Immunization against Clostridium perfringens cells elicits protection against Clostridium tetani in mouse model: Identification of cross-reactive proteins using proteomic methodologies

BMC Microbiology

Volumn 8, Issue , 2008, Pages

  Alam, Syed Imteyaz ^a   Bansod, Sunita ^a   Singh, Lokendra ^a  

^a DEFENCE RESEARCH AND DEVELOPMENT ESTABLISHMENT   (India)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BACTERIAL VACCINE; BACTERIUM ANTIBODY; PROTEOME;

ANIMAL; ARTICLE; BAGG ALBINO MOUSE; CLOSTRIDIUM PERFRINGENS; CLOSTRIDIUM TETANI; CROSS REACTION; FEMALE; IMMUNIZATION; IMMUNOLOGY; MOUSE; PROTEOMICS; TETANUS;

ANIMALS; ANTIBODIES, BACTERIAL; BACTERIAL PROTEINS; BACTERIAL VACCINES; CLOSTRIDIUM PERFRINGENS; CLOSTRIDIUM TETANI; CROSS REACTIONS; FEMALE; IMMUNIZATION; MICE; MICE, INBRED BALB C; PROTEOME; PROTEOMICS; TETANUS;

EID: 58249109483     PISSN: 14712180     EISSN: 14712180     Source Type: Journal    
DOI: 10.1186/1471-2180-8-194     Document Type: Article

References (23)

1. SS Arnon, The Clostridia San Diego: Academic Press, Rood JI, McClane BA, Songer JG, Titbal RW, 1997 95 115
2. Maternal and neonatal tetanus. MH Roper JH Vandelaer FL Gasse, Lancet 2007 370 1947 1959 17854885
3. Anaerobic infections of war wounds in the Middle East. JD MacLennan, Lancet 1943 ii 123 126
4. Molecular genetics and pathogenesis of Clostridium perfringens. JI Rood ST Cole, Microbiol Rev 1991 55 621 648 1779929
5. Clostridium perfringens wound infection. RW Titball JI Rood, Molecular Medical Microbiology United Kingdom: Academic Press, Sussman M, 2001 1875 1904
6. Analysis of known bacterial protein vaccine antigens reveals biased physical properties and amino acid composition. C Myers M Duffield S Rowe J Miller B Lingard S Hayward RW Titball, Comp Functional Genom 2003 4 468 478
7. Complete genome sequence of Clostridium perfringens, an anaerobic flesh-eater. T Shimizu K Ohtani H Hirakawa K Ohshima A Yamashita T Shiba N Ogasawara M Hattori S Kuhara H Hayashi, Proc Natl Acad Sci 2002 99 996 1001 11792842
8. The genome sequence of Clostridium tetani, the causative agent of tetanus disease. H Bruggemann S Baumer WF Fricke A Wiezer H Liesegang I Decker C Herzberg R Martinez-Arias R Merkl A Henne G Gottschalk, Proc Natl Acad Sci 2003 100 1316 1321 12552129
9. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. MM Bradford, Anal Bichem 1976 72 248 254
10. Systems for polyacrylamide gel electrophoresis. PJ Blackshear, Methods in Enzymology New York: Academic Press, Jaeoby WB, 1984 104 237 255 6717283
11. Characterization of an acidic-pH-inducible stress protein (hsp70), a putative sulfatide binding adhesin, from Helicobacter pylori. M Huesca A Goodwin A Bhagwansingh P Hoffman CA Lingwood1, Infect Immun 1998 66 4061 4067 9712748
12. Chaperones: helpers along the pathways to folding. E Craig, Science 1993 260 1902 1903 8100364
13. Heat shock protein produced by Helicobacter pylori. K Yokota Y Hira M Haque S Hayashi H Isogai T Sugiyama E Nagamachi Y Tsukada N Fujii K Oguma, Microbiol Immunol 1994 38 403 405 7935068
14. Postabortal Chlamydia trachomatis salpingitis: correlating risk with antigen-specific serological responses and with neutralization. RC Brunham R Peeling I Maclean J McDowell K Persson S Osser, J Infect Dis 1987 155 749 755 3546521
15. GroEL (Hsp60) of Clostridium difficile is involved in cell adherence. C Hennequin F Porcheray A Waligora-Dupriet A Collignon MC Barc P Bourlioux T Karjalainen, Microbiology 2001 147 87 96 11160803
16. Sequence analysis of Lengionella micdadei groELS operon. P Hindersson N Hoiby J Banqsborq, FEMS Miocrobiol Lett 1991 61 31 38
17. Post-translational quality control: folding, refolding, and degrading proteins. S Wickner MR Maurizi S Gottesman, Science 1999 286 1888 1893 10583944
18. The Hsp70 and Hsp60 chaperone machines. B Bukau AL Horwich, Cell 1998 92 351 366 9476895
19. Proteome and transcriptome analysis of the virulence genes regulated by the VirR/VirS system in Clostridium perfringens. T Shimizu K Shima K Yoshino K Yonezawa T Shimizu H Hayashi, J Bacteriol 2002 184 2587 2594 11976286
20. Antibodies to streptococcal surface enolase react with human alpha-enolase: implications in poststreptococcal sequelae. PA Fontan V Pancholi MM Nociari VA Fischetti, J Infect Dis 2000 182 1712 1721 11069244
21. Restricted distribution of the butyrate kinase pathway among butyrate-producing bacteria from the human colon. P Louis SH Duncan SI McCrae J Millar MS Jackson HJ Flint, J Bact 2004 186 2099 2106 15028695
22. Surface Analyses and Immune Reactivities of Major Cell Wall-Associated Proteins of Group A Streptococcus. JN Cole RD Ramirez BJ Currie SJ Cordwell SP Djordjevic MJ Walker, Infect Immun 2005 73 3137 3146 15845522
23. Proteomic analysis and identification of Streptococcus pyogenes surface-associated proteins. A Severin E Nickbarg J Wooters SA Quazi YV Matsuka E Murphy IK Moutsatsos RJ Zagursky SB Olmsted, J Bact 2007 189 1514 1522 17142387