Characterization of DNase activity and gene in Streptococcus suis and evidence for a role as virulence factor

详细信息    查看全文

• 作者：Bruno Haas (1)
  Laetitia Bonifait (1)
  Katy Vaillancourt (1)
  Steve J Charette (2) (3) (4) (5)
  Marcelo Gottschalk (5) (6)
  Daniel Grenier (1) (5)
  
  1. Groupe de Recherche en 脡cologie Buccale (GREB) ; Facult茅 de M茅decine Dentaire ; Universit茅 Laval ; 2420 Rue de la Terrasse ; Quebec City ; Quebec ; G1V 0A6 ; Canada
  2. Institut de Biologie Int茅grative et des Syst猫mes (IBIS) ; Quebec City ; Quebec ; Canada
  3. Centre de Recherche de l鈥橧nstitut Universitaire de Cardiologie et de Pneumologie de Qu茅bec (CRIUCPQ) ; H么pital Laval ; Quebec City ; Quebec ; Canada
  4. D茅partement de Biochimie ; de Microbiologie et de Bio-Informatique ; Facult茅 des Sciences et de G茅nie ; Universit茅 Laval ; Quebec City ; Quebec ; Canada
  5. Centre de Recherche en Infectiologie Porcine et Avicole (CRIPA) ; Fonds de Recherche du Qu茅bec - Nature et Technologies (FRQNT) ; Saint-Hyacinthe ; Quebec ; Canada
  6. Groupe de Recherche sur les Maladies Infectieuses du Porc (GREMIP) ; Facult茅 de M茅decine V茅t茅rinaire ; Universit茅 de Montr茅al ; Saint-Hyacinthe ; Quebec ; Canada
  
• 关键词：Streptococcus suis ; nuclease ; DNase activity ; Virulence factor ; SsnA
• 刊名：BMC Research Notes
• 出版年：2014
• 出版时间：December 2014
• 年：2014
• 卷：7
• 期：1
• 全文大小：620 KB
• 参考文献：1. Gottschalk, M Streptococcosis. In: Karriger, LRA, Schwartz, KJ, Stevenson, G, Zimmerman, J eds. (2012) Diseases of swine. Wiley Publishers, NJ, USA, pp. 841-855
  2. Gottschalk, M, Segura, M, Xu, J (2007) Streptococcus suis infections in humans: the Chinese experience and the situation in North America. Anim Health Res Rev 8: pp. 29-45 CrossRef
  3. Wertheim, HFL, Nghia, HDT, Taylor, W, Schultsz, C (2009) Streptococcus suis: an emerging human pathogen. Clin Infect Dis 48: pp. 617-625 CrossRef
  4. Yu, H, Jing, H, Chen, Z, Zheng, H, Zhu, X, Wang, H, Wang, S, Liu, L, Zu, R, Luo, L, Xiang, N, Liu, H, Liu, X, Shu, Y, Lee, SS, Chuang, SK, Wang, Y, Xu, J, Yang, W (2006) Human Streptococcus suis outbreak, Sichuan, China. Emerg Infect Dis 12: pp. 914-920 CrossRef
  5. Staats, JJ, Feder, I, Okwumabua, O, Chengappa, MM (1997) Streptococcus suis: past and present. Vet Res Commun 21: pp. 381-407 CrossRef
  6. King, SJ, Leigh, JA, Heath, PJ, Luque, I, Tarradas, C, Dowson, CG, Whatmore, AM (2002) Development of a multilocus sequence typing scheme for the pig pathogen Streptococcus suis: identification of virulent clones and potential capsular serotype exchange. J Clin Microbiol 40: pp. 3671-3680 CrossRef
  7. Fittipaldi, N, Xu, JG, Lacouture, S, Tharavichitkul, P, Osaki, M, Sekizaki, T, Takamatsu, D, Gottschalk, M (2011) Lineage and virulence of Streptococcus suis serotype 2 isolates from North America. Emerg Infect Dis 17: pp. 2239-2244 CrossRef
  8. Fittipaldi, N, Segura, M, Grenier, D, Gottschalk, M (2012) Virulence factors involved in the pathogenesis of the infection caused by the swine pathogen and zoonotic agent Streptococcus suis. Future Microbiol 7: pp. 259-279 CrossRef
  9. Charland, N, Harel, J, Kobisch, M, Lacasse, S, Gottschalk, M (1998) Streptococcus suis serotype 2 mutants deficient in capsular expression. Microbiology 144: pp. 325-332 CrossRef
  10. Smith, HE, Damman, M, van der Velde, J, Wagenaar, F, Wisselink, HJ, Stockhofe-Zurwieden, N, Smits, MA (1999) Identification and characterization of the cps locus of Streptococcus suis serotype 2: the capsule protects against phagocytosis and is an important virulence factor. Infect Immun 67: pp. 1750-1756
  11. Tanabe, SI, Bonifait, L, Fittipaldi, N, Grignon, L, Gottschalk, M, Grenier, D (2010) Pleiotropic effects of polysaccharide capsule loss on selected biological properties of Streptococcus suis. Can J Vet Res 74: pp. 65-70
  12. Mulcahy, H, Charron-Mazenod, L, Lewenza, S (2010) Pseudomonas aeruginosa produces an extracellular deoxyribonuclease that is required for utilization of DNA as a nutrient source. Environ Microbiol 12: pp. 1621-1629
  13. Mann, EE, Rice, KC, Boles, BR, Endres, JL, Ranjit, D, Chandramohan, L, Tsang, LH, Smeltzer, MS, Horswill, AR, Bayles, KW (2009) Modulation of eDNA release and degradation affects Staphylococcus aureus biofilm maturation. PLoS ONE 4: pp. e5822 CrossRef
  14. Berends, ETM, Horswill, AR, Haste, NM, Monestier, M, Nizet, V, von Kockritz-Blickwede, M (2010) Nuclease expression by Staphylococcus aureus facilitates escape from neutrophil extracellular traps. J Innate Immun 2: pp. 576-586 CrossRef
  15. Fontaine, MC, Perez-Casal, J, Willson, PJ (2004) Investigation of a novel DNase of Streptococcus suis serotype 2. Infect Immun 72: pp. 774-781 CrossRef
  16. Gomez-Gascon, L, Luque, I, Olaya-Abril, A, Jimenez-Munguia, I, Orbegozo-Medina, RA, Peralbo, E, Tarradas, C, Rodriguez-Ortega, MJ (2012) Exploring the pan-surfome of Streptococcus suis: looking for common protein antigens. J Proteomics 75: pp. 5654-5666 CrossRef
  17. de Buhr, N, Neumann, A, Jerjomiceva, N, von Kockritz-Blickwede, M, Baums, CG (2014) Streptococcus suis DNase SsnA contributes to degradation of neutrophil extracellular traps (NETs) and evasion of NET-mediated antimicrobial activity. Microbiology 160: pp. 385-395 CrossRef
  18. Choi, SJ, Szoka, FC (2000) Fluorometric determination of deoxyribonuclease I activity with PicoGreen. Anal Biochem 281: pp. 95-97 CrossRef
  19. Slater, JD, Allen, AG, May, JP, Bolitho, S, Lindsay, H, Maskell, DJ (2003) Mutagenesis of Streptococcus equi and Streptococcus suis by transposon Tn917. Vet Microbiol 93: pp. 197-206 CrossRef
  20. Bonifait, L, Dominguez-Punaro, MD, Vaillancourt, K, Bart, C, Slater, J, Frenette, M, Gottschalk, M, Grenier, D (2010) The cell envelope subtilisin-like proteinase is a virulence determinant for Streptococcus suis. BMC Microbiol 10: pp. 42 CrossRef
  21. Bonifait, L, Charette, SJ, Filion, G, Gottschalk, M, Grenier, D (2011) Amoeba host model for evaluation of Streptococcus suis virulence. Appl Environ Microb 77: pp. 6271-6273 CrossRef
  22. Bonifait, L, Grenier, D (2011) The SspA subtilisin-like protease of Streptococcus suis triggers a pro-inflammatory response in macrophages through a non-proteolytic mechanism. BMC Microbiol 11: pp. 47 CrossRef
  23. Gadi, J, Ruthala, K, Kong, KA, Park, HW, Kim, MH (2009) The third helix of the Hoxc8 homeodomain peptide enhances the efficiency of gene transfer in combination with lipofectamine. Mol Biotechnol 42: pp. 41-48 CrossRef
  24. Hasegawa, T, Minami, M, Okamoto, A, Tatsuno, I, Isaka, M, Ohta, M (2010) Characterization of a virulence-associated and cell-wall-located DNase of Streptococcus pyogenes. Microbiology 156: pp. 184-190 CrossRef
  25. Aziz, RK, Ismail, SA, Park, HW, Kotb, M (2004) Post-proteomic identification of a novel phage-encoded streptodornase, Sda1, in invasive M1T1 Streptococcus pyogenes. Mol Microbiol 54: pp. 184-197 CrossRef
  26. Bozzaro, S, Bucci, C, Steinert, M (2008) Phagocytosis and host-pathogen interactions in Dictyostelium with a look at macrophages. Int Rev Cell Mol Biol 271: pp. 253-300 CrossRef
  27. Dallaire-Dufresne, S, Paquet, VE, Charette, SJ (2011) Dictyostelium discoideum: a model for the study of bacterial virulence. Can J Microbiol 57: pp. 699-707 CrossRef
  28. Lopez-Cortes, LF, Cruz-Ruiz, M, Gomez-Mateos, J, Jimenez-Hernandez, D, Palomino, J, Jimenez, E (1993) Measurement of levels of tumor necrosis factor-alpha and interleukin-1 beta in the CSF of patients with meningitis of different etiologies: utility in the differential diagnosis. Clin Infect Dis 16: pp. 534-539 CrossRef
  29. Leppert, D, Leib, SL, Grygar, C, Miller, KM, Schaad, UB, Hollander, GA (2000) Matrix metalloproteinase (MMP)-8 and MMP-9 in cerebrospinal fluid during bacterial meningitis: association with blood鈥揵rain barrier damage and neurological sequelae. Clin Infect Dis 31: pp. 80-84 CrossRef
  30. Azeh, I, Mader, M, Smirnov, A, Beuche, W, Nau, R, Weber, F (1998) Experimental pneumococcal meningitis in rabbits: the increase of matrix metalloproteinase-9 in cerebrospinal fluid correlates with leucocyte invasion. Neurosci Lett 256: pp. 127-130 CrossRef
  31. Chang, A, Khemlani, A, Kang, H, Proft, T (2011) Functional analysis of Streptococcus pyogenes nuclease A (SpnA), a novel group A streptococcal virulence factor. Mol Microbiol 79: pp. 1629-1642 CrossRef
  32. Sumby, P, Barbian, KD, Gardner, DJ, Whitney, AR, Welty, DM, Long, RD, Bailey, JR, Parnell, MJ, Hoe, NP, Adams, GG, DeLeo, FR, Musser, JM (2005) Extracellular deoxyribonuclease made by group A Streptococcus assists pathogenesis by enhancing evasion of the innate immune response. Proc Natl Acad Sci U S A 102: pp. 1679-1684 CrossRef
  33. Brinkmann, V, Reichard, U, Goosmann, C, Fauler, B, Uhlemann, Y, Weiss, DS, Weinrauch, Y, Zychlinsky, A (2004) Neutrophil extracellular traps kill bacteria. Science 303: pp. 1532-1535 CrossRef
  
• 刊物主题：Biomedicine general; Medicine/Public Health, general; Life Sciences, general;
• 出版者：BioMed Central
• ISSN：1756-0500

文摘

Background The Gram-positive bacterium Streptococcus suis serotype 2 is an important swine pathogen and emerging zoonotic agent. Multilocus sequence typing allowed dividing S. suis serotype 2 into sequence types (STs). The three major STs of S. suis serotype 2 from North America are 1 (most virulent), 25 (intermediate virulence) and 28 (less virulent). Although the presence of DNase activity in S. suis has been previously reported, little data is available. The aim of this study was to investigate DNase activity in S. suis according to STs, to characterize the activity and gene, and to provide evidence for a potential role in virulence. Results We showed that ST1 and ST28 strains exhibited DNase activity that was absent in ST25 strains. The lack of activity in ST25 isolates was associated with a 14-bp deletion resulting in a shifted reading frame and a premature stop codon. The DNase of S. suis P1/7 (ST1) was cell-associated and active on linear DNA. A DNase-deficient mutant of S. suis P1/7 was found to be less virulent in an amoeba model. Stimulation of macrophages with the DNase mutant showed a decreased secretion of pro-inflammatory cytokines and matrix metalloproteinase-9 compared to the parental strain. Conclusions This study further expands our knowledge of S. suis DNase and its potential role in virulence.