Efficient cancer therapy with a nanobody-based conjugate

被引:278
作者
Cortez-Retamozo, V
Backmann, N
Senter, PD
Wernery, U
De Baetselier, P
Muyldermans, S
Revets, H
机构
[1] Free Univ Brussels VIB, Dept Mol & Cellular Intaract, Brussels, Belgium
[2] Seattle Genet, Bothell, WA USA
[3] Cent Vet Res Labs, Dubai, U Arab Emirates
关键词
D O I
10.1158/0008-5472.CAN-03-3935
中图分类号
R73 [肿瘤学];
学科分类号
100214 ;
摘要
Nanobodies are the smallest fragments of naturally occurring single-domain antibodies that have evolved to be fully functional in the absence of a light chain. Nanobodies are strictly monomeric, very stable, and highly soluble entities. We identified a nanobody with subnanomolar affinity for the human tumor-associated carcinoembryonic antigen. This nanobody was conjugated to Enterobacter cloacae beta-lactamase, and its site-selective anticancer prodrug activation capacity was evaluated. The conjugate was readily purified in high yields without aggregation or loss of functionality of the constituents. In vitro experiments showed that the nanobody-enzyme conjugate effectively activated the release of phenylenediamine mustard from the cephalosporin nitrogen mustard prodrug 7-(4-carboxybutanamido) cephalosporin mustard at the surface of carcinoembryonic antigen-expressing LS174T cancer cells. In vivo studies demonstrated that the conjugate had an excellent biodistribution profile and induced regressions and cures of established tumor xenografts. The easy generation and manufacturing yield of nanobody-based conjugates together with their potent antitumor activity make nanobodies promising vehicles for new generation cancer therapeutics.
引用
收藏
页码:2853 / 2857
页数:5
相关论文
共 35 条
  • [1] ANTIBODY DIRECTED ENZYMES REVIVE ANTICANCER PRODRUGS CONCEPT
    BAGSHAWE, KD
    [J]. BRITISH JOURNAL OF CANCER, 1987, 56 (05) : 531 - 532
  • [2] Improving the efficacy of antibody-based cancer therapies
    Carter, P
    [J]. NATURE REVIEWS CANCER, 2001, 1 (02) : 118 - 129
  • [3] PHAGE LIBRARIES FOR GENERATION OF CLINICALLY USEFUL ANTIBODIES
    CHESTER, KA
    BEGENT, RHJ
    ROBSON, L
    KEEP, P
    PEDLEY, RB
    BODEN, JA
    BOXER, G
    GREEN, A
    WINTER, G
    COCHET, O
    HAWKINS, RE
    [J]. LANCET, 1994, 343 (8895) : 455 - 456
  • [4] β-lactamase inhibitors derived from single-domain antibody fragments elicited in the Camelidae
    Conrath, KE
    Lauwereys, M
    Galleni, M
    Matagne, A
    Frère, JM
    Kinne, J
    Wyns, L
    Muyldermans, S
    [J]. ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 2001, 45 (10) : 2807 - 2812
  • [5] Camel single-domain antibodies as modular building units in bispecific and bivalent antibody constructs
    Conrath, KE
    Lauwereys, M
    Wyns, L
    Muyldermans, S
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (10) : 7346 - 7350
  • [6] Efficient tumor targeting by single-domain antibody fragments of camels
    Cortez-Retamozo, V
    Lauwereys, M
    Gh, GH
    Gobert, M
    Conrath, K
    Muyldermans, S
    De Baetselier, P
    Revets, H
    [J]. INTERNATIONAL JOURNAL OF CANCER, 2002, 98 (03) : 456 - 462
  • [7] Single antibody domains as small recognition units: Design and in vitro antigen selection of camelized, human VH domains with improved protein stability
    Davies, J
    Riechmann, L
    [J]. PROTEIN ENGINEERING, 1996, 9 (06): : 531 - 537
  • [8] AUTOMATED-ANALYSIS OF ENZYME INACTIVATION PHENOMENA - APPLICATION TO BETA-LACTAMASES AND DD-PEPTIDASES
    DEMEESTER, F
    JORIS, B
    RECKINGER, G
    BELLEFROIDBOURGUIGNON, C
    FRERE, JM
    WALEY, SG
    [J]. BIOCHEMICAL PHARMACOLOGY, 1987, 36 (14) : 2393 - 2403
  • [9] Crystal structure of a camel single-domain V-H antibody fragment in complex with lysozyme
    Desmyter, A
    Transue, TR
    Ghahroudi, MA
    Thi, MHD
    Poortmans, F
    Hamers, R
    Muyldermans, S
    Wyns, L
    [J]. NATURE STRUCTURAL BIOLOGY, 1996, 3 (09): : 803 - 811
  • [10] Single-domain antibody fragments with high conformational stability
    Dumoulin, M
    Conrath, K
    Van Meirhaeghe, A
    Meersman, F
    Heremans, K
    Frenken, LGJ
    Muyldermans, S
    Wyns, L
    Matagne, A
    [J]. PROTEIN SCIENCE, 2002, 11 (03) : 500 - 515