Properties, production, and applications of camelid single-domain antibody fragments

被引：594
作者：
Harmsen, M. M.
De Haard, H. J.
机构：
[1] Univ Wageningen & Res Ctr, Inst Anim Sci & Hlth, NL-8219 PH Lelystad, Netherlands
[2] Ablynx NV, B-9052 Ghent, Belgium
来源：
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY | 2007年 / 77卷 / 01期
关键词：
single-domain; microbial production; yeast; glycosylation;
D O I：
10.1007/s00253-007-1142-2
中图分类号：
Q81 [生物工程学（生物技术）]; Q93 [微生物学];
学科分类号：
071005 ; 0836 ; 090102 ; 100705 ;
摘要：
Camelids produce functional antibodies devoid of light chains of which the single N-terminal domain is fully capable of antigen binding. These single-domain antibody fragments (VHHs or Nanobodies (R)) have several advantages for biotechnological applications. They are well expressed in microorganisms and have a high stability and solubility. Furthermore, they are well suited for construction of larger molecules and selection systems such as phage, yeast, or ribosome display. This minireview offers an overview of (1) their properties as compared to conventional antibodies, (2) their production in microorganisms, with a focus on yeasts, and (3) their therapeutic applications.
引用
收藏
页码：13 / 22
页数：10
相关论文
共 93 条
  • [31] Passive immunization of guinea pigs with llama single-domain antibody fragments against foot-and-mouth disease
    Harmsen, M. M.
    van Solt, C. B.
    Fijten, H. P. D.
    van Keulen, L.
    Rosalia, R. A.
    Weerdmeester, K.
    Cornelissen, A. H. M.
    De Bruin, M. G. M.
    Eble, P. L.
    Dekker, A.
    [J]. VETERINARY MICROBIOLOGY, 2007, 120 (3-4) : 193 - 206
  • [32] Selection and optimization of proteolytically stable llama single-domain antibody fragments for oral immunotherapy
    Harmsen, M. M.
    van Solt, C. B.
    van Zijderveld-van Bemmel, A. M.
    Niewold, T. A.
    van Zijderveld, F. G.
    [J]. APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 2006, 72 (03) : 544 - 551
  • [33] Escherichia coli F4 fimbriae specific llama single-domain antibody fragments effectively inhibit bacterial adhesion in vitro but poorly protect against diarrhoea
    Harmsen, MM
    van Solt, CB
    Hoogendoorn, A
    van Zijderveld, FG
    Niewold, TA
    van der Meulen, J
    [J]. VETERINARY MICROBIOLOGY, 2005, 111 (1-2) : 89 - 98
  • [34] Prolonged in vivo residence times of llama single-domain antibody fragments in pigs by binding to porcine immunoglobulins
    Harmsen, MM
    Van Solt, CB
    Fijten, HPD
    Van Setten, MC
    [J]. VACCINE, 2005, 23 (41) : 4926 - 4934
  • [35] Llama heavy-chain V regions consist of at least four distinct subfamilies revealing novel sequence features
    Harmsen, MM
    Ruuls, RC
    Nijman, IJ
    Niewold, TA
    Frenken, LGJ
    de Geus, B
    [J]. MOLECULAR IMMUNOLOGY, 2000, 37 (10) : 579 - 590
  • [36] Neutralisation of venom-induced haemorrhage by IgG from camels and llamas immunised with viper venom and also by endogenous, non-IgG components in camelid sera
    Harrison, RA
    Hasson, SS
    Harmsen, M
    Laing, GD
    Conrath, K
    Theakston, RDG
    [J]. TOXICON, 2006, 47 (03) : 364 - 368
  • [37] Structure-immunogenicity relationships of therapeutic proteins
    Hermeling, S
    Crommelin, DJA
    Schellekens, H
    Jiskoot, W
    [J]. PHARMACEUTICAL RESEARCH, 2004, 21 (06) : 897 - 903
  • [38] Engineered antibody fragments and the rise of single domains
    Holliger, P
    Hudson, PJ
    [J]. NATURE BIOTECHNOLOGY, 2005, 23 (09) : 1126 - 1136
  • [39] Retargeting serum immunoglobulin with bispecific diabodies
    Holliger, P
    Wing, M
    Pound, JD
    Bohlen, H
    Winter, G
    [J]. NATURE BIOTECHNOLOGY, 1997, 15 (07) : 632 - 636
  • [40] Generation of heavy-chain-only antibodies in mice
    Janssens, Rick
    Dekker, Sylvia
    Hendriks, Rudi W.
    Panayotou, George
    van Remoortere, Alexandra
    San, John Kong-a
    Grosveld, Frank
    Drabek, Dubravka
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2006, 103 (41) : 15130 - 15135
12345678910