Skip to main content
ARS Home » Southeast Area » Auburn, Alabama » Aquatic Animal Health Research » Research » Publications at this Location » Publication #273331

Research Project: Integrated Aquatic Animal Health Strategies

Location: Aquatic Animal Health Research

Title: Over-expression, purification and immune responses to Aeromonas hydrophila AL09-73 flagellar proteins

item Yeh, Hung-yueh
item Klesius, Phillip

Submitted to: Fish and Shellfish Immunology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 9/18/2011
Publication Date: 11/15/2011
Publication URL:
Citation: Yeh, H., Klesius, P.H. 2011. Over-expression, purification and immune responses to Aeromonas hydrophila AL09-73 flagellar proteins. Fish and Shellfish Immunology. 31:1278-1283.

Interpretive Summary: Aeromonas hydrophila is found in every aquatic environments and causes many human and fish diseases. Recent outbreaks of aeromonad hemorrhagic septicemia in channel catfish in the states of Alabama, Mississippi and Arkansas have caused huge economic losses to the catfish producers. Development of vaccines is one of powerful means for this disease control and will minimize losses caused by this microorganism. Nineteen A. hydrophila flagellar proteins were produced and characterized in an E. coli bacterial expression system. These recombinant proteins can be used for the subunit vaccine development and studying catfish antibody response to each flagellar components after infection. This study is related to the goal of ARS National Program 106-Aquaculture, Component 4C-Prevention of Diseases.

Technical Abstract: Aeromonas hydrophila is ubiquitous in aquatic environments worldwide and causes many diseases in fish as well as human. Recent outbreaks of aeromonad diseases in channel catfish prompted us to investigate catfish immune responses during infection of A. hydrophila. In this communication, we report to amplify, over-express, purify and characterize 19 A. hydrophila flagellar proteins. All recombinant proteins were confirmed by nucleotide sequencing of expression plasmids, SDS-PAGE analysis and His tag Western blot of induced proteins. Our preliminary result also showed that the purified recombinant FlgK protein reacted strongly to sera from experimentally infected catfish, suggesting that this protein has potential for a novel target for vaccine development. It is also anticipated that these recombinant proteins will provide us with very useful tools to investigate host immune response to this microorganism.