Emerging Biomedicines Based on Bacteriophages

Yan, Jianlong; Fan, Xiangyu; Xie, Jianping

doi:10.1615/critreveukaryotgeneexpr.2013006578

Cited by 4 publications

(4 citation statements)

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“…Phage holin/endolysin systems are currently being pursued intensively as novel potential therapeutic agents in the current age of increasing occurrences of bacterial resistance to antibiotics (73). Lytic systems also have the potential to function as delivery systems, introducing drugs, nucleic acids, and proteins into eukaryotic cells (74).…”

Section: Use Of Holins For Therapeutic Purposes In Medicinementioning

confidence: 99%

“…Lytic systems also have the potential to function as delivery systems, introducing drugs, nucleic acids, and proteins into eukaryotic cells (74). Another possibility involves the development of diagnostic methods using genetically engineered phage (73). In this section, we discuss some recent medical applications that depend on holins.…”

Section: Use Of Holins For Therapeutic Purposes In Medicinementioning

confidence: 99%

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Holins in Bacteria, Eukaryotes, and Archaea: Multifunctional Xenologues with Potential Biotechnological and Biomedical Applications

2015

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bHolins form pores in the cytoplasmic membranes of bacteria for the primary purpose of releasing endolysins that hydrolyze the cell wall and induce cell death. Holins are encoded within bacteriophage genomes, where they promote cell lysis for virion release, and within bacterial genomes, where they serve a diversity of potential or established functions. These include (i) release of gene transfer agents, (ii) facilitation of programs of differentiation such as those that allow sporulation and spore germination, (iii) contribution to biofilm formation, (iv) promotion of responses to stress conditions, and (v) release of toxins and other proteins. There are currently 58 recognized families of holins and putative holins with members exhibiting between 1 and 4 transmembrane ␣-helical spanners, but many more families have yet to be discovered. Programmed cell death in animals involves holin-like proteins such as Bax and Bak that may have evolved from bacterial holins. Holin homologues have also been identified in archaea, suggesting that these proteins are ubiquitous throughout the three domains of life. Phage-mediated cell lysis of dualmembrane Gram-negative bacteria also depends on outer membrane-disrupting "spanins" that function independently of, but in conjunction with, holins and endolysins. In this minireview, we provide an overview of their modes of action and the first comprehensive summary of the many currently recognized and postulated functions and uses of these cell lysis systems. It is anticipated that future studies will result in the elucidation of many more such functions and the development of additional applications.

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Section: Use Of Holins For Therapeutic Purposes In Medicinementioning

confidence: 99%

Section: Use Of Holins For Therapeutic Purposes In Medicinementioning

confidence: 99%

Holins in Bacteria, Eukaryotes, and Archaea: Multifunctional Xenologues with Potential Biotechnological and Biomedical Applications

2015

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“…Since the molecular function of endolysin is to cleave the peptidoglycan layer, their attention in medical applications has been increasing, for example, to treat the diseases caused by Gram positive bacteria . Endolysins are comprised of diverse sequences and only some of their structures have been determined .…”

Section: Introductionmentioning

confidence: 99%

The structure of DLP12 endolysin exhibiting alternate loop conformation and comparative analysis with other endolysins

2017

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The lytic enzyme, endolysin, is encoded by bacteriophages (phages) to destroy the peptidoglycan layer of host bacterial cells. The release of phage progenies to start the new infection cycle is dependent on the cell lysis event. Endolysin encoded by DLP12 cryptic prophage is a SAR endolysin which is retained by the bacterium presumably due to the benefit it confers. The structure of DLP12 endolysin (Id: 4ZPU) determined at 2.4 Å resolution is presented here. The DLP12 endolysin structure shows a modular nature and is organized into distinct structural regions. One of the monomers has the loops at the active site in a different conformation. This has led to a suggestion of depicting possibly active and inactive state of DLP12 endolysin. Comparison of DLP12 endolysin structure and sequence with those of related endolysins shows the core three-dimensional fold is similar and the catalytic triad geometry is highly conserved despite the sequence differences. Features essential for T4 lysozyme structure and function such as the distance between catalytic groups, salt bridge and presence of nucleophilic water are conserved in DLP12 endolysin and other endolysins analyzed.

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“…Holins facilitate the release of phage particles from infected bacteria during viral-induced cell lysis [Young, 2014]. They have been used for a variety of medical and industrial purposes [Gao et al, 2013; Yan et al, 2013] and have numerous physiological functions in non-infected bacterial and eukaryotic cells [Saier and Reddy, 2015]. They are exceptionally diverse in sequence, topology, and mechanism of action) [Catalao et al, 2013; Young, 2013].…”

Section: Introductionmentioning

confidence: 99%

Analysis of 58 Families of Holins Using a Novel Program, PhyST

Kuppusamykrishnan¹,

Chau²,

Moreno–Hagelsieb³

et al. 2016

Microb Physiol

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We have designed a freely accessible program, PhyST, which allows the automated characterization of any family of homologous proteins within the Transporter Classification Database. The program performs an NCBI-PSI-BLAST search and reports (1) the average protein sequence length with standard deviations, (2) the average predicted number of transmembrane segments, (3) the total number of homologues retrieved, (4) a quantitative list of all source phyla, and (5) potential fusion proteins of sizes considerably exceeding the average size of the proteins retrieved. We have applied this program to 58 families of holins, and the results are presented. The results show that holins are very rarely fused to other protein domains, suggesting that holins form transmembrane pores as homooligomers without the participation of other proteins or protein domains.

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Emerging Biomedicines Based on Bacteriophages

Cited by 4 publications

References 0 publications

Holins in Bacteria, Eukaryotes, and Archaea: Multifunctional Xenologues with Potential Biotechnological and Biomedical Applications

Holins in Bacteria, Eukaryotes, and Archaea: Multifunctional Xenologues with Potential Biotechnological and Biomedical Applications

The structure of DLP12 endolysin exhibiting alternate loop conformation and comparative analysis with other endolysins

Analysis of 58 Families of Holins Using a Novel Program, PhyST

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