| Literature DB >> 16603378 |
Hongjie Guo1, Kaarina Lokko, Yun Zhang, Wen Yi, Zhengrong Wu, Peng George Wang.
Abstract
O-Antigen plays a critical role in the bacterium-host interplay, the chain length is an important factor in O-antigen functions. Wzz protein is responsible for O-antigen chain length regulation, but the mechanism is still unknown. Here, we overexpressed the Wzz of Escherichia coli O86:H2 in wzz mutant O86:H2 strain, the yield can achieve 15 mg/L. The recombinant Wzz was purified to 99% purity in dodecylmaltoside by sequential Ni-affinity chromatography and anion-exchange. Size exclusion chromatography and in vivo cross-linking experiments both showed that Wzz formed tetramer. Furthermore, analysis with circular dichroism revealed that the predominant structural composition in Wzz is alpha-helices, and incubation with O-antigen significantly changed Wzz conformation. The results suggested that Wzz protein can interact with O-antigen.Entities:
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Year: 2006 PMID： 16603378 DOI： 10.1016/j.pep.2006.01.015
Source DB: PubMed Journal: Protein Expr Purif ISSN： 1046-5928 Impact factor: 1.650