{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,13]],"date-time":"2026-05-13T04:30:58Z","timestamp":1778646658207,"version":"3.51.4"},"reference-count":32,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2007,9,18]],"date-time":"2007-09-18T00:00:00Z","timestamp":1190073600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biotech &amp; Bioengineering"],"published-print":{"date-parts":[[2008,3]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Spores of <jats:italic>Bacillus anthracis<\/jats:italic>, the causative agent of anthrax, are enclosed by an exosporium, which consists of a basal layer surrounded by a nap of hair\u2010like filaments. The major structural component of the filaments is called BclA, which comprises a central collagen\u2010like region (CLR) and a globular C\u2010terminal domain. Here, the entire CLR coding sequence of BclA was removed, and the resulting protein (tBclA) produced in <jats:italic>Escherichia coli<\/jats:italic>. The crystallographic structure of tBclA was determined to 1.35 \u00c5 resolution, and consists of an all\u2010\u03b2 structure with a TNF\u2010like jelly fold topology (12 \u03b2\u2010strands which form 2 \u03b2\u2010sheets of five strands each) consistent with previous studies on wild\u2010type BclA. These globular domains are tightly packed into trimeric structures (surface shape complementarity; <jats:italic>S<\/jats:italic>\n<jats:sub>c<\/jats:sub>\u2009=\u20090.83), demonstrating that formation of the core structure of BclA is independent of the anchoring collagen\u2010like region. A polyclonal antibody raised against tBclA recognized <jats:italic>B. anthracis<\/jats:italic> spores directly, and showed little cross\u2010reactivity (&lt;10%) with the spores of the closely related species <jats:italic>Bacillus cereus<\/jats:italic> and <jats:italic>Bacillus thuringiensis<\/jats:italic>, when compared to two other polyclonal antibodies raised against <jats:italic>B. anthracis<\/jats:italic> spore extracts and inactivated spores. The tBclA protein was used to purify a pool of specific antibodies from bovine colostrum whey samples from cows inoculated with the Sterne strain anthrax vaccine, which also showed reactivity with <jats:italic>B. anthracis<\/jats:italic> spores. Together, these results demonstrate that tBclA provides a safer and more effective way to the production and purification of antibodies with high binding affinity for <jats:italic>B. anthracis<\/jats:italic> spores. Biotechnol. Bioeng. 2008;99: 774\u2013782. \u00a9 2007 Wiley Periodicals, Inc.<\/jats:p>","DOI":"10.1002\/bit.21637","type":"journal-article","created":{"date-parts":[[2007,9,18]],"date-time":"2007-09-18T19:19:07Z","timestamp":1190143147000},"page":"774-782","source":"Crossref","is-referenced-by-count":15,"title":["Construction, crystal structure and application of a recombinant protein that lacks the collagen\u2010like region of BclA from <i>Bacillus anthracis<\/i> spores"],"prefix":"10.1002","volume":"99","author":[{"given":"Chun\u2010Qiang","family":"Liu","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Stewart D.","family":"Nuttall","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hung","family":"Tran","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Michelle","family":"Wilkins","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Victor A.","family":"Streltsov","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Malcolm R.","family":"Alderton","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2008,1,25]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1128\/JB.187.15.5310-5317.2005"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.01202-06"},{"issue":"5","key":"e_1_2_1_4_1","doi-asserted-by":"crossref","first-page":"760","DOI":"10.1107\/S0907444994003112","article-title":"The CCP4 suite: Programs for protein crystallography","volume":"50","author":"CCP4","year":"1994","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_2_1_5_1","volume-title":"Molecular methods for Bacillus","author":"Cutting SM","year":"1990"},{"key":"e_1_2_1_6_1","doi-asserted-by":"publisher","DOI":"10.1128\/AEM.67.8.3665-3670.2001"},{"key":"e_1_2_1_7_1","doi-asserted-by":"publisher","DOI":"10.1056\/NEJM199909093411107"},{"key":"e_1_2_1_8_1","first-page":"1504","article-title":"Cytology of Bacillus anthracis","volume":"26","author":"Gerhardt P","year":"1967","journal-title":"Fed Proc"},{"key":"e_1_2_1_9_1","doi-asserted-by":"publisher","DOI":"10.1128\/JB.91.6.2382-2384.1966"},{"key":"e_1_2_1_10_1","doi-asserted-by":"publisher","DOI":"10.1128\/AEM.69.1.593-599.2003"},{"key":"e_1_2_1_11_1","doi-asserted-by":"publisher","DOI":"10.1016\/0263-7855(96)00018-5"},{"key":"e_1_2_1_12_1","doi-asserted-by":"publisher","DOI":"10.1017\/S0007114500002282"},{"key":"e_1_2_1_13_1","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1993.1648"},{"key":"e_1_2_1_14_1","doi-asserted-by":"publisher","DOI":"10.1097\/01.revmedmi.0000184744.83303.9a"},{"key":"e_1_2_1_15_1","doi-asserted-by":"publisher","DOI":"10.1006\/jsbi.1999.4094"},{"key":"e_1_2_1_16_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.micro.55.1.647"},{"key":"e_1_2_1_17_1","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444996012255"},{"key":"e_1_2_1_18_1","doi-asserted-by":"publisher","DOI":"10.1128\/MMBR.64.3.548-572.2000"},{"key":"e_1_2_1_19_1","first-page":"307","volume-title":"Methods in enzymology. 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