Functional characterization of a masquerade-like serine proteinase homologue from the black tiger shrimp Penaeus

Rungrat Jitvaropas1, Piti Amparyup, Paul S Gross

  • 1Shrimp Molecular Biology and Genomics Laboratory, Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok 10330, Thailand.

Insights

The black tiger shrimp

Area of Science:

  • Marine biology
  • Immunology
  • Biochemistry

Background:

  • The black tiger shrimp, Penaeus monodon, is susceptible to bacterial infections.
  • Vibrio harveyi is a significant shrimp pathogen.
  • Understanding shrimp immune responses is crucial for aquaculture.

Purpose of the Study:

  • To clone and characterize a serine proteinase homologue (PmMasSPH) from Penaeus monodon.
  • To investigate the functional roles of different domains of PmMasSPH in shrimp immunity.
  • To assess the antimicrobial and opsonic activities of PmMasSPH.

Main Methods:

  • Cloning of N-terminal and C-terminal domains of PmMasSPH into an expression vector.
  • Expression and purification of recombinant proteins in E. coli.
  • Assaying proteinase activity, hemocyte adhesion, bacterial binding, bacterial clearance, and antimicrobial activity.
  • In vivo studies to evaluate opsonic activity.

Main Results:

  • The C-terminal SP-like domain binds Vibrio harveyi and lipopolysaccharide (LPS), mediating hemocyte adhesion but lacking proteolytic activity.
  • The N-terminal region exhibits antimicrobial activity against Gram-positive bacteria.
  • PmMasSPH demonstrates opsonic activity, enhancing bacterial clearance in vivo.
  • PmMasSPH is induced upon Vibrio harveyi infection.

Conclusions:

  • PmMasSPH is a multifunctional immune molecule involved in shrimp defense against bacterial pathogens.
  • Different domains of PmMasSPH contribute to distinct immune functions, including bacterial recognition, adhesion, and clearance.
  • PmMasSPH plays a significant role in the innate immune system of Penaeus monodon.

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