The secreted fructose 1,6-bisphosphate aldolase as a broad spectrum vaccine candidate against pathogenic bacteria in aquaculture

被引:18
作者
Sun, Zhongyang [1 ]
Shen, Binbing [1 ]
Wu, Haizhen [1 ]
Zhou, Xiangyu [1 ]
Wang, Qiyao [1 ,3 ]
Xiao, Jingfan [1 ,3 ]
Zhang, Yuanxing [1 ,2 ,3 ]
机构
[1] E China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China
[2] Shanghai Collaborat Innovat Ctr Biomfg Technol, Shanghai 200237, Peoples R China
[3] Shanghai Engn Res Ctr Mariculture Anim Vaccines, Shanghai 200237, Peoples R China
基金
国家高技术研究发展计划(863计划);
关键词
FBA; Locations; Cross-protection; Aquatic pathogenic bacteria; Broad spectrum vaccine; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; ESCHERICHIA-COLI; STREPTOCOCCUS-PNEUMONIAE; VIBRIO-ANGUILLARUM; EDWARDSIELLA-TARDA; IMMUNE-RESPONSE; PROTEIN; EXPRESSION; VIRULENCE; ANTIGEN;
D O I
10.1016/j.fsi.2015.08.001
中图分类号
S9 [水产、渔业];
学科分类号
0908 ;
摘要
The development of aquaculture has been hampered by different aquatic pathogens that can cause edwardsiellosis, vibriosis, or other diseases. Therefore, developing a broad spectrum vaccine against different fish diseases is necessary. In this study, fructose 1,6-bisphosphate aldolase (FBA), a conserved enzyme in the glycolytic pathway, was demonstrated to be located in the non-cytoplasmic components of five aquatic pathogenic bacteria and exhibited remarkable protection and cross-protection against these pathogens in turbot and zebrafish. Further analysis revealed that sera sampled from vaccinated turbot had a high level of specific antibody and bactericidal activity against these pathogens. Meanwhile, the increased expressions of immune response-related genes associated with antigen recognition and presentation indicated that the adaptive immune response was effectively aroused. Taken together, our results suggest that FBA can be utilized as a broad-spectrum vaccine against various pathogenic bacteria of aquaculture in the future. (C) 2015 Elsevier Ltd. All rights reserved.
引用
收藏
页码:638 / 647
页数:10
相关论文
共 38 条
  • [1] Secretion of the housekeeping protein glyceraldehyde-3-phosphate dehydrogenase by the LEE-encoded type III secretion system in enteropathogenic Escherichia coli
    Aguilera, Laura
    Ferreira, Elaine
    Gimenez, Rosa
    Jose Fernandez, Francisco
    Taules, Marta
    Aguilar, Juan
    Cristina Vega, M.
    Badia, Josefa
    Baldoma, Laura
    [J]. INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY, 2012, 44 (06) : 955 - 962
  • [2] Amend D.F., 1981, Environ. Sci., P447, DOI DOI 10.1111/J.1749-7345.1983.TB00082.X
  • [3] α-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface
    Bergmann, S
    Rohde, M
    Chhatwal, GS
    Hammerschmidt, S
    [J]. MOLECULAR MICROBIOLOGY, 2001, 40 (06) : 1273 - 1287
  • [4] Ubiquitylation in innate and adaptive immunity
    Bhoj, Vijay G.
    Chen, Zhijian J.
    [J]. NATURE, 2009, 458 (7237) : 430 - 437
  • [5] Flamingo cadherin:: A putative host receptor for Streptococcus pneumoniae
    Blau, Karin
    Portnoi, Maxim
    Shagan, Marilou
    Kaganovich, Antonina
    Rom, Slava
    Kafka, Daniel
    Caspi, Vered Chalifa
    Porgador, Angel
    Givon-Lavi, Noga
    Gershoni, Jonathan M.
    Dagan, Ron
    Nebenzahl, Yaffa Mizrachi
    [J]. JOURNAL OF INFECTIOUS DISEASES, 2007, 195 (12) : 1828 - 1837
  • [6] Glycolytic and Non-glycolytic Functions of Mycobacterium tuberculosis Fructose-1,6-bisphosphate Aldolase, an Essential Enzyme Produced by Replicating and Non-replicating Bacilli
    de la Paz Santangelo, Maria
    Gest, Petra M.
    Guerin, Marcelo E.
    Coincon, Mathieu
    Ha Pham
    Ryan, Gavin
    Puckett, Susan E.
    Spencer, John S.
    Gonzalez-Juarrero, Mercedes
    Daher, Racha
    Lenaerts, Anne J.
    Schnappinger, Dirk
    Therisod, Michel
    Ehrt, Sabine
    Sygusch, Jurgen
    Jackson, Mary
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2011, 286 (46) : 40219 - 40231
  • [7] Role of secreted glyceraldehyde-3-phosphate dehydrogenase in the infection mechanism of enterohemorrhagic and enteropathogenic Escherichia coli:: Interaction of the extracellular enzyme with human plasminogen and fibrinogen
    Egea, L.
    Aguilera, L.
    Gimenez, R.
    Sorolla, M. A.
    Aguilar, J.
    Badia, J.
    Baldoma, L.
    [J]. INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY, 2007, 39 (06) : 1190 - 1203
  • [8] Bacterial Virulence in the Moonlight: Multitasking Bacterial Moonlighting Proteins Are Virulence Determinants in Infectious Disease
    Henderson, Brian
    Martin, Andrew
    [J]. INFECTION AND IMMUNITY, 2011, 79 (09) : 3476 - 3491
  • [9] The role of the interleukin-10 subfamily members in immunoglobulin production by human B cells
    Hummelshoj, L.
    Ryder, L. P.
    Poulsen, L. K.
    [J]. SCANDINAVIAN JOURNAL OF IMMUNOLOGY, 2006, 64 (01) : 40 - 47
  • [10] Incorporation of heterologous outer membrane and periplasmic proteins into Escherichia coli outer membrane vesicles
    Kesty, NC
    Kuehn, MJ
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (03) : 2069 - 2076