Author(s): Muhammad Hassan, Atif Amin Baig

Email(s): atifamin@unisza.edu.my

DOI: 10.52711/2231-5691.2021.00018   

Address: Muhammad Hassan, Atif Amin Baig*
Faculty of Medicine, Universiti Sultan Zainal Abidin, Medicine Campus, 20400 Kuala, Terengganu, Terengganu.
*Corresponding Author

Published In:   Volume - 11,      Issue - 2,     Year - 2021


ABSTRACT:
Computational approach is used to identify the binding region of alpha-enolase over cell-surface protein of neutrophil. The product of alpha-enolase gene binds the one of the cell surface protein of neutrophil known as myoblast. After the binding on myoblast, neutrophil structure gets change and mobilized chromatin fibers came out to eliminate pathogen though NETosis. Thus, over study revealed that alpha-enolase of Streptococcus Pneumoniae is one of the major factor in inducing NETs during innate immune response.


Cite this article:
Muhammad Hassan, Atif Amin Baig. Induction of Neutrophil Extracellular Traps (NETs) by Alpha-Enolase of Streptococcus pneumoniae. Asian Journal of Pharmaceutical Research. 2021; 11(2):95-6. doi: 10.52711/2231-5691.2021.00018

Cite(Electronic):
Muhammad Hassan, Atif Amin Baig. Induction of Neutrophil Extracellular Traps (NETs) by Alpha-Enolase of Streptococcus pneumoniae. Asian Journal of Pharmaceutical Research. 2021; 11(2):95-6. doi: 10.52711/2231-5691.2021.00018   Available on: https://www.asianjpr.com/AbstractView.aspx?PID=2021-11-2-4


REFERENCES:
1.    Tsirigos, K.D., et al., The TOPCONS web server for consensus prediction of membrane protein topology and signal peptides. Nucleic acids research, 2015. 43(W1): p. W401-W407.
2.    Mori, Y., et al., α-Enolase of Streptococcus pneumoniae induces formation of neutrophil extracellular traps. Journal of Biological Chemistry, 2012. 287(13): p. 10472-10481.
3.    Bergmann, S., et al., α‐Enolase of Streptococcus pneumoniae is a plasmin (ogen)‐binding protein displayed on the bacterial cell surface. Molecular microbiology, 2001. 40(6): p. 1273-1287.
4.    Vajda, S., et al., New additions to the C lus P ro server motivated by CAPRI. Proteins: Structure, Function, and Bioinformatics, 2017. 85(3): p. 435-444.
5.    DeLano, W.L., PyMOL. 2002.

Recomonded Articles:

Asian Journal of Pharmaceutical Research (AJPRes.) is an international, peer-reviewed journal, devoted to pharmaceutical sciences. AJPRes. publishes Original Research Articles, Short Communications..... Read more >>>

RNI: Not Available                     
DOI: 10.5958/2231–5691 


Recent Articles




Tags