Evaluation of Siderophore Production in Streptococcus Pneumoniae by Chrome Azurol S Method

Authors

  • Fereshteh Ebrahimi 1 1- Dept. of Medical Laboratory Sciences, School of Paramedical Sciences, Zanjan University of Medical Sciences, Zanjan, Iran.
  • Mozhgan Kheirandish 2 2. Dept. of Microbiology and Virology, School of Medicine, Zanjan University of Medical Sciences, Zanjan, Iran.
  • Moslem Jafarisani 3 3. Dept. of Clinical Biochemistry, School of Medicine, Shahroud University of Medical Sciences, Shahroud, Iran.
  • Davoud Afshar 4* 4. Dept. of Microbiology and Virology, School of Medicine, Zanjan University of Medical Sciences, Zanjan, Iran. orcid http://orcid.org/0000-0002-3259-3790

DOI:

https://doi.org/10.22100/jkh.v13i4.2090

Keywords:

Streptococcus pneumonia, siderophore, Chrome azurol S (CAS)

Abstract

Introduction: Iron is one of the vital elements for pathogenic bacteria. Some bacteria produce proteins called siderophore, which have high affinity to bind iron and absorb it from many glycoproteins such as transferrin and lactoferrin. The aim of the present study was to investigate the ability of siderophore production in Streptococcus pneumoniae using the chrome azurol S (CAS) method.

Methods: The production of siderophore was measured by chrome azurol S method. Sediment of tested bacteria was added into microtube containing CAS solution and then incubated at 25C for 2h. The optical densities (OD) of samples were measured at 630 nm. Bacillus subtilis ATCC 11778 was used as a positive control for siderophore production.

Results: The OD rate for S. pneumoniae and B. subtilis was 0.043 and -0.016, respectively.

Conclusion: According to results, it seems that S. pneumoniae is not able to produce siderophore. Therefore, it is possible that the bacterium absorbs iron from other iron sources such as lactoferrin, transferrin and ferritin.

References

O’Brien KL, Wolfson LJ, Watt JP, Henkle E, Deloria-Knoll M, McCall N, et al. Hib and Pneumococcal Global Burden of Disease Study Team. Burden of disease caused by Streptococcus pneumoniae in children younger than 5 years: global estimates. Lancet. 2009;374(9693):893-902.

Arushothy R, Ahmad N, Yassin RM. Evolution of Erythromycin Resistance among Streptococcus pneumoniae Isolates in Malaysia from 2005 and 2010. Journal of Biosciences and Medicines 2016;4:116. doi:10.4236/jbm.2016.45012

Schroeder MR, Stephens DS. Macrolide resistance in Streptococcus pneumoniae. Front Cell Infect Microbiology 2016;6:98. doi:10.3389/fcimb.2016.00098

Sritharan M. Iron and bacterial virulence. Indian journal of medical microbiology 2006;24:163.

Brock JH. The physiology of lactoferrin. Biochem Cell Biol 2002;80:1-6.

Kawabata H, Sakamoto S, Masuda T, Uchiyama T, Ohmori K, Koeffler HP, et al. Roles of transferrin receptors in erythropoiesis. Rinsho ketsueki 2016;57:951-8. doi:10.11406/rinketsu.57.951

Gray-Owen SD, Schyvers AB. Bacterial transferrin and lactoferrin receptors. Trends Microbiol 1996;4:185-91.

Saha R, Saha N, Donofrio RS, Bestervelt LL. Microbial siderophores: a mini review. J Basic Microbiol 2013;53:303-17. doi:10.1002/jobm.201100552

Neilands JB. Siderophores: structure and function of microbial iron transport compounds. J Biol Chem 1995;270:26723-6.

Skaar EP. The battle for iron between bacterial pathogens and their vertebrate hosts. PLoS pathog 2010;6:e1000949. doi:10.1371/journal.ppat.1000949

Brown JS, Gilliland SM, Ruiz-Albert J, Holden DW. Characterization of pit, a Streptococcus pneumoniae iron uptake ABC transporter. Infect Immun 2002;70:4389-98.

Tai SS, Lee CJ, Winter RE. Hemin utilization is related to virulence of Streptococcus pneumoniae. Infect Immun 1993;61:5401-5.

Hammerschmidt S, Bethe G, Remane PH, Chhatwal GS. Identification of pneumococcal surface protein A as a lactoferrin-binding protein of Streptococcus pneumoniae. Infect Immun 1999;67:1683-7.

Turner AG, Ong CY, Walker MJ, Djoko KY, McEwan AG. Transition metal homeostasis in streptococcus pyogenes and Streptococcus pneumoniae. Adv Microb Physiol 2017;70:123-91. doi:10.1016/bs.ampbs.2017.01.002

Clarke TE, Ku SY, Dougan DR, Vogel HJ, Tari LW. The structure of the ferric siderophore binding protein FhuD complexed with gallichrome. Nat Struct Biol 2000;7:287-91. doi:10.1038/74048

Ferguson AD, Braun V, Fiedler HP, Coulton JW, Diederichs K, Welte W. Crystal structure of the antibiotic albomycin in complex with the outer membrane transporter FhuA. Protein Sci 2000;9:956-63. doi:10.1110/ps.9.5.956

Wandersman C, Delepelaire P. Bacterial iron sources: from siderophores to hemophores. Annu Rev Microbiol 2004;58:611-47. doi:10.1146/annurev.micro.58.030603.123811

Cheng W, Li Q, Jiang YL, Zhou CZ, Chen Y. Structures of Streptococcus pneumoniae PiaA and its complex with ferrichrome reveal insights into the substrate binding and release of high affinity iron transporters. PloS one 2013;8:e71451. doi:10.1371/journal.pone.0071451

Published

2019-03-11

Issue

Section

Original Article(s)

How to Cite

Evaluation of Siderophore Production in Streptococcus Pneumoniae by Chrome Azurol S Method. (2019). Knowledge and Health in Basic Medical Sciences, 13(4), 27-31. https://doi.org/10.22100/jkh.v13i4.2090

Most read articles by the same author(s)

<< < 7 8 9 10 11 12 13 14 15 16 > >>