{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,8]],"date-time":"2026-09-08T23:10:55Z","timestamp":1788909055261,"version":"build-2803163510"},"update-to":[{"DOI":"10.1371\/journal.ppat.1012917","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2025,5,12]],"date-time":"2025-05-12T00:00:00Z","timestamp":1747008000000}}],"reference-count":77,"publisher":"Public Library of Science (PLoS)","issue":"5","license":[{"start":{"date-parts":[[2025,5,2]],"date-time":"2025-05-02T00:00:00Z","timestamp":1746144000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["T32 AI007509"],"award-info":[{"award-number":["T32 AI007509"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["T32 AI055396"],"award-info":[{"award-number":["T32 AI055396"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["R01 AI160130"],"award-info":[{"award-number":["R01 AI160130"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.plospathogens.org"],"crossmark-restriction":false},"short-container-title":["PLoS Pathog"],"abstract":"<jats:p>\n                    Nontyphoidal and enteric fever serovars of\n                    <jats:italic>Salmonella enterica<\/jats:italic>\n                    display distinctive interactions with serum antibodies and the complement system, which initiate the host immune response to invading microbes. This study examines the contributions of lipopolysaccharide O-antigen (O-ag) and the\n                    <jats:italic>S.<\/jats:italic>\n                    Typhi Vi polysaccharide capsule to serum resistance, complement activation and deposition, and immunoglobulin (Ig) binding in nontyphoidal\n                    <jats:italic>S. enterica<\/jats:italic>\n                    serovar Typhimurium and the enteric fever serovars\n                    <jats:italic>S.<\/jats:italic>\n                    Typhi and\n                    <jats:italic>S.<\/jats:italic>\n                    Paratyphi A. Although all three serovars are resistant to serum killing,\n                    <jats:italic>S.<\/jats:italic>\n                    Typhi and\n                    <jats:italic>S.<\/jats:italic>\n                    Paratyphi A exhibit lower levels of Ig binding, complement binding and complement activation compared to\n                    <jats:italic>S.<\/jats:italic>\n                    Typhimurium. In\n                    <jats:italic>S.<\/jats:italic>\n                    Typhimurium, WzzB-dependent long O-antigen (L O-ag) production with 16-to-35 repeating O-ag units, and FepE-dependent very long O-antigen (VL O-ag) production with over 100 repeating O-ag units, are required for serum resistance but do not prevent IgM binding or complement deposition.\n                    <jats:italic>S.<\/jats:italic>\n                    Typhi lacks VL O-ag, but its production of Vi capsule inhibits IgM binding and complement deposition, while acting in concert with L O-ag to resist serum killing. In\n                    <jats:italic>S.<\/jats:italic>\n                    Paratyphi A, L O-ag production is deficient due to a hypofunctional WzzB protein, but this is compensated by greater quantities of VL O-ag, which are required for serum resistance. Restoration of WzzB function by exchange with the\n                    <jats:italic>S.<\/jats:italic>\n                    Typhimurium or\n                    <jats:italic>S.<\/jats:italic>\n                    Typhi\n                    <jats:italic>wzzB<\/jats:italic>\n                    alleles can restore L O-ag production in\n                    <jats:italic>S.<\/jats:italic>\n                    Paratyphi A but decreases VL O-ag production, resulting in increased IgM binding. Replacement of the\n                    <jats:italic>S.<\/jats:italic>\n                    Paratyphi A O2-type polysaccharide with the\n                    <jats:italic>S.<\/jats:italic>\n                    Typhi O9 polysaccharide further increases IgM binding of\n                    <jats:italic>S.<\/jats:italic>\n                    Paratyphi A, which enhances complement activation but not complement deposition. Lastly, a gene duplication of\n                    <jats:italic>rfbV<\/jats:italic>\n                    in\n                    <jats:italic>S.<\/jats:italic>\n                    Paratyphi A is necessary for higher levels of VL O-ag and resistance to complement deposition and antibody binding. Collectively, these observations demonstrate fundamental differences between nontyphoidal and enteric fever\n                    <jats:italic>Salmonella<\/jats:italic>\n                    serovars in their interactions with innate immune effectors. Whereas nontyphoidal\n                    <jats:italic>S.<\/jats:italic>\n                    Typhimurium elicits, exploits and withstands the host acute inflammatory response, the enteric fever serovars\n                    <jats:italic>S.<\/jats:italic>\n                    Typhi and\n                    <jats:italic>S.<\/jats:italic>\n                    Paratyphi A evade it by limiting antibody recognition and complement activation and deposition.\n                  <\/jats:p>","DOI":"10.1371\/journal.ppat.1012917","type":"journal-article","created":{"date-parts":[[2025,5,2]],"date-time":"2025-05-02T13:34:28Z","timestamp":1746192868000},"page":"e1012917","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":4,"title":["Evasion of serum antibodies and complement by Salmonella Typhi and Paratyphi A"],"prefix":"10.1371","volume":"21","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-6968-7205","authenticated-orcid":true,"given":"Fermin E.","family":"Guerra","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joyce E.","family":"Karlinsey","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stephen J.","family":"Libby","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3243-110X","authenticated-orcid":true,"given":"Ferric C.","family":"Fang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2025,5,2]]},"reference":[{"key":"ppat.1012917.ref001","doi-asserted-by":"crossref","first-page":"391","DOI":"10.3389\/fmicb.2014.00391","article-title":"Same species, different diseases: how and why typhoidal and 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