Previous Article | Next Article ![]()
Journal of Clinical Microbiology, January 2005, p. 321-325, Vol. 43, No. 1
0095-1137/05/$08.00+0 doi:10.1128/JCM.43.1.321-325.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
Department of Microbiology, All India Institute of Medical Sciences,1 International Centre for Genetic Engineering and Biotechnology, New Delhi, India2
Received 28 January 2004/ Returned for modification 28 March 2004/ Accepted 3 August 2004
Mycoplasma pneumoniae is the causative agent of primary atypical pneumonia in humans. Adherence of M. pneumoniae to host cells requires several adhesin proteins, such as P1, P30, and P116. A major limitation in developing a specific diagnostic test for M. pneumoniae is the inability to express adhesin proteins in heterologous expression systems due to unusual usage of the UGA stop codon, leading to premature termination of these proteins in Escherichia coli. In the present study, we successfully expressed the C-terminal (P1-C1) and N-terminal (P1-N1) regions of the P1 protein in E. coli. On screening these recombinant proteins with sera from M. pneumoniae-infected patients, only the P1-C1 protein was found to be immunogenic. This protein can be used as an antigen for immunodiagnosis of M. pneumoniae infection, as well as in adherence inhibition studies to understand the pathophysiology of the disease.
This article has been cited by other articles:
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»