Next Article in Journal
Putative Nonribosomal Peptide Synthetase and Cytochrome P450 Genes Responsible for Tentoxin Biosynthesis in Alternaria alternata ZJ33
Next Article in Special Issue
Auranofin Inhibits the Enzyme Activity of Pasteurella multocida Toxin PMT in Human Cells and Protects Cells from Intoxication
Previous Article in Journal
Hydrolytic Fate of 3/15-Acetyldeoxynivalenol in Humans: Specific Deacetylation by the Small Intestine and Liver Revealed Using in Vitro and ex Vivo Approaches
Open AccessArticle

Selective Membrane Redistribution and Depletion of Gαq-Protein by Pasteurella multocida Toxin

Department of Microbiology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA
Author to whom correspondence should be addressed.
Current address: School of Biotechnology, Southern Medical University, Guangzhou 510515, China.
Academic Editor: Katharina Kubatzky
Toxins 2016, 8(8), 233;
Received: 15 June 2016 / Revised: 22 July 2016 / Accepted: 25 July 2016 / Published: 1 August 2016
(This article belongs to the Special Issue Pasteurella multocida and Its Virulence Factors)
Pasteurella multocida toxin (PMT), the major virulence factor responsible for zoonotic atrophic rhinitis, is a protein deamidase that activates the alpha subunit of heterotrimeric G proteins. Initial activation of G alpha-q-coupled phospholipase C-beta-1 signaling by PMT is followed by uncoupling of G alpha-q-dependent signaling, causing downregulation of downstream calcium and mitogenic signaling pathways. Here, we show that PMT decreases endogenous and exogenously expressed G alpha-q protein content in host cell plasma membranes and in detergent resistant membrane (DRM) fractions. This membrane depletion of G alpha-q protein was dependent upon the catalytic activity of PMT. Results indicate that PMT-modified G alpha-q redistributes within the host cell membrane from the DRM fraction into the soluble membrane and cytosolic fractions. In contrast, PMT had no affect on G alpha-s or G beta protein levels, which are not substrate targets of PMT. PMT also had no affect on G alpha-11 levels, even though G alpha-11 can serve as a substrate for deamidation by PMT, suggesting that membrane depletion of PMT-modified G-alpha-q has specificity. View Full-Text
Keywords: dermonecrosis; Pasteurella multocida; G-protein downregulation; mitogen; deamidation dermonecrosis; Pasteurella multocida; G-protein downregulation; mitogen; deamidation
Show Figures

Graphical abstract

MDPI and ACS Style

Clemons, N.C.; Luo, S.; Ho, M.; Wilson, B.A. Selective Membrane Redistribution and Depletion of Gαq-Protein by Pasteurella multocida Toxin. Toxins 2016, 8, 233.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

Search more from Scilit
Back to TopTop