HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Baensch, M. Articles by Köhl, J. Search for Related Content PubMed PubMed Citation Articles by Baensch, M. Articles by Köhl, J. Agricola Articles by Baensch, M. Articles by Köhl, J.

Conservation of the amino-terminal epitope of elongation factor Tu in eubacteria and archaea

Institute of Medical Microbiology, Medical School Hannover, 30623 Hannover, Germany
AG Molecular Recognition, GBF (Gesellschaft für Biotechnologische Forschung), Braunschweig, Germany

ABSTRACT

An epitope of elongation factor Tu (EF-Tu), which is found in organisms in both the bacterial and archaeal domains, was recently defined by mAb 900. To localize the conserved epitope within the EF-Tu molecule and to determine its sequence, SPOTScan analysis of synthetic peptides, Western blot analysis of purified EF-Tu domains and site-directed mutagenesis studies were used. Analysis of mAb 900 binding to overlapping 15-mer peptides encompassing the complete sequence of EF-Tu of Escherichia coli was inconclusive, suggesting three distinct regions may be epitopes. Western blot analysis of EF-Tu domains 1-3 of Thermus thermophilus suggested that the epitope was located at the N terminus. This was confirmed by site-directed mutagenesis of EF-Tu domain 1 of Mycoplasma hominis. By C-terminal truncation of the N-terminal 15-mer peptide the epitope was mapped to EF-Tu residues 1-6. Replacement of each of the residues in the epitope peptide demonstrated that only positions 5 and 6 were indispensable for antibody binding. These data provide evidence that the highly conserved epitope recognized by mAb 900 in the bacterial and archaeal domains is located at the very end of the N terminus of the EF-Tu molecule.

^*Author for correspondence: Jörg Köhl. Tel: +49 511 532 4340. Fax: +49 511 532 4366. e-mail: Koehl.Joerg@MH-Hannover.DE

This article has been cited by other articles:

				G. Kunze, C. Zipfel, S. Robatzek, K. Niehaus, T. Boller, and G. Felix The N Terminus of Bacterial Elongation Factor Tu Elicits Innate Immunity in Arabidopsis Plants PLANT CELL, December 1, 2004; 16(12): 3496 - 3507. [Abstract] [Full Text] [PDF]