{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,1]],"date-time":"2026-05-01T00:47:33Z","timestamp":1777596453973,"version":"3.51.4"},"reference-count":52,"publisher":"Cambridge University Press (CUP)","issue":"11","license":[{"start":{"date-parts":[[2015,7,9]],"date-time":"2015-07-09T00:00:00Z","timestamp":1436400000000},"content-version":"unspecified","delay-in-days":0,"URL":"https:\/\/www.cambridge.org\/core\/terms"}],"content-domain":{"domain":["journals.cambridge.org"],"crossmark-restriction":true},"short-container-title":["Parasitology"],"published-print":{"date-parts":[[2015,9]]},"abstract":"<jats:title>SUMMARY<\/jats:title><jats:p>Heat shock protein 90 (HSP90) is a key component of the molecular chaperone complex essential for activating many signalling proteins involved in the development and progression of pathogenic cellular transformation. A<jats:italic>Hsp90<\/jats:italic>gene (<jats:italic>BQHsp90<\/jats:italic>) was cloned and characterized from<jats:italic>Babesia<\/jats:italic>sp. BQ1 (Lintan), an ovine<jats:italic>Babesia<\/jats:italic>isolate belonging to<jats:italic>Babesia motasi<\/jats:italic>-like group, by screening a cDNA expression library and performing rapid amplification of cDNA ends. The full-length cDNA of<jats:italic>BQHsp90<\/jats:italic>is 2399 bp with an open reading frame of 2154 bp encoding a predicted 83 kDa polypeptide with 717 amino acid residues. It shows significant homology and similar structural characteristics to<jats:italic>Hsp90<\/jats:italic>of other apicomplex organisms. Phylogenetic analysis, based on the HSP90 amino acid sequences, showed that the<jats:italic>Babesia<\/jats:italic>genus is clearly separated from other apicomplexa genera. Five Chinese ovine<jats:italic>Babesia<\/jats:italic>isolates were divided into 2 phylogenetic clusters, namely<jats:italic>Babesia<\/jats:italic>sp. Xinjiang (previously designated a new species) cluster and<jats:italic>B. motasi<\/jats:italic>-like cluster which could be further divided into 2 subclusters (<jats:italic>Babesia<\/jats:italic>sp. BQ1 (Lintan)\/<jats:italic>Babesia<\/jats:italic>sp. Tianzhu and<jats:italic>Babesia<\/jats:italic>sp. BQ1 (Ningxian)\/<jats:italic>Babesia<\/jats:italic>sp. Hebei). Finally, the antigenicity of rBQHSP90 protein from prokaryotic expression was also evaluated using western blot and enzyme-linked immunosorbent assay (ELISA).<\/jats:p>","DOI":"10.1017\/s0031182015000797","type":"journal-article","created":{"date-parts":[[2015,7,9]],"date-time":"2015-07-09T05:37:52Z","timestamp":1436420272000},"page":"1387-1397","update-policy":"https:\/\/doi.org\/10.1017\/policypage","source":"Crossref","is-referenced-by-count":8,"title":["A member of the HSP90 family from ovine<i>Babesia<\/i>in China: molecular characterization, phylogenetic analysis and 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