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International Journal of Current Microbiology and Applied Sciences (IJCMAS)
IJCMAS is now DOI (CrossRef) registered Research Journal. The DOIs are assigned to all published IJCMAS Articles.
Index Copernicus ICI Journals Master List 2019 - IJCMAS--ICV 2019: 96.39 For more details click here
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National Academy of Agricultural Sciences (NAAS)
NAAS Score: *5.38 (2020)
[Effective from January 1, 2020]
For more details click here

ICV 2019: 96.39
Index Copernicus ICI Journals Master List 2019 - IJCMAS--ICV 2019: 96.39
For more details click here

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Original Research Articles

PRINT ISSN : 2319-7692
Online ISSN : 2319-7706
Issues : 12 per year
Publisher : Excellent Publishers
Email : editorijcmas@gmail.com / submit@ijcmas.com
Editor-in-chief: Dr.M.Prakash
Index Copernicus ICV 2018: 95.39
NAAS RATING 2020: 5.38

Int.J.Curr.Microbiol.App.Sci.2021.10(10): 142-155
DOI: https://doi.org/10.20546/ijcmas.2021.1010.017


Potential Application of Phage ɸ11 Lytic Proteins in Rapid Detection and Elimination of Staphylococcus aureus
Amenti and Rajkrishna Mondal*
Department of Biotechnology, Nagaland University, Dimapur, Nagaland, India
*Corresponding author
Abstract:

The increasing antibiotic resistance conferred by Staphylococcus aureus to multiple potential antibiotics has become a serious issue of concern and threat to mankind worldwide. In light of this, phage lytic proteins have been reported which show potential antimicrobial activity against pathogenic microorganisms that could be a promising alternative to antibiotics to eradicate the antibiotic resistant problems. This review discusses the various applications of S. aureus phage lytic proteins and the potentiality of aureophage phi 11 endolysin and virion associated peptidoglycan hydrolase (VAPGH) against staphylococcus strains. Phage Phi11 endolysin harbors two enzymatically active domain; cysteine and histidine-dependent amidohydrolase/peptidase (CHAP) and Amidase 2 at the N-terminus and a cell wall binding domain (CBD) SH3 5 at the C-terminus, while virion associated peptidoglycan hydrolase (VAPGH) has two catalytic domains, CHAP and Glucosaminidase (Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase) at its N-terminal and C-terminal, respectively.


Keywords: Staphylococcus aureus, Phage ɸ11, endolysin, VAPGH, antibiotic resistant, MRSA, antimicrobials
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How to cite this article:

Amenti and Rajkrishna Mondal. 2021. Potential Application of Phage ɸ11 Lytic Proteins in Rapid Detection and Elimination of Staphylococcus aureus.Int.J.Curr.Microbiol.App.Sci. 10(10): 142-155. doi: https://doi.org/10.20546/ijcmas.2021.1010.017