Document Detail

Sphingomyelin is important for the cellular entry and intracellular localization of Helicobacter pylori VacA.
MedLine Citation:
PMID:  20545942     Owner:  NLM     Status:  MEDLINE    
Plasma membrane sphingomyelin (SM) binds the Helicobacter pylori vacuolating toxin (VacA) to the surface of epithelial cells. To evaluate the importance of SM for VacA cellular entry, we characterized toxin uptake and trafficking within cells enriched with synthetic variants of SM, whose intracellular trafficking properties are strictly dependent on the acyl chain lengths of their sphingolipid backbones. While toxin binding to the surface of cells was independent of acyl chain length, cells enriched with 12- or 18-carbon acyl chain variants of SM (e.g. C12-SM or C18-SM) were more sensitive to VacA, as indicated by toxin-induced cellular vacuolation, than those enriched with shorter 2- or 6-carbon variants (e.g. C2-SM or C6-SM). In C18-SM-enriched cells, VacA was taken into cells by a previously described Cdc42-dependent pinocytic mechanism, localized initially to GPI-enriched vesicles, and ultimately trafficked to Rab7/Lamp1 compartments. In contrast, within C2-SM-enriched cells, VacA was taken up at a slower rate by a Cdc42-independent mechanism and trafficked to Rab11 compartments. VacA-associated predominantly with detergent-resistant membranes (DRMs) in cells enriched with C18-SM, but predominantly with non-DRMs in C2-SM-enriched cells. These results suggest that SM is required for targeting VacA to membrane rafts important for subsequent Cdc42-dependent pinocytic cellular entry.
Vijay R Gupta; Brenda A Wilson; Steven R Blanke
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural    
Journal Detail:
Title:  Cellular microbiology     Volume:  12     ISSN:  1462-5822     ISO Abbreviation:  Cell. Microbiol.     Publication Date:  2010 Oct 
Date Detail:
Created Date:  2010-11-05     Completed Date:  2010-12-21     Revised Date:  2013-05-29    
Medline Journal Info:
Nlm Unique ID:  100883691     Medline TA:  Cell Microbiol     Country:  England    
Other Details:
Languages:  eng     Pagination:  1517-33     Citation Subset:  IM    
Copyright Information:
© 2010 Blackwell Publishing Ltd.
Department of Microbiology, Institute for Genomic Biology, University of Illinois, B103 CLSL, 601 South Goodwin Avenue, Urbana, IL 61801, USA.
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MeSH Terms
Bacterial Proteins / metabolism*
Cell Line
Cell Membrane / chemistry,  physiology*
Epithelial Cells / chemistry,  physiology*
Helicobacter pylori / pathogenicity*
Protein Transport
Sphingomyelins / metabolism*
Virulence Factors / metabolism*
cdc42 GTP-Binding Protein / metabolism
Grant Support
Reg. No./Substance:
0/Bacterial Proteins; 0/Sphingomyelins; 0/VacA protein, Helicobacter pylori; 0/Virulence Factors; EC GTP-Binding Protein

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