Bioinformatics Analysis of Chlamydia psittaci MIP Protein
College of Public Health of University of South China, Key Laboratory of Hengyang for Health Hazard Factors Inspection and Quarantine, Hengyang 421001, China
Molecular Pathogens, 2020, Vol. 11, No. 1
Received: 12 May, 2020 Accepted: 12 May, 2020 Published: 12 May, 2020
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This article was first published in Genomics and Applied Biology in Chinese, and here was authorized to translate and publish the paper in English under the terms of Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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.
Chlamydia parroti; Macrophage infection potentiator; Bioinformatics analysis; Protein structure; Antigen epitope
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