{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"institution":[{"name":"bioRxiv"}],"indexed":{"date-parts":[[2026,1,15]],"date-time":"2026-01-15T18:33:10Z","timestamp":1768501990147,"version":"3.49.0"},"posted":{"date-parts":[[2022,10,13]]},"group-title":"Microbiology","reference-count":90,"publisher":"openRxiv","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"accepted":{"date-parts":[[2022,10,13]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                <jats:p>\n                  Bacteriophages exploit host proteins for successful infection. Small heat shock proteins are a universally conserved family of stress-induced molecular chaperones that prevent irreversible aggregation of proteins. Two small heat shock proteins, IbpA and IbpB, are a class of holding modulators or \u201choldases\u201d, which bind partially folded proteins and await ATP-driven folding chaperones for refolding. Bacteriophage \u03d5X174 is a small, icosahedral, and non-tailed virus belonging to the\n                  <jats:italic>Microviridae<\/jats:italic>\n                  . During \u03d5X174 infection of\n                  <jats:italic>Escherichia coli<\/jats:italic>\n                  C122, IbpA and IbpB were previously found to be the most highly upregulated host proteins, with expression levels comparable to \u03d5X174 proteins. In this work, to understand the role of IbpA and IbpB during \u03d5X174 infection, we used a hybrid approach of CRISPR interference and genomic knockouts to disrupt the\n                  <jats:italic>ibpA<\/jats:italic>\n                  and\n                  <jats:italic>ibpB<\/jats:italic>\n                  genes. We show that these two proteins do not appear to be necessary for efficient \u03d5X174 replication, and moreover, their absence has no effect on \u03d5X174 fecundity.\n                <\/jats:p>\n                <jats:sec>\n                  <jats:title>Importance<\/jats:title>\n                  <jats:p>\n                    The small heat shock proteins (sHsps) are universally conserved family of stress-induced molecular chaperones that prevent irreversible protein aggregation. In\n                    <jats:italic>E. coli<\/jats:italic>\n                    , the IbpA\/B sHsps work together, and separately, to bind partially folded proteins and await ATP-driven folding chaperones for refolding. These proteins are highly upregulated during protein overexpression and bacteriophage infection, but their collective role in bacteriophage infection has not been investigated. Here, we show that the\n                    <jats:italic>ibpA\/B<\/jats:italic>\n                    genes are dispensable for bacteriophage \u03d5X174 infection, and are likely not essential host factors despite their abundance during diverse phage infections. Instead, this work points towards their role as cell wall integrity sensors, similar to the phage shock protein system, in addition to their canonical role as holdases of cytoplasmic protein.\n                  <\/jats:p>\n                <\/jats:sec>","DOI":"10.1101\/2022.10.13.511849","type":"posted-content","created":{"date-parts":[[2022,10,13]],"date-time":"2022-10-13T23:45:18Z","timestamp":1665704718000},"source":"Crossref","is-referenced-by-count":0,"title":["IbpAB small heat shock proteins are not host factors for bacteriophage \u03d5X174 replication"],"prefix":"10.64898","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4553-157X","authenticated-orcid":false,"given":"Hannah X","family":"Zhu","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6233-831X","authenticated-orcid":false,"given":"Bradley W","family":"Wright","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7721-8321","authenticated-orcid":false,"given":"Dominic Y","family":"Logel","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4679-5868","authenticated-orcid":false,"given":"Mark P","family":"Molloy","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2359-1301","authenticated-orcid":false,"given":"Paul R","family":"Jaschke","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"54368","reference":[{"key":"2022101614451006000_2022.10.13.511849v1.1","doi-asserted-by":"publisher","DOI":"10.1016\/j.mib.2003.09.004"},{"key":"2022101614451006000_2022.10.13.511849v1.2","doi-asserted-by":"publisher","DOI":"10.1016\/j.femsre.2003.08.001"},{"key":"2022101614451006000_2022.10.13.511849v1.3","doi-asserted-by":"crossref","first-page":"1081","DOI":"10.1111\/brv.12271","article-title":"Deciphering the virus-to-prokaryote ratio (VPR): insights into virus\u2013host relationships in a variety of ecosystems","volume":"92","year":"2017","journal-title":"Biological reviews of the Cambridge Philosophical Society"},{"key":"2022101614451006000_2022.10.13.511849v1.4","doi-asserted-by":"publisher","DOI":"10.1038\/nrmicro1750"},{"key":"2022101614451006000_2022.10.13.511849v1.5","doi-asserted-by":"crossref","first-page":"e1001017","DOI":"10.1371\/journal.pgen.1001017","article-title":"A forward-genetic screen and dynamic analysis of lambda phage host-dependencies reveals an extensive interaction network and a new anti-viral strategy","volume":"6","year":"2010","journal-title":"PLoS genetics"},{"key":"2022101614451006000_2022.10.13.511849v1.6","first-page":"e1007749","article-title":"Genome-wide CRISPR-dCas9 screens in E","volume":"14","year":"2018","journal-title":"coli identify essential genes and phage host factors. 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