Bioinformatic Analysis of Surface Proteins of Streptococcus pneumoniae Serotype 19F for Identification of Vaccine Candidates

Shirin Tarahomjoo^1,

¹Department of Biotechnology, Razi Vaccine and Serum Research Institute, Karaj, Iran

Cite this paper:
Shirin Tarahomjoo. Bioinformatic Analysis of Surface Proteins of Streptococcus pneumoniae Serotype 19F for Identification of Vaccine Candidates. American Journal of Microbiological Research. 2014; 2(6):174-177. doi: 10.12691/ajmr-2-6-2

Abstract

Streptococcus pneumoniae serotype 19F is one of major pneumococcal serotypes responsible for pneumococcal invasive disease in children less than 5 years worldwide. Pneumococcal conjugate vaccines (PCVs) were developed through chemical coupling of capsular polysaccharides of pneumococci to immunogenic carrier proteins and World Health Organization recommends the inclusion of these vaccines in national immunization programs for children. However, costly manufacture of PCVs can prevent their implementation in developing countries. This issue can be addressed by construction of protein based vaccines against pneumococci. Cell surface proteins are key factors in infectious processes of pathogens and are attractive as vaccine candidates. LPxTG motif containing proteins, lipoproteins, and choline binding proteins are among main groups of pneumococcal surface proteins. In this study, therefore, we aim to identify suitable candidates among these proteins for development of proteinaceous vaccines against S. pneumoniae serotype 19F infection using bioinformatic tools. These proteins were then identified in proteome data of S. pneumoniae 19F-14 through BLAST with LPxTG, lipobox consensus motifs, and the choline binding protein consensus sequence. PRED-LIPO online tool was used to confirm the presence of lipoprotein specific signal peptide. The cellular location of the proteins was analyzed with PSORTb v.3.0. Vaxijen v.2.0 was used to evaluate the protein antigenicity. BLAST against human proteome was done to remove the possibility for autoimmunity induction by the proteins. Moreover, the presence of homolog proteins in other pneumococcal serotype 19F strains including S. pneumoniae A026, S. pneumoniae G54, and S. pneumoniae ST556 were investigated. Our analysis revealed that cell wall surface anchor family protein ( YP_002741626.1), D-alanyl-D-alanyl-carboxy peptidase, surface protein PspC, and choline binding protein D are promising candidates for development of protein based vaccines against S. pneumoniae serotype 19F infection.

Keywords:
choline binding proteins lipoproteins LPxTG motifs protein streptococcus pneumoniae serotype 19F vaccine

This work is licensed under a Creative Commons Attribution 4.0 International License. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

References:

[1]	Mook-Kanamori, B. B., Geldhoff, M., van der Poll, T. and van de Beek, D, “Pathogenesis and pathophysiology of pneumococcal meningitis,” Clin Microbiol Rev, 24 (3), 557-591, Jul. 2011.
[2]	WHO, “Pneumococcal vaccines, WHO position paper,” Wkly Epidemiol Rec, 87 (14), 129-144, Apr. 2012.
[3]	Johnson, H. L., Deloria-Knoll, M., Levin, R. S. et al, “Systematic evaluation of serotypes causing invasive pneumococcal disease among children under five: the pneumococcal global serotype project,” PLoS Med, 7 (10), e1000348, Oct. 2010.
[4]	Foster, T. J., Geoghegan J. A., Ganesh, V. K. and Hook, M, “Adhesion, invasion and evasion: the many functions of surface proteins of Staphylococcus aureus,” Nature Rev Microbiol, 12 (1), 49-62, Dec. 2014.
[5]	Bergmann, S. and Hammerschmidt, S, “Versatility of pneumococcal surface proteins,” Microbiol, 152 (2), 295-303, Feb. 2006.
[6]	Leenhouts, K., Buist, G. and Kok, J, “Anchoring of proteins to lactic acid bacteria,” Antonie van Leeuwen, 76 (1-4), 367-376, Jul.-Nov. 1999.
[7]	Venema, R., Tjalsma, H., van Dijl, J. M. et al, “Active lipoprotein precursors in the gram positive eubacterium Lactococcus lactis,” J Biol Chem, 278 (17), 14739-14746, Apr. 2003.
[8]	Tjalsma, H., Kontinent, V. P., Pragai, Z. et al, “The role of lipoprotein processing by signal peptidase II in the gram-positive eubacterium Bacillus subtilis,” J Biol Chem, 274 (3), 1698-1707, Jan. 1998.
[9]	Davis, M. N. and Flower, D. R, “Harnessing bioinformatics to discover new vaccines,” Drug Discov Today, 12 (9-10), 389-395, May 2007.
[10]	Kelly, D. F. and Rappuoli, R, Hot topics in infection and immunity in children II, Springer, New York, 2005, 217-223.
[11]	Blank, M., Krause, I., Fridkin, M. et al, “Bacterial induction of autoantibodies to β2-glycoprotein-I accounts for the infectious etiology of antiphospholipid syndrome,” J Clin Investig, 109 (6), 797-804, March 2002.
[12]	Scheffers, D-J. and Pinho, M. G, “Bacterial cell wall synthesis: new insights from localization studies,” Microb Mol Biol Rev, 69 (4), 585-607, Dec. 2005.
[13]	Ogunniyi, A. D., Woodrow, M. C., Poolman, J. T., Paton, J.C, “Protection against Streptococcus pneumoniae elicited by immunization with pneumolysin and CbpA,” Infect Immun, 69 (10), 5997-6003, Oct. 2001.
[14]	Kausmally, L., Johnsborg, O., Lunde, M., Knutsen, E. and Havarstein, L. S, “Choline-binding protein D (CbpD) in Streptococcus pneumoniae is essential for competence induced cell lysis,” J Bacteriol, 187 (13), 4338-4345, July 2005.