Document Detail


Rac1, RhoA, and Cdc42 participate in HeLa cell invasion by group B streptococcus.
MedLine Citation:
PMID:  17517067     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The group B streptococcus (GBS) is an important human pathogen with the ability to cause invasive disease. To do so, the bacteria must invade host cells. It has been well documented that GBS are able to invade a variety of nonphagocytic host cell types, and this process is thought to involve a number of pathogen-host cell interactions. While some of the molecular aspects of the GBS-host cell invasion process have been characterized, many events still remain unclear. The objective of this investigation was to evaluate the role of the Rho-family GTPases Rac, Rho, and Cdc42 in GBS invasion into epithelial cells. The epithelial cell invasion process was modeled using HeLa 229 cell culture. Treatment of HeLa cells with 10 microM compactin, a pan-GTPase inhibitor, abolished GBS internalization, suggesting that GTPases are involved in the GBS invasion process. The addition of Toxin B or exoenzyme C3 to HeLa cells before GBS infection reduced invasion by 50%, further suggesting that the Rho-family GTPases are involved in GBS entry. Examining invasion of GBS into HeLa cells with altered genetic backgrounds was used to confirm these findings; GBS invasion into HeLa cells transiently transfected with dominant negative Rac1, Cdc42, or RhoA reduced invasion by 75%, 51%, and 42%, respectively. Results of this study suggest that the Rho-family GTPases are required for efficient invasion of HeLa cells by GBS.
Authors:
Carey-Ann D Burnham; Sandra E Shokoples; Gregory J Tyrrell
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2007-05-21
Journal Detail:
Title:  FEMS microbiology letters     Volume:  272     ISSN:  0378-1097     ISO Abbreviation:  FEMS Microbiol. Lett.     Publication Date:  2007 Jul 
Date Detail:
Created Date:  2007-06-21     Completed Date:  2007-09-21     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7705721     Medline TA:  FEMS Microbiol Lett     Country:  England    
Other Details:
Languages:  eng     Pagination:  8-14     Citation Subset:  IM    
Affiliation:
The Department of Laboratory Medicine and Pathology, The University of Alberta, Edmonton, AB, Canada.
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MeSH Terms
Descriptor/Qualifier:
ADP Ribose Transferases / toxicity
Bacterial Proteins / toxicity
Bacterial Toxins / toxicity
Botulinum Toxins / toxicity
Colony Count, Microbial / methods
Enzyme Inhibitors / pharmacology
Epithelial Cells / microbiology*
GTP Phosphohydrolases / antagonists & inhibitors
Hela Cells
Humans
Lovastatin / analogs & derivatives,  pharmacology
Streptococcus agalactiae / growth & development*,  physiology
Transfection
cdc42 GTP-Binding Protein / genetics,  physiology*
rac1 GTP-Binding Protein / genetics,  physiology*
rhoA GTP-Binding Protein / genetics,  physiology*
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Bacterial Toxins; 0/Botulinum Toxins; 0/Enzyme Inhibitors; 0/toxB protein, Clostridium difficile; 73573-88-3/compactin; 75330-75-5/Lovastatin; EC 2.4.2.-/ADP Ribose Transferases; EC 2.4.2.-/exoenzyme C3, Clostridium botulinum; EC 3.6.1.-/GTP Phosphohydrolases; EC 3.6.5.2/cdc42 GTP-Binding Protein; EC 3.6.5.2/rac1 GTP-Binding Protein; EC 3.6.5.2/rhoA GTP-Binding Protein

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


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