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Biomimetic Materials to Characterize Bacteria-host Interactions
Published on: November 16, 2015
Proteolytic activation of Vibrio mimicus (Vm) major outer membrane protein haemagglutinin (HA) with Vm-HA/protease:
Munirul Alam1, Shin-ichi Miyoshi, Kabir Uddin Ahmed
1Laboratory of Enteric Microbiology, International Center for Diarrhoeal Disease Research, Dhaka, Bangladesh. munirul@icddrb.org
Abstract:
Vibrio mimicus (Vm) haemagglutinins (HAs), such as an extracellular HA/protease (Vm-HA/protease) and a major outer membrane protein-HA (Vm-OMPHA), have been recognized as the putative adherence factors for the bacterium. However, the mechanism by which HAs coordinate the adherence function of the bacterium remains as yet unknown. We report herein the positive interaction between Vm-HA/protease and Vm-OMPHA resulting in significant enhancement of the haemagglutinating ability. In this interaction, no cleaved polypeptide was detected; however, limited proteolysis of Vm-OMPHA was confirmed by SDS-PAGE. The proteolytic activation of the native cell-associated Vm-OMPHA by limited proteolysis was also demonstrated in several V. mimicus strains. Proteolytic activation of OMPHA was also achieved with various proteases from bacterial and eukaryotic sources. These findings may indicate a novel coordination of V. mimicus HAs in the adherence of the bacterium.
Insights
Vibrio mimicus haemagglutinins interact, enhancing bacterial adherence. This study reveals a novel mechanism involving outer membrane protein activation, crucial for Vibrio mimicus adhesion.
Area of Science:
- Microbiology
- Bacterial Pathogenesis
- Molecular Biology
Background:
- Vibrio mimicus haemagglutinins (HAs), including extracellular HA/protease and outer membrane protein-HA (OMPHA), are known adherence factors.
- The precise mechanism coordinating these HAs for bacterial adherence is not fully understood.
Purpose of the Study:
- To investigate the interaction between Vibrio mimicus HA/protease and OMPHA.
- To elucidate the mechanism by which these haemagglutinins contribute to bacterial adherence.
Main Methods:
- Investigated the interaction between Vm-HA/protease and Vm-OMPHA.
- Utilized SDS-PAGE to confirm limited proteolysis of Vm-OMPHA.
- Demonstrated proteolytic activation of cell-associated Vm-OMPHA in various V. mimicus strains.
- Tested activation using proteases from bacterial and eukaryotic sources.
Main Results:
- A positive interaction between Vm-HA/protease and Vm-OMPHA was identified, significantly enhancing haemagglutinating ability.
- Limited proteolysis of Vm-OMPHA was observed, although no cleaved polypeptide was detected.
- Proteolytic activation of native cell-associated Vm-OMPHA was confirmed across multiple V. mimicus strains.
- External proteases also induced proteolytic activation of OMPHA.
Conclusions:
- Findings suggest a novel coordination mechanism for Vibrio mimicus haemagglutinins in bacterial adherence.
- The interaction and proteolytic activation of Vm-OMPHA represent a key aspect of V. mimicus adhesion.
- This study provides new insights into the molecular basis of Vibrio mimicus pathogenesis.
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