Document Detail


The effects of the carboxyl-terminus amino acids of the Shiga toxin B-subunit on retrograde transport.
MedLine Citation:
PMID:  22552548     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The Shiga toxin B-subunit (STxB), from the enteric pathogen, Shigella dysenteriae, is responsible for the attachment of its receptor, globotriaosylceramide (Gb3), and navigates the retrograde pathway from the plasma membrane to the endoplasmic reticulum (ER). In this study, in order to demonstrate the role of carboxyl-terminus (C-terminus/al) amino acids of the B-fragment on the retrograde transport speed and the retrograde transport pathway, STxB was modified by site-directed mutagenesis and by the addition of an amino acid tail. The results showed that when the C-terminal amino acid, arginine [Arg (R)], was mutated to serine [Ser (S)], the speed of the B-fragment transportation into the ER at 37 ˚C was slower. When an acidic amino acid tail 'glutamine (Glu)-Ser' (ES) was added to the C-terminal amino acid 'R', the B-fragment transporting speed slowed down and remained in the Golgi apparatus. Further experiments showed that the effects induced by mutations of the amino acid tail resulted in STxB-EEEES ≥-EEES>-EES>-ES, demonstrating that the retardation effect on the tail was increased and the length of the acidic amino acid was augmented. The effect was possibly produced by an acidic amino acid tail, not only by the amino acid 'E'. The significant inhibitory effect on the speed of B-fragment retrograde transport was observed only when the mutations of the acidic amino acid tail were linked near to the C-terminus. These results may provide important insights for the study of transport mechanisms and for the development of STxB serial proteins as vectors for drug delivery.
Authors:
Dan Liu; Yuying Fan; Jie Li; Xiaoge Gao; Miao Hao; Huiting Xue; Guihua Tai
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-04-23
Journal Detail:
Title:  Molecular medicine reports     Volume:  6     ISSN:  1791-3004     ISO Abbreviation:  Mol Med Rep     Publication Date:  2012 Jul 
Date Detail:
Created Date:  2012-05-09     Completed Date:  2012-09-10     Revised Date:  2013-02-22    
Medline Journal Info:
Nlm Unique ID:  101475259     Medline TA:  Mol Med Rep     Country:  Greece    
Other Details:
Languages:  eng     Pagination:  220-6     Citation Subset:  IM    
Affiliation:
School of Life Sciences, Northeast Normal University, Changchun, Jilin 130024, PR China.
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MeSH Terms
Descriptor/Qualifier:
Amino Acids / metabolism*
Amino Acids, Acidic / metabolism
Base Sequence
Biological Transport
HeLa Cells
Humans
Molecular Sequence Data
Mutagenesis, Site-Directed
Shiga Toxins / chemistry*,  genetics,  metabolism*
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Amino Acids, Acidic; 0/Shiga Toxins; 0/stxB toxin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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