Characterization of an E. coli Bacteriophage and the Molecular Recognition Mechanism

preprint OA: closed
📄 Open PDF Full text JSON View at publisher
AI-generated deep summary by claude@2026-06, 2026-06-24 · read from full text

This preprint studied how a virulent Escherichia coli bacteriophage, E1, recognizes and infects its host, focusing on the molecular interaction between its receptor-binding protein (RBP) and bacterial surface receptor. The authors isolated and characterized phage E1 infecting E. coli DH5α and used antibody blocking, proteinase K treatment, pull-down, and Western blot analyses to identify gp38 as the RBP and OmpC as the functional receptor, with molecular simulations pinpointing gp38 residues Trp9, Arg21, Trp22, and Trp37 as critical for OmpC binding. The main caveat is that the work is presented as a preprint and is not peer reviewed, so the robustness of the findings has not been independently validated. The paper does not explicitly discuss endometriosis or adenomyosis; it was included in the corpus via a keyword match in the upstream search index.

Read from the paper's body, not the abstract. Not a substitute for reading the paper. No clinical advice. How this works

Abstract

The infection of bacteriophages begins with the specific recognition of host receptors by their receptor-binding proteins (RBPs). Although previous studies have characterized interactions between Escherichia coli ( E. coli ) bacteriophages and outer membrane protein C (OmpC), the precise molecular mechanism remains unclear. In this study, we isolated and characterized a virulent bacteriophage, E1, that infects E. coli DH5α. Antibody blocking assays identified gp38 as its RBP, and subsequent Proteinase K treatment, pull-down, and Western blot analyses confirmed OmpC as the functional receptor. These findings demonstrated that the gp38-OmpC interaction constitutes the key molecular basis for host recognition by phage E1. Molecular simulations further revealed that residues Trp9, Arg21, Trp22, and Trp37 of gp38 are critical for OmpC binding, highlighting their essential roles in receptor recognition. Collectively, this study elucidates for the first time the molecular recognition mechanism between gp38 and OmpC at the amino acid level, providing structural insights into the host specificity of bacteriophages and a theoretical foundation for their rational engineering.
Full text 7,109 characters · extracted from preprint-html · click to expand
Characterization of an E. coli Bacteriophage and the Molecular Recognition Mechanism | Authorea try { document.documentElement.classList.add('js'); } catch (e) { } var _gaq = _gaq || []; _gaq.push(['_setAccount', 'G-8VDV14Y67G']); _gaq.push(['_trackPageview']); (function() { var ga = document.createElement('script'); ga.type = 'text/javascript'; ga.async = true; ga.src = ('https:' == document.location.protocol ? 'https://ssl' : 'http://www') + '.google-analytics.com/ga.js'; var s = document.getElementsByTagName('script')[0]; s.parentNode.insertBefore(ga, s); })(); Skip to main content Preprints Collections Wiley Open Research IET Open Research Ecological Society of Japan All Collections About About Authorea FAQs Contact Us Quick Search anywhere Search for preprint articles, keywords, etc. Search Search ADVANCED SEARCH SCROLL This is a preprint and has not been peer reviewed. Data may be preliminary. 5 December 2025 V1 Latest version Share on Characterization of an E. coli Bacteriophage and the Molecular Recognition Mechanism Authors : Yangwei Pan , Xinge Cui , Shuang Jiang , Luwei Chai , Yongkan Zhang , Ying Yang , Hongbing Liu , Xingying Mou , and Tao Le 0000-0002-2771-7744 [email protected] Authors Info & Affiliations https://doi.org/10.22541/au.176492359.97355823/v1 204 views 108 downloads Contents Abstract Supplementary Material Information & Authors Metrics & Citations View Options References Figures Tables Media Share Abstract The infection of bacteriophages begins with the specific recognition of host receptors by their receptor-binding proteins (RBPs). Although previous studies have characterized interactions between Escherichia coli ( E. coli ) bacteriophages and outer membrane protein C (OmpC), the precise molecular mechanism remains unclear. In this study, we isolated and characterized a virulent bacteriophage, E1, that infects E. coli DH5α. Antibody blocking assays identified gp38 as its RBP, and subsequent Proteinase K treatment, pull-down, and Western blot analyses confirmed OmpC as the functional receptor. These findings demonstrated that the gp38-OmpC interaction constitutes the key molecular basis for host recognition by phage E1. Molecular simulations further revealed that residues Trp9, Arg21, Trp22, and Trp37 of gp38 are critical for OmpC binding, highlighting their essential roles in receptor recognition. Collectively, this study elucidates for the first time the molecular recognition mechanism between gp38 and OmpC at the amino acid level, providing structural insights into the host specificity of bacteriophages and a theoretical foundation for their rational engineering. Supplementary Material File (figure 1.docx) Download 8.18 MB File (figure 2.docx) Download 9.26 MB File (figure 3.docx) Download 15.62 MB File (figure 4.docx) Download 2.95 MB File (figure 5.docx) Download 28.11 MB File (figure 6.docx) Download 10.23 MB File (manuscript.docx) Download 85.12 KB Information & Authors Information Version history V1 Version 1 05 December 2025 Copyright This work is licensed under a Non Exclusive No Reuse License. Keywords genetics protein purification protein-protein interaction analysis research and analysis methods virus classification Authors Affiliations Yangwei Pan Chongqing Normal University View all articles by this author Xinge Cui Chongqing Normal University View all articles by this author Shuang Jiang Chongqing Normal University View all articles by this author Luwei Chai Chongqing Normal University View all articles by this author Yongkan Zhang Chongqing Normal University View all articles by this author Ying Yang Chongqing Normal University View all articles by this author Hongbing Liu Chongqing Normal University View all articles by this author Xingying Mou Chongqing Normal University View all articles by this author Tao Le 0000-0002-2771-7744 [email protected] Chongqing Normal University View all articles by this author Metrics & Citations Metrics Article Usage 204 views 108 downloads .FvxKWukQNSOunydq8rnd { width: 100px; } Citations Download citation Yangwei Pan, Xinge Cui, Shuang Jiang, et al. Characterization of an E. coli Bacteriophage and the Molecular Recognition Mechanism. Authorea . 05 December 2025. DOI: https://doi.org/10.22541/au.176492359.97355823/v1 If you have the appropriate software installed, you can download article citation data to the citation manager of your choice. Simply select your manager software from the list below and click Download. For more information or tips please see 'Downloading to a citation manager' in the Help menu . Format Please select one from the list RIS (ProCite, Reference Manager) EndNote BibTex Medlars RefWorks Direct import Tips for downloading citations document.getElementById('citMgrHelpLink').addEventListener('click', function() { popupHelp(this.href); return false; }); $(".js__slcInclude").on("change", function(e){ if ($(this).val() == 'refworks') $('#direct').prop("checked", false); $('#direct').prop("disabled", ($(this).val() == 'refworks')); }); View Options View options PDF View PDF Figures Tables Media Share Share Share article link Copy Link Copied! Copying failed. Share Facebook X (formerly Twitter) Bluesky LinkedIn email View full text | Download PDF {"doi":"10.22541/au.176492359.97355823/v1","type":"Article"} Now Reading: Share Figures Tables Close figure viewer Back to article Figure title goes here Change zoom level Go to figure location within the article Download figure Toggle share panel Toggle share panel Share Toggle information panel Toggle information panel Go to previous graphic Go to next graphic Go to previous table Go to next table All figures All tables View all material View all material xrefBack.goTo xrefBack.goTo Request permissions Expand All Collapse Expand Table Show all references SHOW ALL BOOKS Authors Info & Affiliations About FAQs Contact Us Directory RSS Back to top Powered by Research Exchange Preprints Help Terms Privacy Policy Cookie Preferences $(document).ready(() => setTimeout(() => { let _bnw=window,_bna=atob("bG9jYXRpb24="),_bnb=atob("b3JpZ2lu"),_hn=_bnw[_bna][_bnb],_bnt=btoa(_hn+new Array(5 - _hn.length % 4).join(" ")); $.get("/resource/lodash?t="+_bnt); },4000)); (function(){function c(){var b=a.contentDocument||a.contentWindow.document;if(b){var d=b.createElement('script');d.innerHTML="window.__CF$cv$params={r:'9fee84a38a8c52ad',t:'MTc3OTMxMzQxOA=='};var a=document.createElement('script');a.src='/cdn-cgi/challenge-platform/scripts/jsd/main.js';document.getElementsByTagName('head')[0].appendChild(a);";b.getElementsByTagName('head')[0].appendChild(d)}}if(document.body){var a=document.createElement('iframe');a.height=1;a.width=1;a.style.position='absolute';a.style.top=0;a.style.left=0;a.style.border='none';a.style.visibility='hidden';document.body.appendChild(a);if('loading'!==document.readyState)c();else if(window.addEventListener)document.addEventListener('DOMContentLoaded',c);else{var e=document.onreadystatechange||function(){};document.onreadystatechange=function(b){e(b);'loading'!==document.readyState&&(document.onreadystatechange=e,c())}}}})();

Text is read by the "Ask this paper" AI Q&A widget below. Extraction quality varies by source — PMC NXML preserves structure cleanly, OA-HTML may include some navigation residue, and OA-PDF can have broken hyphenation. The publisher copy (via DOI) is the canonical version.

My notes (saved in your browser only)

Ask this paper AI returns verbatim quotes from the full text · source: preprint-html

Answers must be backed by verbatim quotes from this paper's full text. Hallucinated quotes are dropped automatically; if no verbatim passage answers the question, we say so. How this works

Citation neighborhood (no data yet)

We don't have any in-corpus citations linked to this paper yet. This is a recent paper (2025) — citers typically take a year or two to land, and the OpenAlex reference graph may still be filling in.

Source provenance

europepmc
last seen: 2026-05-20T01:45:00.602351+00:00
unpaywall
last seen: 2026-06-02T02:00:03.124865+00:00