Large scale production of recombinant human lactoferrin in the milk of transgenic cows

被引:193
作者
van Berkel, PHC [1 ]
Welling, MM
Geerts, M
van Veen, HA
Ravensbergen, B
Salaheddine, M
Pauwels, EKJ
Pieper, F
Nuijens, JH
Nibbering, PH
机构
[1] Pharming, Leiden, Netherlands
[2] Leiden Univ, Med Ctr, Dept Radiol, Div Nucl Med, Leiden, Netherlands
[3] Leiden Univ, Med Ctr, Dept Infect Dis, Leiden, Netherlands
关键词
D O I
10.1038/nbt0502-484
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
The limited capacity of current bioreactors has led the biopharmaceutical industry to investigate alternative protein expression systems. The milk of transgenic cattle may provide an attractive vehicle for large-scale production of biopharmaceuticals, but there have been no reports on the characteristics of such recombinant proteins. Here we describe the production of recombinant human lactoferrin (rhLF), an iron-binding glycoprotein involved in innate host defense, at gram per liter concentrations in bovine milk. Natural hLF from human milk and rhLF had identical iron-binding and -release properties. Although natural hLF and rhLF underwent differential N-linked glycosylation, they were equally effective in three different in vivo infection models employing immunocompetent and leukocytopenic mice, and showed similar localization at sites of infection. Taken together, the results illustrate the potential of transgenic cattle in the large-scale production of biopharmaceuticals.
引用
收藏
页码:484 / 487
页数:4
相关论文
共 16 条
  • [1] STRUCTURE OF HUMAN LACTOFERRIN - CRYSTALLOGRAPHIC STRUCTURE-ANALYSIS AND REFINEMENT AT 2.8-A RESOLUTION
    ANDERSON, BF
    BAKER, HM
    NORRIS, GE
    RICE, DW
    BAKER, EN
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1989, 209 (04) : 711 - 734
  • [2] Developing efficient strategies for the generation of transgenic cattle which produce biopharmaceuticals in milk
    Brink, MF
    Bishop, MD
    Pieper, FR
    [J]. THERIOGENOLOGY, 2000, 53 (01) : 139 - 148
  • [3] Transgenically produced human antithrombin: Structural and functional comparison to human plasma-derived antithrombin
    Edmunds, T
    Van Patten, SM
    Pollock, J
    Hanson, E
    Bernasconi, R
    Higgins, E
    Manavalan, P
    Ziomek, C
    Meade, H
    McPherson, JM
    Cole, ES
    [J]. BLOOD, 1998, 91 (12) : 4561 - 4571
  • [4] Biotech industry faces new bottleneck
    Garber, K
    [J]. NATURE BIOTECHNOLOGY, 2001, 19 (03) : 184 - 185
  • [5] INHIBITION WITH LACTOFERRIN OF IN-VITRO INFECTION WITH HUMAN HERPES-VIRUS
    HASEGAWA, K
    MOTSUCHI, W
    TANAKA, S
    DOSAKO, S
    [J]. JAPANESE JOURNAL OF MEDICAL SCIENCE & BIOLOGY, 1994, 47 (02): : 73 - 85
  • [6] Kamerling J. P., 1989, MASS SPECTROMETRY, V1, P176
  • [7] KRIMPENFORT P, 1991, BIO-TECHNOL, V9, P844, DOI 10.1038/nbt0991-844
  • [8] Human lactoferrin and peptides derived from its N terminus are highly effective against infections with antibiotic-resistant bacteria
    Nibbering, PH
    Ravensbergen, E
    Welling, MM
    van Berkel, LA
    van Berkel, PHC
    Pauwels, EKJ
    Nuijens, JH
    [J]. INFECTION AND IMMUNITY, 2001, 69 (03) : 1469 - 1476
  • [9] Structure and Biological Actions of Lactoferrin
    Nuijens, Jan H.
    van Berkel, Patrick H. C.
    Schanbacher, Floyd L.
    [J]. JOURNAL OF MAMMARY GLAND BIOLOGY AND NEOPLASIA, 1996, 1 (03) : 285 - 295
  • [10] Characterization of recombinant human lactoferrin secreted in milk of transgenic mice
    Nuijens, JH
    vanBerkel, PHC
    Geerts, MEJ
    Hartevelt, PP
    deBoer, HA
    vanVeen, HA
    Pieper, FR
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (13) : 8802 - 8807