{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,12]],"date-time":"2026-09-12T04:01:36Z","timestamp":1789185696965,"version":"build-2803163510"},"reference-count":28,"publisher":"American Society for Microbiology","issue":"9","license":[{"start":{"date-parts":[[2010,9,1]],"date-time":"2010-09-01T00:00:00Z","timestamp":1283299200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Infect Immun"],"published-print":{"date-parts":[[2010,9]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            <jats:italic>Pasteurella multocida<\/jats:italic>\n            is the causative agent of a number of diseases in animals, including fowl cholera.\n            <jats:italic>P. multocida<\/jats:italic>\n            strains simultaneously express two lipopolysaccharide (LPS) glycoforms (glycoforms A and B) that differ only in their inner core structure. Glycoform A contains a single 3-deoxy-\n            <jats:sc>d<\/jats:sc>\n            -\n            <jats:italic>manno<\/jats:italic>\n            -octulosonic acid (Kdo) residue that is phosphorylated by the Kdo kinase, KdkA, whereas glycoform B contains two unphosphorylated Kdo residues. We have previously shown that\n            <jats:italic>P. multocida<\/jats:italic>\n            mutants lacking the heptosyltransferase, HptA, produce full-length glycoform B LPS and a large amount of truncated glycoform A LPS, as they cannot add heptose to the glycoform A inner core. These\n            <jats:italic>hptA<\/jats:italic>\n            mutants were attenuated in chickens because the truncated LPS made them vulnerable to host defense mechanisms, including antimicrobial peptides. However, here we show that birds inoculated with high doses of the\n            <jats:italic>hptA<\/jats:italic>\n            mutant developed fowl cholera and the\n            <jats:italic>P. multocida<\/jats:italic>\n            isolates recovered from diseased birds no longer expressed truncated LPS. Sequencing analysis revealed that the\n            <jats:italic>in vivo<\/jats:italic>\n            -derived isolates had mutations in\n            <jats:italic>kdkA<\/jats:italic>\n            , thereby suppressing the production of glycoform A LPS. Interestingly, a number of the spontaneous KdkA mutant strains produced KdkA with a single amino acid substitution (A112V, R123P, H168Y, or D193N). LPS structural analysis showed that complementation of a\n            <jats:italic>P. multocida kdkA<\/jats:italic>\n            mutant with wild-type\n            <jats:italic>kdkA<\/jats:italic>\n            restored expression of glycoform A to wild-type levels, whereas complementation with any of the mutated\n            <jats:italic>kdkA<\/jats:italic>\n            genes did not. We conclude that in\n            <jats:italic>P. multocida<\/jats:italic>\n            KdkA, the amino acids A112, R123, H168, and D193 are critical for Kdo kinase function and therefore for glycoform A LPS assembly.\n          <\/jats:p>","DOI":"10.1128\/iai.00457-10","type":"journal-article","created":{"date-parts":[[2010,6,22]],"date-time":"2010-06-22T02:00:21Z","timestamp":1277172021000},"page":"3669-3677","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":10,"title":["Natural Selection in the Chicken Host Identifies 3-Deoxy-\n            <scp>d<\/scp>\n            -\n            <i>manno<\/i>\n            - Octulosonic Acid Kinase Residues Essential for Phosphorylation of\n            <i>Pasteurella multocida<\/i>\n            Lipopolysaccharide"],"prefix":"10.1128","volume":"78","author":[{"given":"Marina","family":"Harper","sequence":"first","affiliation":[{"name":"Australian Research Council Centre of Excellence in Structural and Functional Microbial Genomics, Monash University, Clayton, VIC 3800, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrew D.","family":"Cox","sequence":"additional","affiliation":[{"name":"Institute for Biological Sciences, National Research Council, Ottawa, ON K1AOR6, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Frank","family":"St. Michael","sequence":"additional","affiliation":[{"name":"Institute for Biological Sciences, National Research Council, Ottawa, ON K1AOR6, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mark","family":"Ford","sequence":"additional","affiliation":[{"name":"CSIRO Livestock Industries, Australian Animal Health Laboratory, Geelong, VIC 3220, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ian W.","family":"Wilkie","sequence":"additional","affiliation":[{"name":"Veterinary Pathology and Anatomy, University of Queensland, St. Lucia, QLD 4072, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ben","family":"Adler","sequence":"additional","affiliation":[{"name":"Australian Research Council Centre of Excellence in Structural and Functional Microbial Genomics, Monash University, Clayton, VIC 3800, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John D.","family":"Boyce","sequence":"additional","affiliation":[{"name":"Australian Research Council Centre of Excellence in Structural and Functional Microbial Genomics, Monash University, Clayton, VIC 3800, Australia"},{"name":"Department of Microbiology, Monash University, Clayton, VIC 3800, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","unstructured":"Current protocols in molecular biology 1995 vol. 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