Author:
Hu P C,Schaper U,Collier A M,Clyde W A,Horikawa M,Huang Y S,Barile M F
Abstract
In previous studies with hyperimmune rabbit sera and monoclonal antibodies against the P1 protein of Mycoplasma pneumoniae, we obtained evidence of a shared antigenic determinant with a single protein of Mycoplasma genitalium. Because of biologic and morphologic similarities between these two human Mycoplasma species, attempts were made to characterize this cross-reacting protein of M. genitalium (designated MgPa). The protein was surface exposed and had an estimated molecular size of 140 kilodaltons. Electron microscopy with monoclonal antibodies produced against either MgPa or P1 demonstrated that MgPa is located over the surface of the terminal structure of M. genitalium which is covered by a nap layer. These immunologic and morphologic findings suggest that the MgPa protein of M. genitalium could be the counterpart of the P1 protein of M. pneumoniae.
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Immunology,Microbiology,Parasitology
Reference31 articles.
1. Growth, cytopathogenicity and morphology of Mycoplasma gallisepticum and Mycoplasma gallinarum in tracheal explants;Abu-Zahr M. N.;J. Comp. Pathol.,1976
2. Molecular basis for cytadsorption of Mycoplasma pneumoniae;Baseman J. B.;J. Bacteriol.,1982
3. Absence of Mycoplasma pneumoniae cytadsorption protein P1 in Mycoplasma genitalium and Mycoplasma gallisepticum;Baseman J. B.;Infect. Immun.,1984
4. Bredt W. 1979. Motility p. 141-145. In M. F. Barile and S. Razin (ed.) The mycoplasmas vol. 1. Academic Press Inc. New York.
5. Cole R. M. and T. J. Popkin. 1981. Electron microscopy and ultrastructure of bacteria p. 34-51. In P. Gerhardt (ed.) Manual of methods for general bacteriology. American Society for Microbiology Washington D.C.
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