Document Detail


Bacterial invasion of eukaryotic cells can be mediated by actin-hydrolysing metalloproteases grimelysin and protealysin.
MedLine Citation:
PMID:  20849390     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Earlier, we have shown that spontaneously isolated non-pathogenic bacteria Serratia grimesii and Serratia proteamaculans invade eukaryotic cells, provided that they synthesize thermolysin-like metalloproteases ECP32/grimelysin or protealysin characterized by high specificity towards actin. To address the question of whether the proteases are active players in entry of these bacteria into host cells, in this work, human larynx carcinoma Hep-2 cells were infected with recombinant Escherichia coli expressing grimelysin or protealysin. Using confocal and electron microscopy, we have found that the recombinant bacteria, whose extracts limitedly cleaved actin, were internalized within the eukaryotic cells residing both in vacuoles and free in cytoplasm. The E. coli-carrying plasmids without inserts of grimelysin or protealysin gene did not enter Hep-2 cells. Moreover, internalization of non-invasive E. coli was not observed in the presence of protealysin introduced into the culture medium. These results are consistent with the direct participation of ECP32/grimelysin and protealysin in entry of bacteria into the host cells. We assume that ECP32/grimelysin and protealysin mediate invasion being injected into the eukaryotic cell and that the high specificity of the enzyme towards actin may be a factor contributed to the bacteria internalization.
Authors:
Ekaterina S Bozhokina; Olga A Tsaplina; Tatiana N Efremova; Ludmila V Kever; Ilya V Demidyuk; Sergey V Kostrov; Thomas Adam; Yan Yu Komissarchik; Sofia Yu Khaitlina
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Cell biology international     Volume:  35     ISSN:  1095-8355     ISO Abbreviation:  Cell Biol. Int.     Publication Date:  2011 Feb 
Date Detail:
Created Date:  2011-01-25     Completed Date:  2011-05-03     Revised Date:  2012-08-02    
Medline Journal Info:
Nlm Unique ID:  9307129     Medline TA:  Cell Biol Int     Country:  England    
Other Details:
Languages:  eng     Pagination:  111-8     Citation Subset:  IM    
Affiliation:
Institute of Cytology, Russian Academy of Sciences, Tikhoretsky pr. 4, 194064, St. Petersburg, Russia.
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MeSH Terms
Descriptor/Qualifier:
Actins / metabolism*
Bacterial Proteins / genetics,  metabolism*
Endopeptidases / genetics,  metabolism*
Escherichia coli / enzymology
Eukaryotic Cells / microbiology*
HeLa Cells
Hep G2 Cells
Humans
Hydrolysis
Microscopy, Electron
Microscopy, Fluorescence
Plasmids
Recombinant Proteins / genetics,  metabolism
Chemical
Reg. No./Substance:
0/Actins; 0/Bacterial Proteins; 0/Recombinant Proteins; EC 3.4.-/Endopeptidases; EC 3.4.-/proteinase ECP 32

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