Source:http://linkedlifedata.com/resource/pubmed/id/20940265
Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
2011-2-1
|
| pubmed:abstractText |
ADP-ribosylation of host cell proteins is a common mode of cell intoxication by pathogenic bacterial toxins. Antibodies induced by immunization with inactivated ADP-ribosylating toxins provide efficient protection in case of some secreted toxins, e.g., diphtheria and pertussis toxins. However, other ADP-ribosylating toxins, such as Salmonella SpvB toxin, are secreted directly from the Salmonella-containing vacuole into the cytosol of target cells via the SPI-2 encoded bacterial type III secretion system, and thus are inaccessible to conventional antibodies. Small-molecule ADP-ribosylation inhibitors are fraught with potential side effects caused by inhibition of endogenous ADP-ribosyltransferases. Here, we report the development of a single-domain antibody from an immunized llama that blocks the capacity of SpvB to ADP-ribosylate actin at a molar ratio of 1:1. The single-domain antibody, when expressed as an intrabody, effectively protected cells from the cytotoxic activity of a translocation-competent chimeric C2IN-C/SpvB toxin. Transfected cells were also protected against cytoskeletal alterations induced by wild-type SpvB-expressing strains of Salmonella. This proof of principle paves the way for developing new antidotes against intracellular toxins.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ADP Ribose Transferases,
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Toxins,
http://linkedlifedata.com/resource/pubmed/chemical/Virulence Factors
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
1530-6860
|
| pubmed:author | |
| pubmed:issnType |
Electronic
|
| pubmed:volume |
25
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
526-34
|
| pubmed:meshHeading |
pubmed-meshheading:20940265-ADP Ribose Transferases,
pubmed-meshheading:20940265-Actins,
pubmed-meshheading:20940265-Amino Acid Sequence,
pubmed-meshheading:20940265-Animals,
pubmed-meshheading:20940265-Antibodies, Bacterial,
pubmed-meshheading:20940265-Bacterial Toxins,
pubmed-meshheading:20940265-Camelids, New World,
pubmed-meshheading:20940265-Cell Line,
pubmed-meshheading:20940265-Cercopithecus aethiops,
pubmed-meshheading:20940265-Cloning, Molecular,
pubmed-meshheading:20940265-Gene Expression Regulation,
pubmed-meshheading:20940265-Macrophages,
pubmed-meshheading:20940265-Mice,
pubmed-meshheading:20940265-Molecular Sequence Data,
pubmed-meshheading:20940265-Protein Structure, Tertiary,
pubmed-meshheading:20940265-Salmonella typhimurium,
pubmed-meshheading:20940265-Vero Cells,
pubmed-meshheading:20940265-Virulence Factors
|
| pubmed:year |
2011
|
| pubmed:articleTitle |
Single-domain llama antibodies as specific intracellular inhibitors of SpvB, the actin ADP-ribosylating toxin of Salmonella typhimurium.
|
| pubmed:affiliation |
Fundación Instituto Leloir, Instituto de Investigaciones Bioquímicas de Buenos Aires–Consejo Nacional de Investigaciones Cientificas y Tecnicas, Buenos Aires, Argentina.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|