Name of the laboratory
Members of the laboratory
- Unit Leader
Gholamreza Hassanzadeh-Ghassabeh email@example.com
Steve Schoonooghe firstname.lastname@example.org
Rolando Paciello email@example.com
Ema Romao firstname.lastname@example.org
Jan Van Gompel email@example.com
Jelle Elseviers firstname.lastname@example.org
Ines Camoes email@example.com
Camelids were found to have IgGs (IgG2 & IgG3) in their serum devoid of light chains. When the antigen binding VHH domain (Nanobody®) is isolated from these heavy-chain-antibodies, a 15 kDa single domain antigen binding fragment is obtained. Besides a near limitless repertoire diversity and the potential for highly discriminating (1 AA difference) & high affinity single domains, the absence of a VL (and a linker to make a scFv) has a number of marked advantages: easy identification, high stability, high solubility and a generally high expression yield. On top of that Nanobodies sometimes provide access to cryptic antigens & epitopes.
These characteristics make Nanobodies very flexible molecules useful in a wide variety of fields, such as immunotherapy, immunohistochemistry, immunomodulation, intracellular expression (intrabodies), bio-imaging and biosensor-applications. As proteomics tools, they can be deployed for expression profiling, physical mapping of proteins, protein-protein interaction studies, functional analysis and (in)activation of genes. Reformatting for these applications is easy: affinity tags, biotynilation, bivalent or bispecific constructs are all possible. They can even be re-formatted as an antibody in front of a human or mouse Fc if a ‘classic’ antibody format is required.
The VIB Nanobody Core provides acces to the powerful Nanobody® technology for both academic as non-academic researchers. At the VIB Nanobody Core we try to cater to our clients with a customized service as much as possible by providing the following services:
- Nanobody generation
- Nanobody and antibody characterization
- Nanobody and antibody construct engineering
We have close ties to VIB research groups studying and combating cancer. As such we have built up a strong expertise in cancer immunotherapy. From this knowledge we are developing Nb based therapeutic molecules for the diagnosis and treatment of cancer. This can be through attaching toxic payloads to cancer targeting Nbs and/or by making Nbs that identify (diagnosis) or target (therapeutics) immune cells important in the progression or destruction of tumors.
Serum half-life extension of therapeutics
Smaller sized therapeutic proteins with a size below the renal cut-off value (+/- 60 kDa) are rapidly cleared from circulation. This can be prevented in several ways. Two of the most common methods are by either making the molecule larger or through the addition of an affinity for an abundant molecule in serum. The first approach, mostly done through fusion to an Fc-domain is something we already have on offer. For the second approach, resulting in a smaller molecule with better tissue penetration and arguably less side-effects, we have been developing a set of Nbs that serve to extend the serum-half life of therapeutic proteins (mostly Nbs) in different species. We seek to characterize these Nbs as much as possible so they can be easily translated to a clinical setting. Currently we have an extensively characterized Nb available against human, mouse, cyno and rat albumin which we offer through licensing. Other Nbs for albumins in other species are also being actively persued.
- Nanobody generation
- Various immunization techniques
- Antibody phage library generation and screening
- Screening and affinity characterisation through ELISA, FACS, BLI(Octet), SPR(Biacore)
- Thermo-, solvent- and freeze-thaw stability determinations using fluorometric assays and Uncle platform
- In silico analysis of Nanobody B-cell lineages and potential developability issues
- (Re-)Engineering of Nanobody & Antibody constructs: Fc-fusions, GFP fusions, multi-specifics, multi-valents,...
- Development of anti-matrix metalloproteinase-2 (MMP-2) nanobodies as potential therapeutic and diagnostic tools. Marturano A, Hendrickx M, Falcinelli E, Sebastiano M, Guglielmini G, Hassanzadeh Ghassabeh G, Muyldermans S, Declerck P, Gresele P. NANOMEDICINE-UK, 102103, 24,2020
- Targeting Neuropilin-1 with Nanobodies Reduces Colorectal Carcinoma Development. De V*, Bonelli S*, Awad R, Dewilde M, Rizzolio S, Lecocq Q, Bolli E, Santos A, Laoui D, Schoonooghe S, Tamagnone L, Goyvaerts C, Mazzone M, BRECKPOT K, Van Ginderachter J. Cancers, 3582, 12, 2020
- Identification of Nanobodies against the Acute Myeloid Leukemia Marker CD33. Romão E*, Krasniqi A*, Maes L, Vandenbrande C, Sterckx Y, Stijlemans B, Vincke C, Devoogdt N, Muyldermans S. INT J MOL SCI, 21, 2020
- Structural basis for the high specificity of a Trypanosoma congolense immunoassay targeting glycosomal aldolase. Pinto Torres J*, Odongo S*, Lee F, Gaspariunaite V, Muyldermans S, Magez S, Sterckx Y. PLOS NEGL TROP DIS, e0005932, 11, 2017
- Single-domain antibody fusion proteins can target and shuttle functional proteins into macrophage mannose receptor expressing macrophages. De V, Lecocq Q, Giron P, Heirman C, Geeraerts X, Bolli E, Movahedi K, Massa S, Schoonooghe S, Thielemans K, Goyvaerts C, Van Ginderachter J, Breckpot K. J CONTROL RELEASE, 107-120, 299, 2019
- An innovative approach in the detection of Toxocara canis excretory/secretory antigens using specific nanobodies. Morales-yanez F, Sariego I, Vincke C, Hassanzadeh Ghassabeh G, Polman K, Muyldermans S. INT J PARASITOL, 635-645, 49, 2019
- Novel half-life extended anti-MIF nanobodies protect against endotoxic shock. Sparkes A, De Baetselier P, Brys L, Cabrito I, Sterckx Y, Schoonooghe S, Muyldermans S, Raes G, Bucala R, Vanlandschoot P, Van Ginderachter J, Stijlemans B. FASEB J, 3411-3422, 32, 2018
- In planta expression of nanobody-based designer chicken antibodies targeting Campylobacter. Vanmarsenille C, Elseviers J, Yvanoff C, Hassanzadeh Ghassabeh G, Garcia Rodriguez G, Martens E, Depicker A, Martel A, Haesebrouck F, Pasmans F, Hernalsteens J, De Greve H. PLoS One, e0204222, 13, 2018
- Identification and characterization of Nanobodies targeting the EphA4 receptor. Schoonaert L*, Rué Cabré L*, Roucourt B, Timmers M, Little S, Chávez Gutiérrez L, Dewilde M, Joyce P, Curnock A, Weber P, Haustraete J, Hassanzadeh Ghassabeh G, De Strooper B, Van Den Bosch L, Van Damme P, Lemmens R, Robberecht W. J BIOL CHEM, 11452-11465, 292, 2017
- Hierarchical and Redundant Roles of Activating FcgammaRs in Protection against Influenza Disease by M2e-Specific IgG1 and IgG2a Antibodies. Van den Hoecke S, Ehrhardt K, Kolpe A, El B, Deng L, Grootaert H, Schoonooghe S, Smet A, Bentahir M, Roose K, Schotsaert M, Schepens B, Callewaert N, Nimmerjahn F, Staeheli P, Hengel H, Saelens X. J VIROL, e02500-16, 91, 2017
- Nanobodies targeting conserved epitopes on the major outer membrane protein of Campylobacter as potential tools for control of Campylobacter colonization. Vanmarsenille C, Diaz D, Elseviers J, Hassanzadeh Ghassabeh G, Moonens K, Vertommen D, Martel A, Haesebrouck F, Pasmans F, Hernalsteens J, De Greve H. VET RES, 86, 48, 2017
- Structural evaluation of a nanobody targeting complement receptor Vsig4 and its cross reactivity. Wen Y, Ouyang Z, Schoonooghe S, Luo S, De Baetselier P, Lu W, Muyldermans S, Raes G, Zheng F. IMMUNOBIOLOGY, 807-813, 222, 2017