New Diphtheria Toxins Study Findings Have Been Reported from University of Kansas Medical Center (Crucial role of H322 in folding of the diphtheria...

Life Science Weekly |

New Diphtheria Toxins Study Findings Have Been Reported from University of Kansas Medical Center (Crucial role of H322 in folding of the diphtheria toxin T-domain into the open-channel state) By a News Reporter-Staff News Editor at Life Science Weekly -- Investigators publish new report on Biological Factors. According to news reporting out of Kansas City, Kansas, by NewsRx editors, research stated, "The translocation (T) domain plays a key role in the entry of diphtheria toxin into the cell. Upon endosomal acidification, the T-domain undergoes a series of conformational changes that lead to its membrane insertion and formation of a channel." Our news journalists obtained a quote from the research from the University of Kansas Medical Center, "Recently, we have reported that the triple replacement of C-terminal histidines H322, H323, and H372 with glutamines prevents the formation of open channels in planar lipid bilayers. Here, we report that this effect is primarily due to the mutation of H322. We further examine the relationship between the loss of functionality and membrane folding in a series of mutants with C-terminal histidine substitutions using spectroscopic assays. The membrane insertion pathway for the mutants differs from that of the wild type as revealed by the membrane-induced red shift of tryptophan fluorescence at pH 6.0-6.5. T-Domain mutants with replacements at H323 and H372, but not at H322, regain a wild-type-like spectroscopic signature upon further acidification. Circular dichroism measurements confirm that affected mutants misfold during insertion into vesicles. Conductance measurements reveal that substituting H322 dramatically reduces the numbers of properly folded channels in a planar bilayer, but the properties of the active channels appear to be unaltered." According to the news editors, the research concluded: "We propose that H322 plays an important role in the formation of open channels and is involved in guiding the proper insertion of the N-terminal region of the T-domain into the membrane." For more information on this research see: Crucial role of H322 in folding of the diphtheria toxin T-domain into the open-channel state. Biochemistry, 2013;52(20):3457-63. Biochemistry can be contacted at: Springer, 233 Spring Street, New York, NY 10013, USA. (American Chemical Society - www.acs.org; Biochemistry - www.pubs.acs.org/journal/bichaw) Our news journalists report that additional information may be obtained by contacting M. Vargas-Uribe, Dept. of Biochemistry and Molecular Biology, University of Kansas Medical Center , Kansas City, Kansas 66160, United States. Additional authors for this research include M.V. Rodnin, P. Kienker, A. Finkelstein and A.S Ladokhin (see also Biological Factors). Publisher contact information for the journal Biochemistry is: Springer, 233 Spring Street, New York, NY 10013, USA. Keywords for this news article include: Kansas City, United States, Bacterial Toxins, Diphtheria Toxin, Biological Factors, North and Central America. Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2014, NewsRx LLC

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