WikiJournal of Science/Lysenin/XML

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    <full_title>WikiJournal of Science/Lysenin</full_title>
    <abbrev_title>Wiki.J.Sci.</abbrev_title>
    <issn media_type='electronic'>2002-4436 / 2470-6345 / 2639-5347</issn>
    <doi_data>
     <doi>10.15347/WJS</doi>
     <resource>http://www.WikiJSci.org/</resource>
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   <journal_issue>  
    <publication_date media_type='online'>     
     <year>2019</year>  
    </publication_date>   
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     <volume></volume>
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    <issue></issue>
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   <journal_article publication_type='full_text'>   
    <titles>     
     <title>Lysenin</title>
    </titles>   
    <contributors>
    <person_name sequence='first' contributor_role='author'>
     <surname></surname>
    </person_name><person_name sequence='additional' contributor_role='contributors'>
     <surname>et al.</surname><affiliation>Wikipedia editors of Lysenin</affiliation><link>https://xtools.wmflabs.org/articleinfo/en.wikipedia.org/Lysenin//2019-08-17</link>
    </person_name>  
    </contributors> 
    <publication_date media_type='online'>     
     <year>2019</year>
    </publication_date>   
    <doi_data>     
     <doi>10.15347/wjs/2019.006</doi>     
     <resource>https://en.wikiversity.org/wiki/WikiJournal of Science/Lysenin</resource>
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     <license-p>[[File:Open_Access_logo_PLoS_white.svg|11px|link=Wikipedia:Open Access]] [[File:Cc.logo.circle.svg|16px|link=Wikipedia:Creative Commons]]
This is an open access article distributed under the&nbsp;[http://creativecommons.org/licenses/by-sa/3.0/ Creative Commons Attribution ShareAlike License], which permits unrestricted use, distribution, and reproduction, provided the original author and source are credited.</license-p>
    </license>
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   <abstract>
    </p>
Lysenin is a pore-forming toxin present in the coelomic fluid of the earthworm ''Eisenia fetida''. Pore-forming toxins (PFTs) are proteinaceous virulence factors produced by many pathogenic bacteria. Following the general mechanism of action of PFTs, lysenin is secreted as a soluble monomer that binds specifically to the membrane receptor sphingomyelin. After attachment, lysenin forms a 9-copy oligomer (nonamer) prepore on the lipid bilayer before membrane insertion. The biological role of lysenin is still unclear, however the most plausible theory is that it is part of an immune-avoiding mechanism. There are many proposed technological applications proposed for lysenin, and understanding its molecular role in bacterial infection could help in developing different antibiotic strategies to solve the problem of multiple drug resistance in bacteria.
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