Mapping of conformational epitopes of monoclonal antibodies against Escherichia coli penicillin-binding protein 1B (PBP 1B) by means of hybrid protein analysis: implications for the tertiary structure of PBP 1B.
We have analyzed the location of the epitope areas of the four monoclonal antibody groups against penicillin-binding protein 1B (PBP 1B; T. den Blaauwen, F. B. Wientjes, A. H. J. Kolk, B. G. Spratt, and N. Nanninga, J. Bacteriol. 171:1393-1401). They could be specified by studying monoclonal antibody binding patterns to amino- and carboxy-terminal truncated PBP 1B molecules. Monoclonal antibodies against conformational epitopes, with the exception of one epitope area, did not recognize PBP 1B molecules that had not been translocated across the membrane. Apparently, translocation is required for PBP 1B to fully obtain its native conformation.
Den Blaauwen
T
T
Department of Molecular Cell Biology, University of Amsterdam, The Netherlands.
Pas
E
E
Edelman
A
A
Spratt
B G
BG
Nanninga
N
N
D000911:Antibodies, Monoclonal / Q000276:immunology*; D001426:Bacterial Proteins; D015153:Blotting, Western; D002352:Carrier Proteins / Q000235:genetics / Q000276:immunology*; D003001:Cloning, Molecular; D004252:DNA Mutational Analysis; D000939:Epitopes; D004926:Escherichia coli / Q000235:genetics / Q000276:immunology*; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase / Q000235:genetics / Q000276:immunology*; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases; D011487:Protein Conformation; D011993:Recombinant Fusion Proteins / Q000276:immunology; D013329:Structure-Activity Relationship
D000911:Antibodies, Monoclonal; D001426:Bacterial Proteins; D002352:Carrier Proteins; D000939:Epitopes; D046915:Penicillin-Binding Proteins; D011993:Recombinant Fusion Proteins; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase