Immunoproteomic Assay of Antigenic Surface Proteins in Streptococcus equi ssp. zooepidemicus

doi:10.1016/S1671-2927(11)60099-0

Journal of Integrative Agriculture ›› 2011, Vol. 10 ›› Issue (7): 1096-1105.DOI: 10.1016/S1671-2927(11)60099-0

Immunoproteomic Assay of Antigenic Surface Proteins in Streptococcus equi ssp. zooepidemicus

1Key Laboratory of Animal Disease Diagnostic and Immunology, Ministry of Agriculture/College of Veterinary Medicine, Nanjing Agricultural University

收稿日期:2010-07-26 出版日期:2011-07-21 发布日期:2011-08-14
通讯作者: Correspondence FAN Hong-jie, Professor, Tel: +86-25-843965328, Fax: +86-25-84396517, E-mail: fhj@njau.edu.cn
作者简介:MAO Ying, MSc, E-mail: maoying_00@yahoo.com.cn

Immunoproteomic Assay of Antigenic Surface Proteins in Streptococcus equi ssp. zooepidemicus

1Key Laboratory of Animal Disease Diagnostic and Immunology, Ministry of Agriculture/College of Veterinary Medicine, Nanjing Agricultural University

Received:2010-07-26 Online:2011-07-21 Published:2011-08-14
Contact: Correspondence FAN Hong-jie, Professor, Tel: +86-25-843965328, Fax: +86-25-84396517, E-mail: fhj@njau.edu.cn
About author:MAO Ying, MSc, E-mail: maoying_00@yahoo.com.cn

摘要/Abstract

摘要： Streptococcus equi ssp. zooepidemicus (S. zooepidemicus) is a zoonotic pathogen with worldwide distribution. Lackingsuitable vaccine and virulent maker is still bottleneck to control this infection. An immunoproteomic approach has beenused to screen the membrane-associated and cell wall-associated proteins of S. zooepidemicus isolate in China CY todiscover vaccine candidate antigens and therapeutic agents. Finally, 11 membrane-associated proteins, and 13 cell wallassociatedproteins were successfully identified. BLAST (www.sanger.ac.uk) results also indicated that nucleotidesequences of majority identified proteins shared high homology (>60%) with S. zooepidemicus, except for AC1-3, AC5,AC8, and AC13. Moreover, genes for 7 of the identified proteins were detected from CY; compared with ST171, 3 of them(AM1, AM8 and AC11) were only found in virulent strains (CY). All of the proteins identified in this study remain not tobe reported in S. zooepidemicus. Some of the proteins serve a vital role in the immune system and reproduction of hostspecies according to available data, while the functions of the rest were seldom researched.

Abstract: Streptococcus equi ssp. zooepidemicus (S. zooepidemicus) is a zoonotic pathogen with worldwide distribution. Lackingsuitable vaccine and virulent maker is still bottleneck to control this infection. An immunoproteomic approach has beenused to screen the membrane-associated and cell wall-associated proteins of S. zooepidemicus isolate in China CY todiscover vaccine candidate antigens and therapeutic agents. Finally, 11 membrane-associated proteins, and 13 cell wallassociatedproteins were successfully identified. BLAST (www.sanger.ac.uk) results also indicated that nucleotidesequences of majority identified proteins shared high homology (>60%) with S. zooepidemicus, except for AC1-3, AC5,AC8, and AC13. Moreover, genes for 7 of the identified proteins were detected from CY; compared with ST171, 3 of them(AM1, AM8 and AC11) were only found in virulent strains (CY). All of the proteins identified in this study remain not tobe reported in S. zooepidemicus. Some of the proteins serve a vital role in the immune system and reproduction of hostspecies according to available data, while the functions of the rest were seldom researched.

MAO Ying, FAN Hong-jie, ZHOU Yong-hua, LU Cheng-ping. Immunoproteomic Assay of Antigenic Surface Proteins in Streptococcus equi ssp. zooepidemicus[J]. Journal of Integrative Agriculture, 2011, 10(7): 1096-1105.

参考文献

[1]       Buchmeier N A, Heffron F. 1990. Induction of Salmonella stress proteins upon infection of macrophages. Science, 248, 730-732.
[2]       Bumann D, Holland P, Siejak F, Koesling J, Sabarth N, Lamer S,Zimny-Arndt U, Jungblut P R, Meyer T F. 2002. Acomparison of murine and human immunoproteomes ofHelicobacter pylori validates the preclinical murine infectionmodel for antigen screening. Infection and Immunity, 70, 6494-6498.
[3]       Causey R C, Weber J A, Emmans E E, Stephenson L A, HomolaA D, Knapp K R, Crowley I F, Wooley N A. 2006. Theequine immune response to Streptococcus equi subspecieszooepidemicus during uterine infection. The VeterinaryJournal, 172, 248-257.
[4]       Cole J N, Ramirez R D, Currie B J, Cordwell S J, Djordjevic S P,Walker M J. 2005. Surface analyses and immune reactivitiesof major cell wall-associated proteins of group astreptococcus. Infection and Immunity, 73, 3137-3146.
[5]       Donoghue P R, McManus C A, O’Donoghue N M, PenningtonS R, Dunn M J. 2006. CyDye immunoblotting for proteomics:co-detection of specific immunoreactive and total proteinprofiles. Proteomics, 24, 6400-6404.
[6]       Esgleas M, Li Y, Hancock M A, Harel J, Dubreuil J D, GottschalkM. 2008. Isolation and characterization of alpha-enolase, anovel fibronectin-binding protein from Streptococcus suis.Microbiology, 154, 2668-2679.
[7]       Evarsson A A, Brazhnikov E, Garber M, Zheltonosova J,Chirgadze Y, SalKaradaghi S, Svensson L A, Liljas A. 1994.Three-dimensional structure of the ribosomal translocase:elongation factor G from Thermus thermophilus. EMBOJournal, 13, 3669-3677.
[8]       Feng Z G, Hu J S. 1977. Outbreak of swine Streptococcosis inSichan Province and identification of pathogen. AnimalHusbandry and Vertinary Medicine Letters, 2, 7-12.
[9]       (inChinese)Gahan C G M, O’Mahony J, Hill C. 2001. Characterization ofthe groESL operon in listeria monocytogenes: Utilization oftwo reporter systems (gfp and hly) for evaluating in vivoexpression. Infection and Immunity, 69, 3924-3932.
[10]    Ge J, Catt D M, Gregory R L. 2004. Streptococcus mutanssurface alpha-enolase binds salivary mucin MG2 and humanplasminogen. Infection and Immunity, 72, 6748-6752.
[11]    Jing H B, Yuan J, Wang J, Yuan Y, Zhu L, Liu X K, Zheng Y L,Wei K H, Zhang X M, Geng H R, et al. 2008. Proteomeanalysis of Streptococcus suis serotype 2. Proteomics, 8,333-349.
[12]    Jonsson H, Lindmark H, Guss B. 1995. A protein G-related cellsurface protein in Streptococcus zooepidemicus. Infection andImmunity, 63, 2968-2975.
[13]    Kannan N, Chander P, Ghosh P, Vishveshwara S, Chatterji D.2001. Stabilizing interactions in the dimer interface of alphasubunitin Escherichia coli RNA polymerase: a graph spectraland point mutation study. Protein Science, 10, 46-54.
[14]    Laemmli U K. 1970. Cleavage of structural proteins during theassembly of the head of bacteriophage T4. Nature, 227, 680-685.
[15]    Lestrate P, Dricot A, Delrue R M, Lambert C, Martinelli V,Bolle D, Letesson J, Tibor A. 2003. Attenuated signaturetaggedmutagenesis mutants of Brucella melitensis identifiedduring the acute phase of infection in mice. Infection andImmunity, 71, 7053-7060.
[16]    Lindmark H, Jacobsson K, Frykberg L, Guss B. 1996. Fibronectinbindingprotein of Streptococcus equi subsp. zooepidemicus.Infection and Immunity, 64, 3993-3999.
[17]    Maass M, Dalhoff K. 1994. Comparison of sample preparationmethods for detection of Chlamydia pneumoniae inbronchoalveolar lavage fluid by PCR. Journal of ClinicalMicrobiology, 32, 2616-2619.
[18]    Maria S C, Luca B, Maurizio C, Roberto R, Barbara M, VitalianoP, Giulio R. 1999. Identification of immunoreactive proteinsof Chlamydia trachomatis by Western blot analysis of a twodimensionalelectrophoresis map with patient sera.Electrophoresis, 20, 2269-2279.Pancholi V. 2001. Multifunctional alpha-enolase: its role indiseases. cellular and molecular life sciences, 58, 902-920.
[19]    Pancholi V, Fischetti V A. 1998. Alpha-enolase, a novel strongplasmin(ogen) binding protein on the surface of pathogenicstreptococci. Journal of Biological Chemistry, 273, 14503-14515.
[20]    Rodriguez-Ortega M J, Norais N, Bensi G, Liberatori S, Capo S,Mora M, Scarselli M, Doro F, Ferrari G, Garaguso I, et al.2006. Characterization and identification of vaccine candidateproteins through analysis of the group A Streptococcussurface proteome. Nature Biotechnology, 24, 191-197.
[21]    Schäfer K, Magnusson U, Scheffel F, Schiefner A, Sandgren M OJ, Diederichs K, Welte W, Hülsmann A, Schneider E,Mowbray S L. 2004. X-ray structures of the maltosemaltodextrin-binding protein of the thermoacidophilicbacterium Alicyclobacillus acidocaldarius provide insight intoacid stability of proteins. Journal of Molecular Biology, 335,261-274.
[22]    Schomburg D, Schomburg I, Chang A. 2007. FMNadenylyltransferase. In: Schomburg D, Schomburg I, eds.,Hand Book of Enzymes. 2nd ed. vol. 38. Springer, Heidelberg.pp. 63-70.
[23]    Segal R, Ron E Z. 1996. Regulation and organization of the groEand dnaK operons in Eubacteria. FEMS Microbiology Letters,138, 1-10.
[24]    Shelburne S A III, Fang H, Okorafor N, Sumby P, Sitkiewicz I,Keith D, Patel P, Austin C, Graviss E A, Musser J M, et al.2007. MalE of group A Streptococcus participates in the rapid transport of maltotriose and longer maltodextrins.Journal of Bacteriology, 189, 2610-2617.
[25]    Shelburne S A III, Sumby P, Sitkiewicz I, Okorafor N, GranvilleC, Patel P, Voyich J, Hull R, DeLeo F R, Musser J M. 2006.Maltodextrin utilization plays a key role in the ability ofgroup A Streptococcus to colonize the oropharynx. Infectionand Immunity, 74, 4605-4614.
[26]    Timoney J F, Walker J, Zhou M, Ding J. 1995. Cloning andsequence analysis of a protective M-like protein gene fromStreptococcus equi subsp. zooepidemicus. Infection andImmunity, 63, 1440-1445.
[27]    Tsugawa H, Ito H, Ohshima M, Okawa Y. 2007. Cell adherencepromotedactivity of Plesiomonas shigelloides groEL. Journalof Medical Microbiology, 56, 23-29.
[28]    Wang J, Ying T, Wang H, Shi Z X, Li M Z, He K, Feng E L, WangJ, Yuan J, Li T, et al. 2005. 2-D reference map of Bacillusanthracis vaccine strain A16R proteins. Proteomics, 5, 4488-4495.
[29]    Wang Y, Yang L, Xu H, Li Q, Ma Z, Chu C. 2005. Differentialproteomic analysis of proteins in wheat spikes induced byFusarium graminearum. Proteomics, 5, 4496-4503.
[30]    Winterhoff N, Goethe R, Gruening P, Rohde M, Kalisz H, SmithH E, Valentin-Weigand P. 2002. Identification andcharacterization of two temperature-induced surfaceassociatedproteins of Streptococcus suis with high homologiesto members of the arginine deiminase system of Streptococcuspyogenes. Journal of Bacteriology, 184, 6768-6776.
[31]    Wistedt A C, Ringdahl U, Muller-Esterl W, Sjobring U. 1995.Identification of a plasminogen-binding motif in PAM, abacterial surface protein. Molecular Microbiology, 18, 569-578.
[32]    World Health Organization. 2005. Outbreak associated withStreptococcus suis in pigs, China. Weekly EpidemiologicalRecord, 80, 269-270.
[33]    Zhang W, Lu C P. 2007a. Immunoproteomics of extracellularproteins of Chinese virulent strains of Streptococcus suistype 2. Proteomics, 24, 4468-4476.
[34]   Zhang W, Lu C P. 2007b. Immunoproteomic assay of membraneassociatedproteins of Streptococcus suis type 2 China vaccinestrain HA9801. Zoonoses Public Health, 5, 253-259.

Immunoproteomic Assay of Antigenic Surface Proteins in Streptococcus equi ssp. zooepidemicus

Immunoproteomic Assay of Antigenic Surface Proteins in Streptococcus equi ssp. zooepidemicus

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