Author Correspondence author
Molecular Pathogens, 2020, Vol. 11, No. 3
Received: 12 May, 2020 Accepted: 12 May, 2020 Published: 12 May, 2020
To investigate the biological characteristics of Macrophage infection potentiator (MIP) of Chlamydia psittaci. Methods: The MIP gene sequences of all C. psittaci strains were retrieved and downloaded from the national biotechnology information (NCBI) center database. The homology of MIP genes was compared among different C. psittacis strains, and the amino acid sequence, physicochemical properties, transmembrane region, signal peptide, spatial structure and antigenic epitopes of MIP protein were analyzed with bioinformatics softwares. Result: The homology of MIP gene among different C. psittaci strains was 98.96% ~ 99.87%. C. psittaci MIP protein was an unstable and weak acidic hydrophilic protein, had no transmembrane domain and signal peptide andα-helix and β-turn were its major structural features. There were five dominant B cell antigen epitopes and two dominant T cell antigen epitopes in C. psittaci MIP protein. Conclusion: C. psittaci MIP is a weakly acidic, hydrophilic protein which does not participate in the transport of substances, and has T and B cell antigen epitopes indicate it can act as a good potential vaccine candidate.
(The advance publishing of the abstract of this manuscript does not mean final published, the end result whether or not published will depend on the comments of peer reviewers and decision of our editorial board.)s
(The advance publishing of the abstract of this manuscript does not mean final published, the end result whether or not published will depend on the comments of peer reviewers and decision of our editorial board.)
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