Bacteriophage Lytic Proteins

A special issue of Viruses (ISSN 1999-4915). This special issue belongs to the section "Bacterial Viruses".

Deadline for manuscript submissions: 31 December 2024 | Viewed by 3393

Special Issue Editor


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Guest Editor
Research Institute for Medicines (iMed.ULisboa), Faculty of Pharmacy, Universidade de Lisboa, Lisboa, Portugal
Interests: mechanisms of bacteriophage-induced lysis; mycobacteriophages; activity of lytic proteins; bacteriophage engineering; development of bacteriophage-based products for therapeutic purposes

Special Issue Information

Dear Colleagues,

The global problem of bacterial resistance to antibiotics has increased the focus on bacteriophage research, particularly due to the potential of these viruses to lyse bacterial pathogens. Phage-induced lysis results from the synthesis of lytic proteins that compromise each barrier of the bacterial cell envelope. These proteins are designed to target bacteriophages’ specific hosts, being structurally diverse and having different activities. Knowledge of their characteristics and understanding their modes of action are important contributions to the development of new tools to kill bacteria and fight multidrug resistance.

This Special Issue, entitled “Bacteriophage Lytic Proteins”, aims to present recent research on any aspect of lysis protein activity, such as holins, endolysins, spanins, and the specific proteins of actinobacteriophages targeting the mycolil layers. Some of its focal points include, but are not limited to, the following:

  1. Delivery of phage lytic proteins to their targets;
  2. Understanding endolysin activation and contribution of their functional domains to lysis;
  3. Mechanisms of phage-induced lysis;
  4. Bioengineering and applications of phage-derived lytic proteins.

Dr. Madalena Pimentel
Guest Editor

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Keywords

  • bacteriophage
  • phage lysis
  • holins
  • endolysins
  • spanins
  • mycolil esterases
  • antimicrobials

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Published Papers (2 papers)

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Research

11 pages, 1703 KiB  
Article
Influence of Lipopolysaccharide-Interacting Peptides Fusion with Endolysin LysECD7 and Fatty Acid Derivatization on the Efficacy against Acinetobacter baumannii Infection In Vitro and In Vivo
by Xiaowan Li, Wenwen Shangguan, Xiaoqian Yang, Xiaoyue Hu, Yanan Li, Wenjie Zhao, Meiqing Feng and Jun Feng
Viruses 2024, 16(5), 760; https://doi.org/10.3390/v16050760 - 11 May 2024
Cited by 2 | Viewed by 1474
Abstract
Acinetobacter baumannii has developed multiple drug resistances, posing a significant threat to antibiotic efficacy. LysECD7, an endolysin derived from phages, could be a promising therapeutic agent against multi-drug resistance A. baumannii. In this study, in order to further enhance the antibacterial efficiency [...] Read more.
Acinetobacter baumannii has developed multiple drug resistances, posing a significant threat to antibiotic efficacy. LysECD7, an endolysin derived from phages, could be a promising therapeutic agent against multi-drug resistance A. baumannii. In this study, in order to further enhance the antibacterial efficiency of the engineered LysECD7, a few lipopolysaccharide-interacting peptides (Li5, MSI594 and Li5-MSI) were genetically fused with LysECD7. Based on in vitro antibacterial activity, the fusion protein Lys-Li5-MSI was selected for further modifications aimed at extending its half-life. A cysteine residue was introduced into Lys-Li5-MSI through mutation (Lys-Li5-MSIV12C), followed by conjugation with a C16 fatty acid chain via a protonation substitution reaction(V12C-C16). The pharmacokinetic profile of V12C-C16 exhibited a more favorable characteristic in comparison to Lys-Li5-MSI, thereby resulting in enhanced therapeutic efficacy against lethal A. baumannii infection in mice. The study provides valuable insights for the development of novel endolysin therapeutics and proposes an alternative therapeutic strategy for combating A. baumannii infections. Full article
(This article belongs to the Special Issue Bacteriophage Lytic Proteins)
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22 pages, 4705 KiB  
Article
Bacteriophage vB_SepP_134 and Endolysin LysSte_134_1 as Potential Staphylococcus-Biofilm-Removing Biological Agents
by Natalia N. Golosova, Andrey L. Matveev, Nina V. Tikunova, Yana A. Khlusevich, Yulia N. Kozlova, Vera V. Morozova, Igor V. Babkin, Tatiana A. Ushakova, Elena V. Zhirakovskaya, Elizaveta A. Panina, Elena I. Ryabchikova and Artem Y. Tikunov
Viruses 2024, 16(3), 385; https://doi.org/10.3390/v16030385 - 29 Feb 2024
Viewed by 1506
Abstract
Bacteria of the genus Staphylococcus are significant challenge for medicine, as many species are resistant to multiple antibiotics and some are even to all of the antibiotics we use. One of the approaches to developing new therapeutics to treat staphylococcal infections is the [...] Read more.
Bacteria of the genus Staphylococcus are significant challenge for medicine, as many species are resistant to multiple antibiotics and some are even to all of the antibiotics we use. One of the approaches to developing new therapeutics to treat staphylococcal infections is the use of bacteriophages specific to these bacteria or the lytic enzymes of such bacteriophages, which are capable of hydrolyzing the cell walls of these bacteria. In this study, a new bacteriophage vB_SepP_134 (St 134) specific to Staphylococcus epidermidis was described. This podophage, with a genome of 18,275 bp, belongs to the Andhravirus genus. St 134 was able to infect various strains of 12 of the 21 tested coagulase-negative Staphylococcus species and one clinical strain from the Staphylococcus aureus complex. The genes encoding endolysin (LysSte134_1) and tail tip lysin (LysSte134_2) were identified in the St 134 genome. Both enzymes were cloned and produced in Escherichia coli cells. The endolysin LysSte134_1 demonstrated catalytic activity against peptidoglycans isolated from S. aureus, S. epidermidis, Staphylococcus haemolyticus, and Staphylococcus warneri. LysSte134_1 was active against S. aureus and S. epidermidis planktonic cells and destroyed the biofilms formed by clinical strains of S. aureus and S. epidermidis. Full article
(This article belongs to the Special Issue Bacteriophage Lytic Proteins)
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