Expression and Immunological Characterization of the Carboxy-Terminal Region of the P1 Adhesin Protein of Mycoplasma pneumoniae

Author:

Chaudhry Rama1,Nisar Nazima1,Hora Bhavna2,Chirasani Sridhar Reddy1,Malhotra Pawan2

Affiliation:

1. Department of Microbiology, All India Institute of Medical Sciences

2. International Centre for Genetic Engineering and Biotechnology, New Delhi, India

Abstract

ABSTRACT 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.

Publisher

American Society for Microbiology

Subject

Microbiology (medical)

Reference34 articles.

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4. Dallo, S. F., C. J. Su, J. R. Horton, and J. B. Baseman. 1988. Identification of P1 gene domain containing epitopes mediating Mycoplasma pneumoniae cytadherence. J. Exp. Med.167:718-773.

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