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Nucleic Acids Research, 1980, Vol. 8, No. 20 4639-4650
© 1980

MOLECULAR BIOLOGY

Monoclonal antibodies to Escherichia coli 5OS ribosomes

V. Shen, T.C. King, V. Kumar and B. Daugherty

Department of Microbiology and Immunology, Washington University School of Medicine St. Louis, MO 63110, USA

Received August 18, 1980. Hybridoma cell lines that produce monoclonal antibodies directed against 5OS ribosomal proteins have been isolated. Spleen cells (from BALB/c mice immunized with 50S ribosomal subunits extracted from Escherichia coli) were fused to mouse myeloma cell line SP2/0-Ag 14. The initial screening for antibody producing hybridomas was carried out by a double antibody sandwich method; hybridomas were subsequently cloned in soft agar. Antibodies were characterized by their specific binding to individual 50S ribosomal proteins separated on phosphocellulose cohmins and in two-dimensional polyacrylamide gels. The assignments were confirmed with purified single ribosomal proteins. Of four clones analyzed thus far, two are identical with specificity for r-protein L5. The other clones produce two different antibodies directed against r-protein L20. Each monoclonal antibody formed ribosome dimers visualizable in the electron microscope. Dimers could be reacted with a different second antibody to form chains containing 8 or more ribosomes, which may be useful for structural studies.


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