Muhammad Hassan, Atif Amin Baig*
Faculty of Medicine, Universiti Sultan Zainal Abidin, Medicine Campus, 20400 Kuala, Terengganu, Terengganu
*Corresponding Author E-mail: atifamin@unisza.edu.my
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.
KEYWORDS: Neutrophil Extracellular Traps, alpha-enolase gene binds.
INTRODUCTION:
Insilico analysis was used to examine the location of product of alpha-enolase on S. pneumonia. TOPCONS1 used five best models to interpret the input file and predicted best possible results about protein topology and signal peptide.
Results of TOPCONS revealed that alpha-enolase present outside of the cell membrane and had no signal peptide. It was concentrated on the entire cell surface and released into culture supernatant. Moreover, alpha-enolase has been exhibited to be present on the surface of most streptococcal species2.
Alpha-enolase-stimulated neutrophils ruptured and formed extracellular fibers which increased the numbers of ruptured neutrophils by 5-fold. The occurrence of alpha-enolase as the only existence enolase molecule for pneumococci, its equal gene expression shows conserved gene in all strains, and disruption of the eno gene appears to be lethal specify that alpha-enolase is an essential glycolytic enzyme3. Myoblast antigen 24.1D5 is an alpha-enolase-binding protein and localized on the cell surface of live neutrophils, whereas it was not present on monocytes or T cells2.
|
Peptide sequence |
Peptide location |
Protein length |
Protein description |
|
GNPTLEVEVYTESGAFGR |
17–34 |
434 |
alpha-Enolase (S. pneumoniae) |
|
GLETAVGDEGGFAPR |
197–211 |
434 |
alpha-Enolase (S. pneumoniae) |
|
FGQGGAGPVGGQGPR |
356–370 |
396 |
Myoblast antigen 24.1D5 (Homo sapiens) |
ClusPro 2.04 performs three computational steps rigid body docking, RMSD based clustering and the removal of steric clashes by energy minimization to make best protein-protein interaction. ClusPro 2.0 was used get model of protein-protein interaction which was further visualized and analyzed by using PyMol5.
In above figure green and light blue colour represents the Myoblast antigen 24.1D5 (Homo sapiens) and alpha-enolase (S. pneumoniae) respectively, while yellow and red spheres exhibits the binding sites of the Myoblast antigen 24.1D5 (Homo sapiens) and alpha-enolase (S. pneumoniae) respectively.
CONCLUSION:
Myoblast is a receptor of alpha enolase, present on the cell-surface of neutrophil and it doesn’t exhibit on T and B cells. Our study conclude that alpha-enolase urges neutrophil to take out its NETs to eliminate pathogen by binding on myoblast receptor.
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.
Received on 29.03.2020 Modified on 31.10.2020
Accepted on 10.03.2021 ©Asian Pharma Press All Right Reserved
Asian Journal of Pharmaceutical Research. 2021; 11(2):95-96.
DOI: 10.52711/2231-5691.2021.00018