Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 428948
Title Improved functional immobilization of llama single-domain antibody fragments to polystyrene surfaces using small peptides
Author(s) Harmsen, M.M.; Fijten, H.P.D.
Source Journal of Immunoassay and Immunochemistry 33 (2012)3. - ISSN 1532-1819 - p. 234 - 251.
Department(s) CVI Virology
CVI Infection Biology
Publication type Refereed Article in a scientific journal
Publication year 2012
Keyword(s) linked-immunosorbent-assay - escherichia-coli - passive-immunization - mouth-disease - in-vitro - microarrays - strategies - bivalent - pigs - hydrophobins
Abstract We studied the effect of different fusion domains on the functional immobilization of three llama single-domain antibody fragments (VHHs) after passive adsorption to polystyrene in enzyme-linked immunosorbent assays (ELISA). Three VHHs produced without any fusion domain were efficiently adsorbed to polystyrene, which, however, resulted in inefficient antigen binding. Functional VHH immobilization was improved by VHH fusion to a consecutive myc-His6-tag and was even more improved by fusion to the llama antibody long hinge region containing an additional His6-tag (LHc-His6). The partial dimerization of VHH-LHc-His6 fusion proteins through LHc-mediated disulfide-bond formation was not essential for their improved functional immobilization. VHH fusions to specific polystyrene binding peptides, hydrophobins, or other, unrelated VHH domains were less suitable for increasing functional VHH immobilization because of reduced microbial expression levels. Thus, VHH-LHc-His6 fusion proteins are most suited for functional passive adsorption in ELISA.
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