High-level expression of Camelid nanobodies in Nicotiana benthamiana

被引:39
作者
Teh, Yi-Hui Audrey [1 ]
Kavanagh, Tony A. [1 ]
机构
[1] Trinity Coll Dublin, Plant Mol Genet Lab, Smurfit Inst Genet, Dublin 2, Ireland
关键词
Camelid; VHH; Nanobody; Anti-lysozyme; Nicotiana benthamiana; SINGLE-DOMAIN ANTIBODY; HEAVY-CHAIN ANTIBODIES; SECRETORY PATHWAY; TRANSGENIC PLANTS; CANCER-THERAPY; LIGHT-CHAINS; FRAGMENTS; ANTIGEN; PROTEIN; BINDING;
D O I
10.1007/s11248-009-9338-0
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Nanobodies (or VHHs) are single-domain antigen-binding fragments derived from Camelid heavy chain-only antibodies. Their small size, monomeric behaviour, high stability and solubility, and ability to bind epitopes not accessible to conventional antibodies make them especially suitable for many therapeutic and biotechnological applications. Here we describe high-level expression, in Nicotiana benthamiana, of three versions of an anti-hen egg white lysozyme (HEWL) nanobody which include the original VHH from an immunized library (cAbLys3), a codon-optimized derivative, and a codon-optimized hybrid nanobody comprising the CDRs of cAbLys3 grafted onto an alternative 'universal' nanobody framework. His6- and StrepII-tagged derivatives of each nanobody were targeted for accumulation in the cytoplasm, chloroplast and apoplast using different pre-sequences. When targeted to the apoplast, intact functional nanobodies accumulated at an exceptionally high level (up to 30% total leaf protein), demonstrating the great potential of plants as a nanobody production system.
引用
收藏
页码:575 / 586
页数:12
相关论文
共 60 条
[31]   Resistance to root-knot nematode in tomato roots expressing a nematicidal Bacillus thuringiensis crystal protein [J].
Li, Xiang-Qian ;
Wei, Jun-Zhi ;
Tan, Anderson ;
Aroian, Raffi V. .
PLANT BIOTECHNOLOGY JOURNAL, 2007, 5 (04) :455-464
[32]   GENERATION AND ASSEMBLY OF SECRETORY ANTIBODIES IN PLANTS [J].
MA, JKC ;
HIATT, A ;
HEIN, M ;
VINE, ND ;
WANG, F ;
STABILA, P ;
VANDOLLEWEERD, C ;
MOSTOV, K ;
LEHNER, T .
SCIENCE, 1995, 268 (5211) :716-719
[33]   In planta engineering of viral RNA replicons:: Efficient assembly by recombination of DNA modules delivered by Agrobacterium [J].
Marillonnet, S ;
Giritch, A ;
Gils, M ;
Kandzia, R ;
Klimyuk, V ;
Gleba, Y .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2004, 101 (18) :6852-6857
[34]   Subcellular targeting of human interleukin-10 in plants [J].
Menassa, R ;
Kennette, W ;
Nguyen, V ;
Rymerson, R ;
Jevnikar, A ;
Brandle, J .
JOURNAL OF BIOTECHNOLOGY, 2004, 108 (02) :179-183
[35]   Selection of phage-displayed llama single-domain antibodies that transmigrate across human blood-brain barrier endothelium [J].
Muruganandam, A ;
Tanha, J ;
Narang, S ;
Stanimirovic, D .
FASEB JOURNAL, 2001, 15 (14) :240-+
[36]   SEQUENCE AND STRUCTURE OF V-H DOMAIN FROM NATURALLY-OCCURRING CAMEL HEAVY-CHAIN IMMUNOGLOBULINS LACKING LIGHT-CHAINS [J].
MUYLDERMANS, S ;
ATARHOUCH, T ;
SALDANHA, J ;
BARBOSA, JARG ;
HAMERS, R .
PROTEIN ENGINEERING, 1994, 7 (09) :1129-1135
[37]  
Muyldermans S, 2001, J Biotechnol, V74, P277
[38]   Codon usage tabulated from international DNA sequence databases: status for the year 2000 [J].
Nakamura, Y ;
Gojobori, T ;
Ikemura, T .
NUCLEIC ACIDS RESEARCH, 2000, 28 (01) :292-292
[39]   Camel heavy-chain antibodies:: diverse germline VHH and specific mechanisms enlarge the antigen-binding repertoire [J].
Nguyen, VK ;
Hamers, R ;
Wyns, L ;
Muyldermans, S .
EMBO JOURNAL, 2000, 19 (05) :921-930
[40]   Highly efficient targeting and accumulation of a Fab fragment within the secretory pathway and apoplast of Arabidopsis thaliana [J].
Peeters, K ;
De Wilde, C ;
Depicker, A .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 2001, 268 (15) :4251-4260