Abstract
The human respiratory pathogen Mycoplasma pneumoniae has several peculiar properties: despite its diminutive size1 it possesses a specialized tip structure2–4; it is motile and glides with considerable speed along inert surfaces5,6, and it exhibits strong attachment to animal cells7 and to inert surfaces8. The latter property is a prerequisite for the survival of this obligate parasite in the host organism. Experimental evidence9–12 suggested that the binding site(s) mediating attachment of the pathogen is a protein, but so far this substance has not been characterized, nor has it been localized in the cell. By using a monoclonal antibody we have been able to localize the adhesin at the surface of the tip structure; it was identified by autoradiography as a protein of molecular weight (Mr) 160,000–190,000. We report that the monoclonal antibody inhibited erythrocyte adherence, attachment to glass and gliding motility of M. pneumoniae.
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Feldner, J., Göbel, U. & Bredt, W. Mycoplasma pneumoniae adhesin localized to tip structure by monoclonal antibody. Nature 298, 765–767 (1982). https://doi.org/10.1038/298765a0
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DOI: https://doi.org/10.1038/298765a0
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