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
[1]   Unintended molecular interactions in transgenic plants expressing clinically useful proteins: The case of bovine aprotinin traveling the potato leaf cell secretory pathway [J].
Badri, M. Amine ;
Rivard, Daniel ;
Coenen, Karine ;
Michaud, Dominique .
PROTEOMICS, 2009, 9 (03) :746-756
[2]   Experimental therapy of African trypanosomiasis with a nanobody-conjugated human trypanolytic factor [J].
Baral, Toya Nath ;
Magez, Stefan ;
Stijlemans, Benoit ;
Conrath, Katja ;
Vanhollebeke, Benoit ;
Pays, Etienne ;
Muyldermans, Serge ;
De Baetselier, Patrick .
NATURE MEDICINE, 2006, 12 (05) :580-584
[3]   Preventing unintended proteolysis in plant protein biofactories [J].
Benchabane, Meriem ;
Goulet, Charles ;
Rivard, Daniel ;
Faye, Loic ;
Gomord, Veronique ;
Michaud, Dominique .
PLANT BIOTECHNOLOGY JOURNAL, 2008, 6 (07) :633-648
[4]   Compartment-specific accumulation of recombinant immunoglobulins in plant cells: an essential tool for antibody production and immunomodulation of physiological functions and pathogen activity [J].
Conrad, U ;
Fiedler, U .
PLANT MOLECULAR BIOLOGY, 1998, 38 (1-2) :101-109
[5]   Formatted anti-tumor necrosis factor α VHH proteins derived from camelids show superior potency and targeting to inflamed joints in a murine model of collagen-induced arthritis [J].
Coppieters, Ken ;
Dreier, Torsten ;
Silence, Karen ;
de Haard, Hans ;
Lauwereys, Marc ;
Casteels, Peter ;
Beirnaert, Els ;
Jonckheere, Heidi ;
de Wiele, Christophe Van ;
Staelens, Ludovicus ;
Hostens, Jeroen ;
Revets, Hilde ;
Remaut, Erik ;
Elewaut, Dirk ;
Rottiers, Pieter .
ARTHRITIS AND RHEUMATISM, 2006, 54 (06) :1856-1866
[6]   Efficient cancer therapy with a nanobody-based conjugate [J].
Cortez-Retamozo, V ;
Backmann, N ;
Senter, PD ;
Wernery, U ;
De Baetselier, P ;
Muyldermans, S ;
Revets, H .
CANCER RESEARCH, 2004, 64 (08) :2853-2857
[7]   Molecular basis for the preferential cleft recognition by dromedary heavy-chain antibodies [J].
De Genst, E ;
Silence, K ;
Decanniere, K ;
Conrath, K ;
Loris, R ;
Kinne, R ;
Muyldermans, S ;
Wyns, L .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2006, 103 (12) :4586-4591
[8]   Boosting heterologous protein production in transgenic dicotyledonous seeds using Phaseolus vulgaris regulatory sequences [J].
De Jaeger, G ;
Scheffer, S ;
Jacobs, A ;
Zambre, M ;
Zobell, O ;
Goossens, A ;
Depicker, A ;
Angenon, G .
NATURE BIOTECHNOLOGY, 2002, 20 (12) :1265-1268
[9]   Crystal structure of a camel single-domain V-H antibody fragment in complex with lysozyme [J].
Desmyter, A ;
Transue, TR ;
Ghahroudi, MA ;
Thi, MHD ;
Poortmans, F ;
Hamers, R ;
Muyldermans, S ;
Wyns, L .
NATURE STRUCTURAL BIOLOGY, 1996, 3 (09) :803-811
[10]   Antigen specificity and high affinity binding provided by one single loop of a camel single-domain antibody [J].
Desmyter, A ;
Decanniere, K ;
Muyldermans, S ;
Wyns, L .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (28) :26285-26290