Peptidomic analysis of Chinese shrimp (Fenneropenaeus chinensis) hemolymph by magnetic bead-based MALDI-TOF MS

Baojie Wang; Mei Liu; Keyong Jiang; Guofan Zhang; Lei Wang

doi:10.1007/s00343-013-2076-4

Your Location：

Home >

Browse articles >

Peptidomic analysis of Chinese shrimp (Fenneropenaeus chinensis) hemolymph by magnetic bead-based MALDI-TOF MS

Updated：2023-05-16

- Peptidomic analysis of Chinese shrimp (Fenneropenaeus chinensis) hemolymph by magnetic bead-based MALDI-TOF MS
- Journal of Oceanology and Limnology Vol. 31, Issue 2, Pages: 407-415(2013)
- Affiliations：
  
  1. Institute of Oceanlogy Chinese Academy of Sciences
  2. Graduate University of Chinese Academy of Sciences
- Author bio：
- Funds：
- DOI：10.1007/s00343-013-2076-4
  CLC：
- Online First：07 March 2013，
  
  Published：2013
- Accepted：
Scan QR Code
Wang, B., Liu, M., Jiang, K. et al. Peptidomic analysis of Chinese shrimp (Fenneropenaeus chinensis) hemolymph by magnetic bead-based MALDI-TOF MS., Chin. J. Ocean. Limnol. 31, 407–415 (2013). https://doi.org/10.1007/s00343-013-2076-4
DOI：

Wang, B., Liu, M., Jiang, K. et al. Peptidomic analysis of Chinese shrimp (Fenneropenaeus chinensis) hemolymph by magnetic bead-based MALDI-TOF MS., Chin. J. Ocean. Limnol. 31, 407–415 (2013). https://doi.org/10.1007/s00343-013-2076-4 DOI：

摘要

Abstract

Peptides in shrimp hemolymph play an important role in the innate immune response. Analysis of hemolymph will help to detect and identify potential novel biomarkers of microbial infection. We used magnetic bead-based purification (ClinProt system) and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI-TOF MS) to characterize shrimp hemolymph peptides. Shrimp serum and plasma were used as the source of samples for comparative analysis

and it was found that serum was more suitable for shrimp hemolymph peptidomic analysis. To screen potential specific biomarkers in serum of immune-challenged shrimps

we applied magnetic bead-based MALDI-TOF MS to serum samples from 10 immune-challenged and 10 healthy shrimps. The spectra were analyzed using FlexAnalysis 3.0 and ClinProTools 2.1 software. Thirteen peptide peaks significantly different between the two groups were selected as candidate biomarkers of lipopolysaccharide (LPS)-infection. The diagnostic model established by genetic algorithm using five of these peaks was able to discriminate LPS-challenged shrimps from healthy control shrimps with a sensitivity of 90% and a specificity of 100%. Our approach in MALDITOF MS-based peptidomics is a powerful tool for screening bioactive peptides or biomarkers derived from hemolymph

and will help to enable a better understanding of the innate immune response of shrimps.

关键词

Keywords

references

Albrecht W. 2005. Clinprot, an expandable platform for biomarker discovery. Molecular and Cellular Proteomics, 4(8): S387–S387.

Antony S P, Singh I S B, Philip R. 2010. Molecular characterization of a crustin-like, putative antimicrobial peptide, Fi-crustin, from the Indian white shrimp, Fenneropenaeus indicus. Fish and Shellfish Immunology, 28(1): 216–220.

Baumann S, Ceglarek U, Fiedler G M, Lembcke J, Leichtle A, Thiery J. 2005. Standardized approach to proteome profiling of human serum based on magnetic bead separation and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Clinical Chemistry, 51(6): 973–980.

Bosso N, Chinello C, Picozzi S C M, Gianazza E, Mainini V, Galbusera C, Raimondo F, Perego R, Casellato S, Rocco F, Ferrero S, Bosari S, Mocarelli P, Kienle M G, Magni F. 2008. Human urine biomarkers of renal cell carcinoma evaluated by ClinProt. Proteomics Clinical Applications, 2(7–8): 1 036–1 046.

Cheng W, Tsai I H, Huang C J, Chiang P C, Cheng C H, Yeh M S. 2008. Cloning and characterization of hemolymph clottable proteins of kuruma prawn (Marsupenaeus japonicus) and white shrimp (Litopenaeus vannamei). Developmental and Comparative Immunology, 32(3): 265–274.

Chiou T T, Wu J L, Chen T T, Lu J K. 2005. Molecular cloning and characterization of cDNA of penaeidin-like antimicrobial peptide from tiger shrimp (Penaeus monodon). Marine Biotechnology, 7(2): 119–127.

Cuthbertson B J, Deterding L J, Williams J G, Tomer K B, Etienne K, Blackshear P J, Bullesbach E E, Grosse P S. 2008. Diversity in penaeidin antimicrobial peptide form and function. Developmental and Comparative Immunology, 32(3): 167–181.

FigueroaSoto C G, delaBarca A M C, VazquezMoreno L, HigueraCiapara I, YepizPlascencia G. 1997. Purification of hemocyanin from white shrimp (Penaeus vannamei Boone) by immobilized metal affinity chromatography. Comparative Biochemistry and Physiology B-Biochemistry and Molecular Biology, 117(2): 203–208.

Flegel T W, Sritunyalucksana K. 2011. Shrimp molecular responses to viral pathogens. Marine Biotechnology, 13(4): 587–607.

Hauton C, Brockton V, Smith V J. 2007. Changes in immune gene expression and resistance to bacterial infection in lobster (Homarus gammarus) post-larval stage VI following acute or chronic exposure to immune stimulating compounds. Molecular Immunology, 44(4): 443–450.

Huang B X, Zhang J Q, Xiang J H. 2008. Purification and primary identification of haemocyanin in the Chinese shrimp, Fenneropenaeus chinensis (Decapoda, Penaeoidea). Crustaceana, 81(7): 769–780.

Kang C, Wang J, Zhao X, Yang X, Shao H, Xiang J. 2004. Molecular cloning and expression analysis of Chpenaeidin, an antimicrobial peptide from Chinese shrimp, Fenneropenaeus chinensis. Fish and Shellfish Immunology, 16(4): 513–525.

Levy F, Bulet P, Ehret-Sabatier L. 2004. Proteomic analysis of the systemic immune response of Drosophila. Molecular and Cellular Proteomics, 3(2): 156–166.

Liu F S, Liu Y C, Li F H, Dong B, Xiang J H. 2005. Molecular cloning and expression profile of putative antilipopolysaccharide factor in Chinese shrimp (Fenneropenaeus chinensis). Marine Biotechnology, 7(6): 600–608.

Magni F, Van Der Burgt Y E M, Chinello C, Mainini V, Gianazza E, Squeo V, Deelder A M, Kienle M G. 2010. Biomarkers discovery by peptide and protein profiling in biological fluids based on functionalized magnetic beads purification and mass spectrometry. Blood Transfusion, 8: S92–S97.

Perazzolo L M, Lorenzini D M, Daffre S, Barracco M A. 2005. Purification and partial characterization of the plasma clotting protein from the pink shrimp Farfantepenaeus paulensis. Comparative Biochemistry and Physiology B-Biochemistry and Molecular Biology, 142(3): 302–307.

Qiu F, Liu H Y, Zhang X J, Tian Y P. 2009. Optimization of magnetic beads for MALDI-TOF MS analysis. Frontiers in Bioscience, 14: 3 712–3 723.

Robalino J, Almeida J S, McKillen D, Colglazier J, Trent H F, Chen Y A, Peck M E T, Browdy C L, Chapman R W, Warr G W, Gross P S. 2007. Insights into the immune transcriptome of the shrimp Litopenaeus vannamei: tissue-specific expression profiles and transcriptomic responses to immune challenge. Physiological Genomics, 29(1): 44–56.

Rowley A F, Powell A. 2007. Invertebrate immune systemsspecific, quasi-specific, or nonspecific? Journal of Immunology, 179(11): 7 209–7 214.

Schuerenbeg M, Luebbert C, Eickhoff H, Kalkum M, Lehrach H, Nordhoff E. 2000. Prestructured MALDI-MS sample supports. Analytical Chemistry, 72(15): 3 436–3 442.

Somboonwiwat K, Chaikeeratisak V, Wang H C, Lo C F, Tassanakajon A. 2010. Proteomic analysis of differentially expressed proteins in Penaeus monodon hemocytes after Vibrio harveyi infection. Proteome Science, 8: 39.

Sun J, Wang L, Wang B, Guo Z, Liu M, Jiang K, Luo Z. 2007. Purification and characterisation of a natural lectin from the serum of the shrimp Litopenaeus vannamei. Fish and Shellfish Immunology, 23(2): 292–299.

Sun J, Wang L, Wang B, Guo Z, Liu M, Jiang K, Tao R, Zhang G. 2008. Purification and characterization of a natural lectin from the plasma of the shrimp Fenneropenaeus chinensis. Fish and Shellfish Immunology, 25(3): 290–297.

Timms J F, Arslan-Low E, Gentry-Maharaj A, Luo Z, T’Jampens D, Podust V N, Ford J, Fung E T, Gammerman A, Jacobs I, Menon U. 2007. Preanalytic influence of sample handling on SELDI-TOF serum protein profiles. Clinical Chemistry, 53(4): 645–656.

Uttenweiler-Joseph S, Moniatte M, Lagueux M, Van Dorsselaer A, Hoffmann J A, Bulet P. 1998. Differential display of peptides induced during the immune response of Drosophila: A matrix-assisted laser desorption ionization time-of-flight mass spectrometry study. Proceedings of the National Academy of Sciences of the United States of America, 95(19): 11 342–11 347.

Vierstraete E, Verleyen P, De Loof A, Schoofs L. 2005. Differential proteomics for studying Drosophila immunity. Trends in Comparative Endocrinology and Neurobiology, 1040: 504–507.

West-Norager M, Kelstrup C D, Schou C, Hogdall E V, Hogdall C K, Heegaard N H H. 2007. Unravelling in vitro variables of major importance for the outcome of mass spectrometry-based serum proteomics. Journal of Chromatography B-Analytical Technologies in the Biomedical and Life Sciences, 847(1): 30–37.

Yao C, Wu C, Xiang J, Dong B. 2005. Molecular cloning and response to laminarin stimulation of arginine kinase in haemolymph in Chinese shrimp, Fenneropenaeus chinensis. Fish and Shellfish Immunology, 19(4): 317–329.

Views

Downloads

CSCD

Alert me when the article has been cited

Submit

Tools

Publicity Resources

Chromosome behavior of heat shock induced triploid inFenneropenaeus chinensis

Isolation, cloning and sequencing of AFLP markers related to disease-resistance traits inFenneropenaeus chinensis

Effects of salinity fluctuation amplitudes on growth, osmolarity, Na+-K+-ATPase activity and Hsp70 of juvenile Chinese shrimp Fenneropenaeus chinensis Osbeck

Genetic improvement on Chinese shrimp (Fenneropenaeus chinensis): growth and viability performance in F1 hybrids of different populations

Cloning, characterization, and expression analysis of the DEAD-box family genes, Fc-vasa and Fc-PL10a, in Chinese shrimp (Fenneropenaeus chinensis)

Related Author

Xiang Jianhai

Li Fuhua

Zhang Xiaojun

Dai Jixun

Kong Jie

Wang Weiji

Yue Zhiqin

Shuanglin Dong

Related Institution

Institute of Oceanology Chinese Academy of Sciences

Food Laboratory of qingdao Entry-Exit Inspection and Quarantine Bureau

College of Marine Life Science Ocean University of China

Key Laboratory for Sustainable Utilization of Marine Fisheries Resources Yellow Sea Fisheries Research Institute

The Key Laboratory of Mariculture Ministry of Education Ocean University of China

Address：Editorial Office of JOL, 88 Haijun Rd. Qingdao, 266000, China
Tel：+86-532-82898754 Email：jol@qdio.ac.cn
Technical support is provided by Beijing Founder electronics co., LTD 京ICP备09064830号-19 京公网安备11010802024621
It is recommended to read the content of this site in Chrome&IE9+. Please switch to extreme mode in browser 360.
Cookies We use cookies to help provide and enhance our service and tailor content. By continuing, you agree to the use of cookies.

⁰