The mechanistic landscape of Lytic transglycosylase as targets for antibacterial therapy
Lytic transglycosylases (Ltgs) are glycan strand cleaving enzymes whose role is poorly understood in the genesis of the bacterial envelope. They play multiple roles in all stages of a bacterial life cycle, by creating holes in the peptidoglycan that is necessary for cell division and separation. Her...
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| Veröffentlicht in: | Current opinion in structural biology 2022-12, Vol.77, p.102480-102480, Article 102480 |
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| container_title | Current opinion in structural biology |
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| creator | Martinez-Bond, Elizabeth A. Soriano, Berliza M. Williams, Allison H. |
| description | Lytic transglycosylases (Ltgs) are glycan strand cleaving enzymes whose role is poorly understood in the genesis of the bacterial envelope. They play multiple roles in all stages of a bacterial life cycle, by creating holes in the peptidoglycan that is necessary for cell division and separation. Here, we review recent advances in understanding the suitability of Ltgs as antibacterial drug targets. We specifically highlight a known inhibitor bulgecin A that is able to inhibit the function of structurally diverse Ltgs, as well as synergize with beta-lactams to improve its efficacy in antibiotic insensitive strains. Discovery of new antibiotics or new targets has been challenging. These studies could provide a viable path toward designing broad-spectrum inhibitors that targets Ltgs.
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| doi_str_mv | 10.1016/j.sbi.2022.102480 |
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[Display omitted]</description><subject>Anti-Bacterial Agents - pharmacology</subject><subject>Bacteria</subject><subject>Bacterial Proteins</subject><subject>beta-Lactams - pharmacology</subject><subject>Cell Wall</subject><subject>Glycosyltransferases</subject><subject>Peptidoglycan</subject><issn>0959-440X</issn><issn>1879-033X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMtKAzEUhoMoWi8P4EaydDM1t7nhSsQbFNwodBcymZM2ZTpTc1Jh3t6UVpeuDufw_T-cj5Brzqac8eJuNcXGTwUTIu1CVeyITHhV1hmTcn5MJqzO60wpNj8j54grxljBVXVKzmQhheRSTsj8Ywl0DXZpeo_RW9qZvkVrNkAHR2fj7hSD6XHRjXbAsTMI1CCNJiwgInVDoKaPvjE2QvCmo3EJwWzGS3LiTIdwdZgX5PP56ePxNZu9v7w9PswyK-siZqJWHBR3dVvk1igpS2cr5qqmrLmpGsaZKqsmV6pVytnaAbd5WYiilNzlreDygtzuezdh-NoCRr32aKFLf8CwRS0SWSZFMk8o36M2DIgBnN4EvzZh1JzpnVC90kmo3gnVe6Epc3Oo3zZraP8SvwYTcL8HID357SFotB56C60PYKNuB_9P_Q8_WIZK</recordid><startdate>202212</startdate><enddate>202212</enddate><creator>Martinez-Bond, Elizabeth A.</creator><creator>Soriano, Berliza M.</creator><creator>Williams, Allison H.</creator><general>Elsevier Ltd</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-0726-141X</orcidid></search><sort><creationdate>202212</creationdate><title>The mechanistic landscape of Lytic transglycosylase as targets for antibacterial therapy</title><author>Martinez-Bond, Elizabeth A. ; Soriano, Berliza M. ; Williams, Allison H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c396t-2941e41f9d65ca4337fc80f8b791a8b010478b544d44fc9fe1c57626731f5d213</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Anti-Bacterial Agents - pharmacology</topic><topic>Bacteria</topic><topic>Bacterial Proteins</topic><topic>beta-Lactams - pharmacology</topic><topic>Cell Wall</topic><topic>Glycosyltransferases</topic><topic>Peptidoglycan</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Martinez-Bond, Elizabeth A.</creatorcontrib><creatorcontrib>Soriano, Berliza M.</creatorcontrib><creatorcontrib>Williams, Allison H.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Current opinion in structural biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Martinez-Bond, Elizabeth A.</au><au>Soriano, Berliza M.</au><au>Williams, Allison H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The mechanistic landscape of Lytic transglycosylase as targets for antibacterial therapy</atitle><jtitle>Current opinion in structural biology</jtitle><addtitle>Curr Opin Struct Biol</addtitle><date>2022-12</date><risdate>2022</risdate><volume>77</volume><spage>102480</spage><epage>102480</epage><pages>102480-102480</pages><artnum>102480</artnum><issn>0959-440X</issn><eissn>1879-033X</eissn><abstract>Lytic transglycosylases (Ltgs) are glycan strand cleaving enzymes whose role is poorly understood in the genesis of the bacterial envelope. They play multiple roles in all stages of a bacterial life cycle, by creating holes in the peptidoglycan that is necessary for cell division and separation. Here, we review recent advances in understanding the suitability of Ltgs as antibacterial drug targets. We specifically highlight a known inhibitor bulgecin A that is able to inhibit the function of structurally diverse Ltgs, as well as synergize with beta-lactams to improve its efficacy in antibiotic insensitive strains. Discovery of new antibiotics or new targets has been challenging. These studies could provide a viable path toward designing broad-spectrum inhibitors that targets Ltgs.
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| subjects | Anti-Bacterial Agents - pharmacology Bacteria Bacterial Proteins beta-Lactams - pharmacology Cell Wall Glycosyltransferases Peptidoglycan |
| title | The mechanistic landscape of Lytic transglycosylase as targets for antibacterial therapy |
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