereof, to bind membrane-associated full-length NA. The introduction of Fc silencing mutations in mAb 21H8 resulted in an inability to activate NK cells or mediate phagocytosis in vitro and significantly reduced protection in vivo, indicating that the protective efficacy of mAb 21H8 is Fc-dependent. However, mAb 21H8 expressed with reduced core fucosylation of its Fc N-glycan, which specifically enhanced NK cell activation in vitro, failed to improve protection against H1N1 challenge in vivo. Future work is needed to decipher in more detail the mechanism of Fc-mediated protection against influenza via NA-specific antibodies and to identify the optimal strategies for their enhancement.

microbiology↗

Ultrapotent SARS coronavirus-neutralizing single-domain antibodies that bind a conserved membrane proximal epitope of the spike

Currently circulating SARS-CoV-2 variants have gained complete or significant resistance to all SARS-CoV-2-neutralizing antibodies that have been used in the clinic. Such antibodies can prevent severe disease in SARS-CoV-2 exposed patients for whom vaccines may not provide optimal protection. Here, we describe single-domain antibodies (VHHs), also known as nanobodies, that can broadly neutralize SARS-CoV-2 with unusually high potency. Structural analysis revealed their binding to a unique, highly conserved, membrane proximal, quaternary epitope in the S2 subunit of the spike. Furthermore, a VHH-human IgG1 Fc fusion, efficiently expressed in Chinese hamster ovary cells as a stable antibody construct, protected hamsters against SARS-CoV-2 replication in a therapeutic setting when administered systemically at low dose. This VHH-based antibody represents a new candidate anti-COVID-19 biologic that targets the Achilles heel of the viral spike.

microbiology↗

Cleavage of cFLIP restrains cell death during viral infection and tissue injury and favors tissue repair

Cell death coordinates repair programs following pathogen attack and tissue injury. However, aberrant cell death can interfere with such programs and cause organ failure. cFLIP is a crucial regulator of cell death and a substrate of Caspase-8. Yet, the physiological role of cFLIP cleavage by Caspase-8 remains elusive. Here, we discovered an essential role for cFLIP cleavage in restraining cell death in different pathophysiological scenarios. Mice expressing a cleavage-resistant cFLIP mutant, CflipD377A, exhibited increased sensitivity to SARS-CoV-induced lethality, impaired skin wound healing and increased tissue damage caused by Sharpin deficiency. In vitro, abrogation of cFLIP cleavage sensitizes cells to TNF-induced necroptosis and apoptosis by favoring complex-II formation. Mechanistically, the cell death-sensitizing effect of the D377A mutation depends on Gln(Q)469. These results reveal a crucial role for cFLIP cleavage in controlling the amplitude of cell death responses occurring upon tissue stress, to ensure the execution of repair programs.

cell biology↗