{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,14]],"date-time":"2026-10-14T01:47:05Z","timestamp":1791942425815,"version":"4.3.4"},"reference-count":66,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2008,2,14]],"date-time":"2008-02-14T00:00:00Z","timestamp":1202947200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["enviromicro-journals.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Environmental Microbiology"],"published-print":{"date-parts":[[2008,6]]},"abstract":"<jats:title>Summary<\/jats:title>\n                  <jats:p>\n                    Primarily, three operons,\n                    <jats:italic>hmsHFRS, hmsT<\/jats:italic>\n                    and\n                    <jats:italic>hmsP<\/jats:italic>\n                    , are responsible for the development of a\n                    <jats:italic>Yersinia pestis<\/jats:italic>\n                    biofilm, which is essential for blockage\u2010dependent transmission of plague from fleas to mammals. Here, using specific antibodies, a polymeric \u03b2\u20101,6\u2010\n                    <jats:italic>N<\/jats:italic>\n                    \u2010acetyl\u2010\n                    <jats:sc>d<\/jats:sc>\n                    \u2010glucosamine\u2010like polysaccharide was detected in the extracellular matrix of\n                    <jats:italic>hmsHFRS<\/jats:italic>\n                    \u2010dependent\n                    <jats:italic>Y.\u2003pestis<\/jats:italic>\n                    biofilm. The production of this exopolysaccharide (EPS) was controlled by diguanylate cyclase HmsT and EAL domain phosphodiesterase HmsP, acting as positive and negative regulators respectively. Cellular compartmentalization of soluble segments of Hms inner membrane proteins, including the putative glycosyltransferase domain of HmsR, the diguanylate cyclase\/GGDEF domain of HmsT and the phosphodiesterase\/EAL domain of HmsP, was determined by a combination of topology prediction algorithms and construction of C\u2010terminal translational fusions with \u03b2\u2010galactosidase and alkaline phosphatase. Multiple interactions of Hms inner membrane proteins were detected using bacterial cAMP based two\u2010hybrid system. Biochemical analyses confirmed some of these protein\u2013protein interactions. Our results indicate that synthesis and regulation of the\n                    <jats:italic>Y.\u2003pestis<\/jats:italic>\n                    biofilm EPS occurs in the cytoplasm by a proposed Hms enzymatic complex.\n                  <\/jats:p>","DOI":"10.1111\/j.1462-2920.2007.01554.x","type":"journal-article","created":{"date-parts":[[2008,2,15]],"date-time":"2008-02-15T01:50:24Z","timestamp":1203040224000},"page":"1419-1432","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":137,"title":["Insights into\n                    <i>Yersinia pestis<\/i>\n                    biofilm development: topology and co\u2010interaction of Hms inner membrane proteins involved in exopolysaccharide production"],"prefix":"10.1111","volume":"10","author":[{"given":"Alexander 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