Functional characterization of the maltose ATP-binding-cassette transporter of Salmonella typhimurium by means of monoclonal antibodies directed against the MalK subunit.

Title:

Functional characterization of the maltose ATP-binding-cassette transporter of Salmonella typhimurium by means of monoclonal antibodies directed against the MalK subunit.

Dataset

identifier:	1865710
description:	epitope description:RVNQVAEVLQL antigen name:Maltose/maltodextrin import ATP-binding protein MalK host organism:Mus musculus BALB/c antibody name:4H12
aggregation:	instance of dataset
availability:	available
primaryPublications:	12180984

Access

authorizations:	registration not required
accessURL:	http://www.iedb.org/reference/1009535
landingPage:	http://www.iedb.org/assay/1865710

Publication

type:	Literature
publicationVenue:	Eur J Biochem
dates:	2002

Dimension

study type:	b cell assays
subject species:	Salmonella enterica subsp. enterica serovar Typhimurium

Person

fullName:	Anke Stein Martina Seifert Rudolf Volkmer-Engert Jö rg Siepelmeyer Knut Jahreis Erwin Schneider

Data Type

method:	antigen inhibition

Study

name:	Functional characterization of the maltose ATP-binding-cassette transporter of Salmonella typhimurium by means of monoclonal antibodies directed against the MalK subunit.
description:	The epitope sequence was deduced. MalK inhibited the binding of the epitope-specific mAb to MalK. Similar results were observed with the MalFGK₂ complex. Binding was reduced by preincubation with ATP, indicating that binding to ATP induces a conformation change in MalK. Similar results were observed with a Fab fragment. The mAb also bound MalK and the MalFGK₂ complex in direct ELISA.

Data Repository

name:	iedb
homePage:	http://www.iedb.org

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