| Literature DB >> 27226529 |
Evelyn De Tavernier1, Laurent Detalle1, Erika Morizzo1, Annelies Roobrouck1, Severine De Taeye1, Melanie Rieger1, Tom Verhaeghe1, Andreia Correia1, Rob Van Hegelsom1, Rita Figueirido1, Jeroen Noens1, Søren Steffensen1, Thomas Stöhr1, Willem Van de Velde1, Erik Depla1, Bruno Dombrecht2.
Abstract
Improving potencies through concomitant blockage of multiple epitopes and avid binding by fusing multiple (different) monovalent Nanobody building blocks via linker sequences into one multivalent polypeptide chain is an elegant alternative to affinity maturation. We explored a large and random formatting library of bivalent (combinations of two identical) and biparatopic (combinations of two different) Nanobodies for functional blockade of Pseudomonas aeruginosa PcrV. PcrV is an essential part of the P. aeruginosa type III secretion system (T3SS), and its oligomeric nature allows for multiple complex binding and blocking options. The library screening yielded a large number of promising biparatopic lead candidates, revealing significant (and non-trivial) preferences in terms of Nanobody building block and epitope bin combinations and orientations. Excellent potencies were confirmed upon further characterization in two different P. aeruginosa T3SS-mediated cytotoxicity assays. Three biparatopic Nanobodies were evaluated in a lethal mouse P. aeruginosa challenge pneumonia model, conferring 100% survival upon prophylactic administration and reducing lung P. aeruginosa burden by up to 2 logs. At very low doses, they protected the mice from P. aeruginosa infection-related changes in lung histology, myeloperoxidase production, and lung weight. Importantly, the most potent Nanobody still conferred protection after therapeutic administration up to 24 h post-infection. The concept of screening such formatting libraries for potency improvement is applicable to other targets and biological therapeutic platforms.Entities:
Keywords: PcrV; Pseudomonas aeruginosa (P. aeruginosa); avidity; biparatopic; bivalent; epitope mapping; formatting; high throughput screening (HTS); single-domain antibody (sdAb, Nanobody); type III secretion system (T3SS)
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Year: 2016 PMID: 27226529 PMCID: PMC4946937 DOI: 10.1074/jbc.M115.684241
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157