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 Citation Map 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 Kolberg, J. Articles by Sletten, K. Search for Related Content PubMed PubMed Citation Articles by Kolberg, J. Articles by Sletten, K. Agricola Articles by Kolberg, J. Articles by Sletten, K.

Monoclonal Antibodies Against Streptococcus Pneumoniae Detect Epitopes on Eubacterial Ribosomal Proteins L7/L12 and on Streptococcal Elongation Factor Ts

¹National Institute of Public Health, Departments of Vaccinology, PO Box 4404 Torshov, N-0403 Oslo, Norway
²National Institute of Public Health, Departments of Bacteriology, PO Box 4404 Torshov, N-0403 Oslo, Norway
³Biotechnology Centre of Oslo and Department of Biochemistry, University of Oslo, Gaustadailéen 21, N-0371 Oslo, Norway

ABSTRACT

Two monoclonal antibodies (mAbs) designated 144,H-3 (lgG2a) and 218,C-5 (lgM) were produced after immunization of mice with two different heattreated and sonicated pneumococcal strains. Western blotting, with solubilized proteins from different bacterial genera and from mammalian lymphocytes, showed that both mAbs reacted with a protein of approximately 12 kDa in all 66 strains of eubacteria examined, representing 27 different species. The 12 kDa protein was isolated by immunoaffinity chromatography. Subsequent preparative Western blotting enabled N-terminal amino acid sequence analysis by microsequencing. A high degree of amino acid sequence similarity with eubacterial ribosomal proteins L7/L12 was demonstrated. One of the mAbs (144,H-3) also cross-reacted in Western blotting with a 43 kDa protein, but only from streptococci. The 43 kDa protein carrying the common streptococcal epitope was isolated and sequenced in the N-terminal region. A high degree of amino acid sequence identity was found to elongation factor Ts from Escherichia coli.

⁴Author for correspondence: Jan Kolberg. Tel: +47 2 204 2660. Fax: +47 2 235 3605.

This article has been cited by other articles:

				R. O. Mattos-Graner, K. A. Porter, D. J. Smith, Y. Hosogi, and M. J. Duncan Functional Analysis of Glucan Binding Protein B from Streptococcus mutans J. Bacteriol., June 1, 2006; 188(11): 3813 - 3825. [Abstract] [Full Text] [PDF]

				R. Govind, G. Vediyappan, R. D. Rolfe, and J. A. Fralick Evidence that Clostridium difficile TcdC Is a Membrane-Associated Protein. J. Bacteriol., May 1, 2006; 188(10): 3716 - 3720. [Abstract] [Full Text] [PDF]

				J. Kolberg, A. Aase, S. Bergmann, T. K. Herstad, G. Rodal, R. Frank, M. Rohde, and S. Hammerschmidt Streptococcus pneumoniae enolase is important for plasminogen binding despite low abundance of enolase protein on the bacterial cell surface. Microbiology, May 1, 2006; 152(Pt 5): 1307 - 1317. [Abstract] [Full Text] [PDF]

				T. E. Michaelsen, O. Ihle, K. J. Beckstrom, T. K. Herstad, J. Kolberg, E. A. Hoiby, and A. Aase Construction and Functional Activities of Chimeric Mouse-Human Immunoglobulin G and Immunoglobulin M Antibodies against the Neisseria meningitidis PorA P1.7 and P1.16 Epitopes Infect. Immun., October 1, 2003; 71(10): 5714 - 5723. [Abstract] [Full Text] [PDF]

				E. Rosenqvist, A. Musacchio, A. Aase, E. A. Hoiby, E. Namork, J. Kolberg, E. Wedege, A. Delvig, R. Dalseg, T. E. Michaelsen, et al. Functional Activities and Epitope Specificity of Human and Murine Antibodies against the Class 4 Outer Membrane Protein (Rmp) of Neisseria meningitidis Infect. Immun., March 1, 1999; 67(3): 1267 - 1276. [Abstract] [Full Text] [PDF]