{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,9]],"date-time":"2026-09-09T02:58:33Z","timestamp":1788922713071,"version":"build-2803163510"},"reference-count":57,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2008,11,17]],"date-time":"2008-11-17T00:00:00Z","timestamp":1226880000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biopolymers"],"published-print":{"date-parts":[[2009,3]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The anti\u2010lipopolysaccharide factor ALF\u2010<jats:italic>Pm3<\/jats:italic> is a 98\u2010residue protein identified in hemocytes from the black tiger shrimp <jats:italic>Penaeus monodon<\/jats:italic>. It was expressed in <jats:italic>Pichia pastoris<\/jats:italic> from the constitutive glyceraldehyde\u20103\u2010phosphate dehydrogenase promoter as a folded and <jats:sup>15<\/jats:sup>N uniformly labeled <jats:italic>r<\/jats:italic>ALF\u2010<jats:italic>Pm3<\/jats:italic> protein. Its 3D structure was established by NMR and consists of three \u03b1\u2010helices packed against a four\u2010stranded \u03b2\u2010sheet. The C<jats:sup>34<\/jats:sup>\uf8ffC<jats:sup>55<\/jats:sup> disulfide bond was shown to be essential for the structure stability. By using surface plasmon resonance, we demonstrated that <jats:italic>r<\/jats:italic>ALF\u2010<jats:italic>Pm3<\/jats:italic> binds to LPS, lipid A and to OM\u00ae\u2010174, a soluble analogue of lipid A. Biophysical studies of <jats:italic>r<\/jats:italic>ALF\u2010<jats:italic>Pm3<\/jats:italic>\/LPS and <jats:italic>r<\/jats:italic>ALF\u2010<jats:italic>Pm3<\/jats:italic>\/OM\u00ae\u2010174 complexes indicated rather high molecular sized aggregates, which prevented us to experimentally determine by NMR the binding mode of these lipids to rALF\u2010<jats:italic>Pm3<\/jats:italic>. However, on the basis of striking structural similarities to the FhuA\/LPS complex, we designed an original model of the possible lipid A\u2010binding site of ALF\u2010<jats:italic>Pm3<\/jats:italic>. Such a binding site, located on the ALF\u2010<jats:italic>Pm3<\/jats:italic> \u03b2\u2010sheet and involving seven charged residues, is well conserved in ALF\u2010L from <jats:italic>Limulus polyphemus<\/jats:italic> and in ALF\u2010T from <jats:italic>Tachypleus tridentatus<\/jats:italic>. In addition, our model is in agreement with experiments showing that \u03b2\u2010hairpin synthetic peptides corresponding to ALF\u2010L \u03b2\u2010sheet bind to LPS. Delineating lipid A\u2010binding site of ALFs will help go further in the <jats:italic>de novo<\/jats:italic> design of new antibacterial or LPS\u2010neutralizing drugs. \u00a9 2008 Wiley Periodicals, Inc. Biopolymers 91: 207\u2013220, 2009.<\/jats:p><jats:p>This article was originally published online as an accepted preprint. The \u201cPublished Online\u201d date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com<\/jats:p>","DOI":"10.1002\/bip.21119","type":"journal-article","created":{"date-parts":[[2008,11,17]],"date-time":"2008-11-17T20:58:15Z","timestamp":1226955495000},"page":"207-220","source":"Crossref","is-referenced-by-count":78,"title":["NMR structure of <i>r<\/i>ALF\u2010<i>Pm3<\/i>, an anti\u2010lipopolysaccharide factor from shrimp: Model of the possible lipid A\u2010binding 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