Molecular cloning and sequence analysis of lamB encoding outer membrane maltose-inducible porin of Aeromonas
Tanuja Upadhyaya1, Rajesh K Singh, Aparna Dixit
1Gene Regulation Laboratory, Centre for Biotechnology, Jawaharlal Nehru University, New Delhi, India.
Abstract:
Aeromonas hydrophila is a significantly important pathogen causing major diseases in humans and fresh water fish. The outer membrane proteins (OMP) which are strong immunogens have been reported to act as adhesins aiding in the attachment of enteropathogenic bacteria. It is of interest to investigate the role of OMP in pathogenesis and their potential as vaccine candidates. In our laboratory, we cloned the gene encoding channel protein LamB porin of A. hydrophila. DNA sequence analysis revealed a full length gene of 1345 bp having a high level of homology with the lamB gene of different bacteria. Open reading frame of A. hydrophila lamB consists of a signal peptide of 25 amino acids, two protein translation start sites ATG present at the 31st and 37th base pairs, a translation termination codon, TAA at 1333rd base pair.
Insights
This study cloned the Aeromonas hydrophila LamB porin gene, revealing its high homology with other bacterial lamB genes. This research explores outer membrane proteins (OMP) for potential vaccine development against A. hydrophila infections.
Area of Science:
- Microbiology
- Molecular Biology
- Immunology
Background:
- Aeromonas hydrophila is a significant pathogen affecting humans and freshwater fish.
- Outer membrane proteins (OMP) are immunogenic and act as adhesins in bacterial pathogenesis.
- Investigating OMP roles is crucial for understanding pathogenesis and developing vaccines.
Purpose of the Study:
- To clone and analyze the gene encoding the LamB porin of Aeromonas hydrophila.
- To explore the potential of A. hydrophila OMP as vaccine candidates.
Main Methods:
- Cloning of the A. hydrophila LamB porin gene.
- DNA sequence analysis of the cloned gene.
- Homology analysis with known bacterial lamB genes.
Main Results:
- A full-length gene of 1345 bp was successfully cloned.
- The A. hydrophila lamB gene exhibits high homology with homologous genes in other bacteria.
- Sequence analysis identified a signal peptide, translation start sites (ATG), and a termination codon (TAA).
Conclusions:
- The cloned LamB porin gene provides a basis for further studies on its role in A. hydrophila pathogenesis.
- Understanding the structure and function of LamB porin can contribute to the development of novel vaccines against A. hydrophila.
