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Microbial Esterases: Genomics, Physiology, Structure, and Applications
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Microbial Esterases: Genomics, Physiology, Structure, and Applications

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: closed (30 June 2022) | Viewed by 2103

Special Issue Editor

Prof. Dr. T. Doohun Kim

E-Mail Website
Guest Editor
Department of Chemistry, College of Natural Science, Sookmyung Women’s University, Seoul 04310, Korea
Interests: enzyme structure; protein crystallography; assay development; immobilization; protein engineering

Special Issue Information

Dear Colleagues,

Microbial esterases, a major branch of the hydrolases family, are involved in the formation and cleavage of ester bonds at the molecular level. This enzyme family, which can be used in food, pulp, textile, cosmetics, cosmetics, and biodiesel industries, gained a lot of academic and industrial interest due to their functional significances and application potentials. Although a number of molecular studies were done, further studies are still necessary for the full understanding of this enzyme family. This Special Issue (SI) aims to put together recent advances on microbial esterases, and the main emphasis is given, but not limited, to genomics, functional physiology, structural analysis, and industrial applications of microbial esterases. Manuscripts of original research, communications, and reviews are all welcome.

Prof. Dr. T. Doohun Kim
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • genomics and genetic engineering
  • identification and characterization
  • functional analysis and metabolism
  • structural determination and analysis
  • immobilization and industrial applications
  • theoretical and computer modelling studies

Published Papers (1 paper)

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Research

10 pages, 2453 KiB  
Article
Functional and Transcriptome Analysis of Streptococcus pyogenes Virulence on Loss of Its Secreted Esterase
by Xiaolan Zhang, Yue Wang, Hui Zhu and Zhaohua Zhong
Int. J. Mol. Sci. 2022, 23(14), 7954; https://doi.org/10.3390/ijms23147954 - 19 Jul 2022
Cited by 1 | Viewed by 1577
Abstract
Esterases are broadly expressed in bacteria, but much remains unknown about their pathogenic effect. In previous studies, we focused on an esterase secreted by Streptococcus pyogenes (group A Streptococcus, GAS). Streptococcal secreted esterase (Sse) can hydrolyze the sn−2 ester bonds of [...] Read more.
Esterases are broadly expressed in bacteria, but much remains unknown about their pathogenic effect. In previous studies, we focused on an esterase secreted by Streptococcus pyogenes (group A Streptococcus, GAS). Streptococcal secreted esterase (Sse) can hydrolyze the sn−2 ester bonds of platelet−activating factor (PAF), converting it to an inactive form that inhibits neutrophil chemotaxis to the infection sites. However, as a virulent protein, Sse probably participates in GAS pathogenesis far beyond chemotaxis inhibition. In this study, we generated the sse gene knockout strain (Δsse) from the parent strain MGAS5005 (hypervirulent M1T1 serotype) and compared the difference in phenotypes. Absence of Sse was related to weakened skin invasion in a murine infection model, and significantly reduced GAS epithelial adherence, invasion, and intracellular survival. Reduced virulence of the Δsse mutant strain was explored through transcriptome analysis, revealing a striking reduction in the abundance of invasive virulence factors including M protein, SIC, ScpA, and SclA. Besides the influence on the virulence, Sse also affected carbohydrate, amino acid, pyrimidine, and purine metabolism pathways. By elucidating Sse−mediated pathogenic process, the study will contribute to the development of new therapeutic agents that target bacterial esterases to control clinical GAS infections. Full article
(This article belongs to the Special Issue Microbial Esterases: Genomics, Physiology, Structure, and Applications)
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