ATTENTION: The software behind KU ScholarWorks is being upgraded to a new version. Starting July 15th, users will not be able to log in to the system, add items, nor make any changes until the new version is in place at the end of July. Searching for articles and opening files will continue to work while the system is being updated. If you have any questions, please contact Marianne Reed at .

Show simple item record

dc.contributor.authorChen, Xiaotong
dc.contributor.authorChoudhari, Shyamal P.
dc.contributor.authorMartinez-Becerra, Francisco J.
dc.contributor.authorKim, Jae Hyun
dc.contributor.authorDickenson, Nicholas E.
dc.contributor.authorToth, Ronald T., IV
dc.contributor.authorJoshi, Sangeeta B.
dc.contributor.authorGreenwood, Jamie C., II
dc.contributor.authorClements, John D.
dc.contributor.authorPicking, William D.
dc.contributor.authorMiddaugh, C. Russell
dc.contributor.authorPicking, Wendy Lynn
dc.identifier.citationChen, Xiaotong et al. “Impact of Detergent on Biophysical Properties and Immune Response of the IpaDB Fusion Protein, a Candidate Subunit Vaccine against Shigella Species.” Ed. S. M. Payne. Infection and Immunity 83.1 (2015): 292–299. PMC. Web. 20 Sept. 2016.en_US
dc.description.abstractShigella spp. are causative agents of bacillary dysentery, a human illness with high global morbidity levels, particularly among elderly and infant populations. Shigella infects via the fecal-oral route, and its virulence is dependent upon a type III secretion system (T3SS). Two components of the exposed needle tip complex of the Shigella T3SS, invasion plasmid antigen D (IpaD) and IpaB, have been identified as broadly protective antigens in the mouse lethal pneumonia model. A recombinant fusion protein (DB fusion) was created by joining the coding sequences of IpaD and IpaB. The DB fusion is coexpressed with IpaB's cognate chaperone, IpgC, for proper recombinant expression. The chaperone can then be removed by using the mild detergents octyl oligooxyethelene (OPOE) or N,N-dimethyldodecylamine N-oxide (LDAO). The DB fusion in OPOE or LDAO was used for biophysical characterization and subsequent construction of an empirical phase diagram (EPD). The EPD showed that the DB fusion in OPOE is most stable at neutral pH below 55°C. In contrast, the DB fusion in LDAO exhibited remarkable thermal plasticity, since this detergent prevents the loss of secondary and tertiary structures after thermal unfolding at 90°C, as well as preventing thermally induced aggregation. Moreover, the DB fusion in LDAO induced higher interleukin-17 secretion and provided a higher protective efficacy in a mouse challenge model than did the DB fusion in OPOE. These data indicate that LDAO might introduce plasticity to the protein, promoting thermal resilience and enhanced protective efficacy, which may be important in its use as a subunit vaccine.en_US
dc.publisherAmerican Society for Microbiologyen_US
dc.rightsCopyright © 2015, American Society for Microbiology. All Rights Reserved.en_US
dc.titleImpact of detergent on biophysical properties and immune response of the IpaDB fusion protein, a candidate subunit vaccine against Shigella species.en_US
kusw.kuauthorPicking, William D.
kusw.kuauthorPicking, Wendy Lynn
kusw.kudepartmentPharmaceutical Chemistryen_US
kusw.oaversionScholarly/refereed, publisher versionen_US
kusw.oapolicyThis item meets KU Open Access policy criteria.en_US

Files in this item


This item appears in the following Collection(s)

Show simple item record