The prevalence of unusual intramolecular thioester cross-link on the surface proteins of Enterococci

The emergence of nosocomial infections caused by multi-drug resistant enterococci is becoming a cause for concern. According to the 2015 National Surveillance of Antibiotic Resistance (NSAR) report by the Ministry of Health Malaysia, Enterococcus faecium was found to be resistant to a variety of a...

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Main Authors: Su-yin, Kan, Nabilah Huda, Abdul Halim
Format: Article
Language:English
Published: 2017
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Online Access:http://eprints.unisza.edu.my/5804/1/FH02-FSK-18-13124.pdf
http://eprints.unisza.edu.my/5804/
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spelling my-unisza-ir.58042022-02-27T02:10:09Z http://eprints.unisza.edu.my/5804/ The prevalence of unusual intramolecular thioester cross-link on the surface proteins of Enterococci Su-yin, Kan Nabilah Huda, Abdul Halim Q Science (General) QH426 Genetics The emergence of nosocomial infections caused by multi-drug resistant enterococci is becoming a cause for concern. According to the 2015 National Surveillance of Antibiotic Resistance (NSAR) report by the Ministry of Health Malaysia, Enterococcus faecium was found to be resistant to a variety of antibiotics especially to vancomycin which recorded an increased resistant rate. Recent studies showed that many clinically significant Grampositive human pathogens possess a unique covalent intramolecular thioester bond on at least one of their surface 24dhesion proteins which may serve as potential therapeutic targets, an alternative to antibiotics. Sequence search based on the protein query of thioester-containing domain (TED) of Streptococcus pyogenes were performed using the Basic Local Alignment Search Tool (BLAST) against non-redundant protein sequences (nr) and UniProt Knowledgebase (UniProtKB) databases. The protein BLAST followed by multiple sequence alignment revealed that a total of 54 strains of E. faecium and 75 strains of E. faecalis were predicted to contain a thioester bond on their surface protein, whereby the critical cysteine and glutamine residues were found to be perfectly conserved. These predicted TEDs showed low sequence homology (about 35 % similarity) to known streptococcal TED and many of which functions are unknown. However, the high prevalence of TEDs across enterococcal strains is astonishing. Therefore, the biochemical function of thioester bond in these proteins contributing to enterococcal pathogenicity needs to be further assessed experimentally, which may serve as a new drug target or diagnostic tool for enterococcal infections. 2017-12 Article PeerReviewed text en http://eprints.unisza.edu.my/5804/1/FH02-FSK-18-13124.pdf Su-yin, Kan and Nabilah Huda, Abdul Halim (2017) The prevalence of unusual intramolecular thioester cross-link on the surface proteins of Enterococci. Research Journal of Pharmacy and Technology, 10 (12). pp. 24-25. ISSN 0974-3618
institution Universiti Sultan Zainal Abidin
building UNISZA Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Sultan Zainal Abidin
content_source UNISZA Institutional Repository
url_provider https://eprints.unisza.edu.my/
language English
topic Q Science (General)
QH426 Genetics
spellingShingle Q Science (General)
QH426 Genetics
Su-yin, Kan
Nabilah Huda, Abdul Halim
The prevalence of unusual intramolecular thioester cross-link on the surface proteins of Enterococci
description The emergence of nosocomial infections caused by multi-drug resistant enterococci is becoming a cause for concern. According to the 2015 National Surveillance of Antibiotic Resistance (NSAR) report by the Ministry of Health Malaysia, Enterococcus faecium was found to be resistant to a variety of antibiotics especially to vancomycin which recorded an increased resistant rate. Recent studies showed that many clinically significant Grampositive human pathogens possess a unique covalent intramolecular thioester bond on at least one of their surface 24dhesion proteins which may serve as potential therapeutic targets, an alternative to antibiotics. Sequence search based on the protein query of thioester-containing domain (TED) of Streptococcus pyogenes were performed using the Basic Local Alignment Search Tool (BLAST) against non-redundant protein sequences (nr) and UniProt Knowledgebase (UniProtKB) databases. The protein BLAST followed by multiple sequence alignment revealed that a total of 54 strains of E. faecium and 75 strains of E. faecalis were predicted to contain a thioester bond on their surface protein, whereby the critical cysteine and glutamine residues were found to be perfectly conserved. These predicted TEDs showed low sequence homology (about 35 % similarity) to known streptococcal TED and many of which functions are unknown. However, the high prevalence of TEDs across enterococcal strains is astonishing. Therefore, the biochemical function of thioester bond in these proteins contributing to enterococcal pathogenicity needs to be further assessed experimentally, which may serve as a new drug target or diagnostic tool for enterococcal infections.
format Article
author Su-yin, Kan
Nabilah Huda, Abdul Halim
author_facet Su-yin, Kan
Nabilah Huda, Abdul Halim
author_sort Su-yin, Kan
title The prevalence of unusual intramolecular thioester cross-link on the surface proteins of Enterococci
title_short The prevalence of unusual intramolecular thioester cross-link on the surface proteins of Enterococci
title_full The prevalence of unusual intramolecular thioester cross-link on the surface proteins of Enterococci
title_fullStr The prevalence of unusual intramolecular thioester cross-link on the surface proteins of Enterococci
title_full_unstemmed The prevalence of unusual intramolecular thioester cross-link on the surface proteins of Enterococci
title_sort prevalence of unusual intramolecular thioester cross-link on the surface proteins of enterococci
publishDate 2017
url http://eprints.unisza.edu.my/5804/1/FH02-FSK-18-13124.pdf
http://eprints.unisza.edu.my/5804/
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