Production of human papillomavirus type 16 E7 protein in Lactococcus lactis

被引：100
作者：
Bermúdez-Humarán, LG
Langella, P
Miyoshi, A
Gruss, A
Guerra, RT
de Oca-Luna, RM
Le Loir, Y
机构：
[1] INRA, Unite Rech Laitieres & Genet Appl, F-78352 Jouy En Josas, France
[2] Univ Autonoma Nuevo Leon, Fac Ciencias Biol, Lab Inmunol & Virol, San Nicolas De Los Garza, Nuevo Leon, Mexico
[3] Univ Fed Minas Gerais, Inst Ciencias Biol, Inst Biol Sci, Belo Horizonte, MG, Brazil
来源：
APPLIED AND ENVIRONMENTAL MICROBIOLOGY | 2002年 / 68卷 / 02期
关键词：
D O I：
10.1128/AEM.68.2.917-922.2002
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 E7 protein of human papillomavirus type 16 was produced in Lactococcus lactis. Secretion allowed higher production yields than cytoplasmic production. In stationary phase, amounts of cytoplasmic E7 were reduced, while amounts of secreted E7 increased, suggesting a phase-dependent intracellular proteolysis. Fusion of E7 to the staphylococcal nuclease, a stable protein, resulted in a highly stable cytoplasmic protein. This work provides new candidates for development of viral screening systems and for oral vaccine against cervical cancer.
引用
收藏
页码：917 / 922
页数：6
相关论文
共 43 条
[1]   EXPRESSION OF HUMAN PAPILLOMAVIRUS PROTEINS IN YEAST SACCHAROMYCES CEREVISIAE [J].
CARTER, JJ ;
YAEGASHI, N ;
JENISON, SA ;
GALLOWAY, DA .
VIROLOGY, 1991, 182 (02) :513-521
[2]   Induction of mucosal immune response after intranasal or oral inoculation of mice with Lactococcus lactis producing bovine beta-lactoglobulin [J].
Chatel, JM ;
Langella, P ;
Adel-Patient, K ;
Commissaire, J ;
Wal, JM ;
Corthier, G .
CLINICAL AND DIAGNOSTIC LABORATORY IMMUNOLOGY, 2001, 8 (03) :545-551
[3]   SYNTHETIC SITES FOR TRANSCRIPTION TERMINATION AND A FUNCTIONAL COMPARISON WITH TRYPTOPHAN OPERON TERMINATION SITES INVITRO [J].
CHRISTIE, GE ;
FARNHAM, PJ ;
PLATT, T .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES, 1981, 78 (07) :4180-4184
[4]   Gene expression systems for lactic acid bacteria [J].
de Vos, WM .
CURRENT OPINION IN MICROBIOLOGY, 1999, 2 (03) :289-295
[5]   Controlled gene expression systems for Lactococcus lactis with the food-grade inducer nisin [J].
deRuyter, PGGA ;
Kuipers, OP ;
deVos, WM .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1996, 62 (10) :3662-3667
[6]   Design of a protein-targeting system for lactic acid bacteria [J].
Dieye, Y ;
Usai, S ;
Clier, F ;
Gruss, A ;
Piard, JC .
JOURNAL OF BACTERIOLOGY, 2001, 183 (14) :4157-4166
[7]   Bovine rotavirus nonstructural protein 4 produced by Lactococcus lactis is antigenic and immunogenic [J].
Enouf, V ;
Langella, P ;
Commissaire, J ;
Cohen, J ;
Corthier, G .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2001, 67 (04) :1423-1428
[8]   ClpP participates in the degradation of misfolded protein in Lactococcus lactis [J].
Frees, D ;
Ingmer, H .
MOLECULAR MICROBIOLOGY, 1999, 31 (01) :79-87
[9]   Inactivation of a gene that is highly conserved in Gram-positive bacteria stimulates degradation of non-native proteins and concomitantly increases stress tolerance in Lactococcus lactis [J].
Frees, D ;
Varmanen, P ;
Ingmer, H .
MOLECULAR MICROBIOLOGY, 2001, 41 (01) :93-103
[10]   Gene cloning and expression and secretion of Listeria monocytogenes bacteriophage-lytic enzymes in Lactococcus lactis [J].
Gaeng, S ;
Scherer, S ;
Neve, H ;
Loessner, MJ .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2000, 66 (07) :2951-2958
12345