Identification and characterization of a porcine-specific transferrin receptor in Actinobacillus pleuropneumoniae.
All six strains of Actinobacillus pleuropneumoniae screened for the ability to use different transferrins as a source of iron for growth were capable of using porcine but not human, bovine, or avian transferrins. A specific binding activity for porcine transferrin (pTf) was expressed in cells grown in the presence of specific iron-chelators and was repressed by addition of excess iron. Two iron-repressible outer-membrane proteins of 105 and 56 kD were specifically isolated from serotype 1, 2 and 7 strains of A. pleuropneumoniae by an affinity-isolation method using biotinylated porcine transferrin and streptavidin-agarose.
Gonzalez
G C
GC
Department of Microbiology and Infectious Diseases, University of Calgary, Alberta, Canada.
Caamano
D L
DL
Schryvers
A B
AB
D000188:Actinobacillus / Q000254:growth & development / Q000378:metabolism*; D000818:Animals; D001426:Bacterial Proteins; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007501:Iron / Q000494:pharmacology; D007502:Iron Chelating Agents / Q000494:pharmacology; D011990:Receptors, Transferrin / Q000302:isolation & purification / Q000378:metabolism*; D013045:Species Specificity; D019809:Streptavidin; D013552:Swine; D014168:Transferrin / Q000378:metabolism*
D001426:Bacterial Proteins; D007502:Iron Chelating Agents; D011990:Receptors, Transferrin; D014168:Transferrin; D019809:Streptavidin; D007501:Iron