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In-depth proteomic and glycomic analysis of the adult-stage Cooperia oncophora excretome/secretome

(2013) JOURNAL OF PROTEOME RESEARCH. 12(9). p.3900-3911
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Abstract
Cooperia oncophora is one of the most common intestinal parasitic nematodes in cattle worldwide. To date, C. oncophora infections are treated using broad-spectrum anthelmintics. However, during the past decade, reports of anthelmintic resistance in this parasite species have emerged worldwide, necessitating new avenues for its control, possibly through vaccination. In this frame, we analyzed the adult-stage C. oncophora excretome/secretome (ES), covering both the protein and glycan components, since this fraction constitutes the primary interface between parasite and host and may hold potential vaccine candidates. Two-dimensional gel electrophoretic separation of the ES material enabled the MALDI-TOF mass spectrometry (MS)-directed identification of 12 distinct proteins, grouped in three separate molecular weight fractions: (i) a high molecular weight fraction consisting of a double-domain activation-associated secreted protein (ASP), (ii) a midmolecular weight fraction predominantly containing a single-domain ASP, a thioredoxin peroxidase and innexin, and (iii) a low molecular weight protein pool essentially holding two distinct low molecular weight antigens. Further MS-driven glycan analysis mapped a variety of N-glycans to the midmolecular weight single-domain ASP, with Man(6)GlcNAc(2) oligomannosyl glycans as the major species. The predominance of the nonglycosylated double-domain ASP in the high-molecular weight fraction renders it ideal for advancement toward vaccine trials and development.
Keywords
glycomics, EXCRETORY-SECRETORY PRODUCTS, helminth proteomics, excretome/secretome, Cooperia oncophora, sequence analysis, RESISTANCE, NECATOR-AMERICANUS, ONCHOCERCA-VOLVULUS, SCHISTOSOMA-JAPONICUM, THIOREDOXIN PEROXIDASE, BRUGIA-MALAYI, FASCIOLA-HEPATICA, OSTERTAGIA-OSTERTAGI, GAP-JUNCTION PROTEINS

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Citation

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Chicago
Borloo, Jimmy, Jessie De Graef, Iris Peelaers, D Linh Nguyen, Makedonka Mitreva, Bart Devreese, Cornelis H Hokke, Jozef Vercruysse, Edwin Claerebout, and Peter Geldhof. 2013. “In-depth Proteomic and Glycomic Analysis of the Adult-stage Cooperia Oncophora Excretome/secretome.” Journal of Proteome Research 12 (9): 3900–3911.
APA
Borloo, J., De Graef, J., Peelaers, I., Nguyen, D. L., Mitreva, M., Devreese, B., Hokke, C. H., et al. (2013). In-depth proteomic and glycomic analysis of the adult-stage Cooperia oncophora excretome/secretome. JOURNAL OF PROTEOME RESEARCH, 12(9), 3900–3911.
Vancouver
1.
Borloo J, De Graef J, Peelaers I, Nguyen DL, Mitreva M, Devreese B, et al. In-depth proteomic and glycomic analysis of the adult-stage Cooperia oncophora excretome/secretome. JOURNAL OF PROTEOME RESEARCH. 2013;12(9):3900–11.
MLA
Borloo, Jimmy, Jessie De Graef, Iris Peelaers, et al. “In-depth Proteomic and Glycomic Analysis of the Adult-stage Cooperia Oncophora Excretome/secretome.” JOURNAL OF PROTEOME RESEARCH 12.9 (2013): 3900–3911. Print.
@article{5638639,
  abstract     = {Cooperia oncophora is one of the most common intestinal parasitic nematodes in cattle worldwide. To date, C. oncophora infections are treated using broad-spectrum anthelmintics. However, during the past decade, reports of anthelmintic resistance in this parasite species have emerged worldwide, necessitating new avenues for its control, possibly through vaccination. In this frame, we analyzed the adult-stage C. oncophora excretome/secretome (ES), covering both the protein and glycan components, since this fraction constitutes the primary interface between parasite and host and may hold potential vaccine candidates. Two-dimensional gel electrophoretic separation of the ES material enabled the MALDI-TOF mass spectrometry (MS)-directed identification of 12 distinct proteins, grouped in three separate molecular weight fractions: (i) a high molecular weight fraction consisting of a double-domain activation-associated secreted protein (ASP), (ii) a midmolecular weight fraction predominantly containing a single-domain ASP, a thioredoxin peroxidase and innexin, and (iii) a low molecular weight protein pool essentially holding two distinct low molecular weight antigens. Further MS-driven glycan analysis mapped a variety of N-glycans to the midmolecular weight single-domain ASP, with Man(6)GlcNAc(2) oligomannosyl glycans as the major species. The predominance of the nonglycosylated double-domain ASP in the high-molecular weight fraction renders it ideal for advancement toward vaccine trials and development.},
  author       = {Borloo, Jimmy and De Graef, Jessie and Peelaers, Iris and Nguyen, D Linh and Mitreva, Makedonka and Devreese, Bart and Hokke, Cornelis H and Vercruysse, Jozef and Claerebout, Edwin and Geldhof, Peter},
  issn         = {1535-3893},
  journal      = {JOURNAL OF PROTEOME RESEARCH},
  keyword      = {glycomics,EXCRETORY-SECRETORY PRODUCTS,helminth proteomics,excretome/secretome,Cooperia oncophora,sequence analysis,RESISTANCE,NECATOR-AMERICANUS,ONCHOCERCA-VOLVULUS,SCHISTOSOMA-JAPONICUM,THIOREDOXIN PEROXIDASE,BRUGIA-MALAYI,FASCIOLA-HEPATICA,OSTERTAGIA-OSTERTAGI,GAP-JUNCTION PROTEINS},
  language     = {eng},
  number       = {9},
  pages        = {3900--3911},
  title        = {In-depth proteomic and glycomic analysis of the adult-stage Cooperia oncophora excretome/secretome},
  url          = {http://dx.doi.org/10.1021/pr400114y},
  volume       = {12},
  year         = {2013},
}

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