American Journal of Microbiological Research
ISSN (Print): 2328-4129 ISSN (Online): 2328-4137 Website: https://www.sciepub.com/journal/ajmr Editor-in-chief: Apply for this position
Open Access
Journal Browser
Go
American Journal of Microbiological Research. 2015, 3(6), 190-196
DOI: 10.12691/ajmr-3-6-3
Open AccessArticle

In silico Analysis of Surface Proteins of Streptococcus pneumoniae Serotype 19F for Identification of Immunoprotective Epitopes

Shirin Tarahomjoo1,

1Division of Genomics and Genetic Engineering, Department of Biotechnology and Central Laboratory, Razi Vaccine and Serum Research Institute, Karaj, Iran

Pub. Date: November 28, 2015

Cite this paper:
Shirin Tarahomjoo. In silico Analysis of Surface Proteins of Streptococcus pneumoniae Serotype 19F for Identification of Immunoprotective Epitopes. American Journal of Microbiological Research. 2015; 3(6):190-196. doi: 10.12691/ajmr-3-6-3

Abstract

Pneumococcal conjugate vaccines (PCVs) were developed through chemical coupling of polysaccharide capsules of pneumococci to immunogenic carrier proteins and World Health Organization recommends inclusion of these vaccines in national immunization programs for children. However, the PCVs implementation in developing countries can be prevented by the high manufacturing costs. This issue can be overcome by construction of protein based vaccines against pneumococci. We already identified three pneumococcal surface proteins including D-alanyl-D-alanine-carboxy peptidase (DDCP), choline binding protein D (CBPD), and cell wall surface anchor family protein (CWSAP) as appropriate protein candidates for eliciting protection against S. pneumoniae serotype 19F. The protein protective antigenicity, the absence of autoimmunity induction, and the amino acid sequence conservancy in serotype 19F pneumococcal strains were used as selection criteria. However, regarding the requirement of both antibody and cellular immune responses for protection against pneumococci, analysis of protective B and T-cell epitopes of these proteins is necessary to examine their usefulness in new vaccine formulations. In the present study, therefore, we aim to identify protective epitopes of these proteins via widely used bioinformatic tools. The Bepipred program was used for identification of linear B-cell epitopes. The conformational B-cell epitopes were predicted using the CBTope program. T-cell epitopes were identified using the Immune Epitope Database tool. The immunoprotective abilities of epitopes were evaluated using VaxiJen. Our results showed that all of the three studied proteins included protective epitopes. However, the greatest number of epitopes was identified in a truncated form of CWSAP. Moreover, the most probable immunoprotective epitopes reside in this protein and these epitopes were highly conserved in CWSAPs of the most common pneumococcal serotypes in the world. Therefore, the truncated CWSAP was an appropriate candidate for development of protein based vaccines against the most common pneumococcal serotypes.

Keywords:
cell surface proteins epitopes pneumococcal serotypes pneumococcal vaccines Streptococcus pneumoniae

Creative CommonsThis 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]  Johnson, H. L., Deloria-Knoll, M., Levine, O. 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.
 
[3]  WHO, “Pneumococcal vaccines, WHO position paper.” Wkly Epidemiol Rec, 87 (14), 129-144, Apr. 2012.
 
[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]  Tarahomjoo, S. “Bioinformatic analysis of surface proteins of Streptococcus pneumoniae serotype 19F for identification of vaccine candidates,” Am J Microbiol Research, 2 (6), 174-177, Oct. 2014.
 
[7]  Tarahomjoo, S. “Recent approaches in vaccine development against Streptococcus pneumoniae,” J Mol Microbiol Biotechnol, 24 (4), 215-227, August 2014.
 
[8]  Kelly, D. F. and Rappuoli, R. Hot topics in infection and immunity in children II, Springer, New York, 2005, 217-223.
 
[9]  Doytchinova, I. A. and Flower, D. R. “Bioinformatic approach for identifying parasite and fungal candidate subunit vaccines,” Open Vaccine J, 1 (1), 22-26, Sep. 2008.
 
[10]  Novotny, J., Handschumacher, M., Haber, E. et al. “Antigenic determinants in proteins coincide with surface regions accessible to large probes (antibody domains), Proc Natl Acad Sci USA, 83 (2), 226-230, Jan. 1986.
 
[11]  Quijada, L., Requema M. J., Soto, M. et al. “Mapping of the linear antigenic determinants of the Leishmania infantum Hsp 70 recognized by leishmaniasis sera,” Immunol Lett, 52 (2-3), 73-79, Sep. 1996.
 
[12]  Faria, A. R., Costa, M. M., Giusta, M. S. et al. “High throughput analysis of synthetic peptides for the immunodiagnosis of canine visceral leishmaniasis,” PLos Negl Trop dis, 5 (9): e1310, Sep. 2011.
 
[13]  Abdullah, M. R., Gutierrez-Fernandez, J., Pribyl, T. et al. “Structure of the pneumococcal L, D carboxypeptidase DacB and pathophysiological effects of disabled cell wall hydrolases DacA and DacB,” Mol Microbiol, 93 (6), 1183-1206, Sep. 2014.
 
[14]  Barh, D., Barve, N., Gupta, K. et al. “Exoproteome and secretome derived broad spectrum novel drug and vaccine candidates in Vibrio cholerae targeted by Piper betel derived compounds,” PLos ONE, 8(1): e52773, Jan. 2013.
 
[15]  Gosink, K. K., Mann, E. R., Guglielmo, C. et al. “Role of novel choline binding proteins in virulence of Streptococcus pneumoniae,” Infect Immun, 68 (10), 5690-5695, Oct. 2000.
 
[16]  Henderson, B., Nair, S., Pallas, J. and Williams, M. A. “Fibronectin: a multidomain host adhesin targeted by bacterial fibronectin binding proteins,” FEMS Microbiol Rev, 35 (1), 147-200, Jan. 2011.
 
[17]  Tabatabaei, S. R., Fallah, F., Shiva, F. et al, “Multiplex PCR assay for detection of pneumococcal serotypes in nasopharyngeal samples of healthy children; Tehran, 2009-2010,” Ann Res Rev Biol, 4(24), 3780-3790, Jul. 2014.
 
[18]  Gray, B. M., Converse, G. M. 3rd, Dillon, H. C. Jr. “Epidemiological studies of Streptococcus pneumoniae in infants: acquisition, carriage, and infection during the first 24 months of life,” J Infect Dis, 142 (6), 923-933, Dec. 1980.