The identification of surface proteins of Burkholderia pseudomallei

被引:41
作者
Harding, Sarah V.
Sarkar-Tyson, Mitali
Smither, Sophie J.
Atkins, Timothy P.
Oyston, Petra C. F.
Brown, Katherine A.
Liu, Yichun
Wait, Robin
Titball, Richard W.
机构
[1] Dstl, Salisbury SP4 0JQ, Wilts, England
[2] CMMI, Imperial Coll London, Div Cell & Mol Biol, London SW7 2AZ, England
[3] Natl Lab DSO, DMERI DSO, Singapore 117510, Singapore
[4] Univ London Imperial Coll Sci Technol & Med, Fac Med, Kennedy Inst Rheumatol Div, London W6 8LH, England
关键词
Burkholderia pseudoluallei; proteomics; vaccine;
D O I
10.1016/j.vaccine.2006.12.006
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
Burkholderia pseudoinallei, the causative agent of the disease mehoidosis is a human pathogen endemic in Northern Australia and South-East Asia. At present there is no available vaccine or effective treatment for this disease. Surface proteins play crucial roles in the host-pathogen interaction and have been exploited as vaccine candidates and diagnostic targets. Therefore, we wished to identify immunogenic surface proteins of B. pseudomallei. To this end we used two proteomic-based approaches in parallel: a biotinylation approach for the detection of surface located proteins identified 35 proteins, while screening with human sera identified 12 immunogenic proteins. Nine of these proteins were identified by both methods indicating that they may be both surface located and immunogenic: these proteins will be evaluated further as vaccine candidates and diagnostic targets. (c) 2007 Elsevier Ltd. All rights reserved.
引用
收藏
页码:2664 / 2672
页数:9
相关论文
共 36 条
  • [1] Improved prediction of signal peptides: SignalP 3.0
    Bendtsen, JD
    Nielsen, H
    von Heijne, G
    Brunak, S
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 2004, 340 (04) : 783 - 795
  • [2] INVIVO LABELING OF ESCHERICHIA-COLI CELL-ENVELOPE PROTEINS WITH N-HYDROXYSUCCINIMIDE ESTERS OF BIOTIN
    BRADBURNE, JA
    GODFREY, P
    CHOI, JH
    MATHIS, JN
    [J]. APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1993, 59 (03) : 663 - 668
  • [3] Rapid screening of highly efficient vaccine candidates by immunoproteomics
    Chen, ZJ
    Peng, B
    Wang, SY
    Peng, XX
    [J]. PROTEOMICS, 2004, 4 (10) : 3203 - 3213
  • [4] Surface analyses and immune reactivities of major cell wall-associated proteins of group A streptococcus
    Cole, JN
    Ramirez, RD
    Currie, BJ
    Cordwell, SJ
    Djordjevic, SP
    Walker, MJ
    [J]. INFECTION AND IMMUNITY, 2005, 73 (05) : 3137 - 3146
  • [5] Elongation factor Tu and E1 β subunit of pyruvate dehydrogenase complex act as fibronectin binding proteins in Mycoplasma pneumoniae
    Dallo, SF
    Kannan, TR
    Blaylock, MW
    Baseman, JB
    [J]. MOLECULAR MICROBIOLOGY, 2002, 46 (04) : 1041 - 1051
  • [6] Gharahdaghi F, 1999, ELECTROPHORESIS, V20, P601, DOI 10.1002/(SICI)1522-2683(19990301)20:3<601::AID-ELPS601>3.0.CO
  • [7] 2-6
  • [8] Cell surface-associated elongation factor Tu mediates the attachment of Lactobacillus johnsonii NCC533 (La1) to human intestinal cells and mucins
    Granato, D
    Bergonzelli, GE
    Pridmore, RD
    Marvin, L
    Rouvet, M
    Corthésy-Theulaz, IE
    [J]. INFECTION AND IMMUNITY, 2004, 72 (04) : 2160 - 2169
  • [9] Protection against murine listeriosis by an attenuated recombinant Salmonella typhimurium vaccine strain that secretes the naturally somatic antigen superoxide dismutase
    Hess, J
    Dietrich, G
    Gentschev, I
    Miko, D
    Goebel, W
    Kaufmann, SHE
    [J]. INFECTION AND IMMUNITY, 1997, 65 (04) : 1286 - 1292
  • [10] Profiling of the cell surface proteome
    Jang, JH
    Hanash, S
    [J]. PROTEOMICS, 2003, 3 (10) : 1947 - 1954