Identification, characterization and deduced amino acid sequence of the dominant protease from Kudoa paniformis and K. thyrsites: a unique cytoplasmic cysteine protease

Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology
Valerie A FunkKristina M Miller

Abstract

Kudoa paniformis and Kudoa thyrsites (Myxozoa: Myxosporea) infections are associated with severe proteolysis of host muscle tissue post-mortem. The present study was undertaken to identify and characterize the protease responsible for myoliquefaction and determine mechanisms controlling protease function in vivo. N-terminal sequence analysis of partially purified protease from hake muscle infected with K. paniformis and K. thyrsites revealed a 23 amino acid sequence that aligned with cysteine proteases. Enzyme inhibition assays confirmed the presence of an essential active site cysteine residue. Using the above K. paniformis amino acid sequence data, a corresponding cDNA sequence from K. thyrsites plasmodia was elucidated revealing a cathepsin L proenzyme (Kth-CL). The translated amino acid sequence lacked a signal sequence characteristic of lysosomal and secreted proteins suggesting a unique cytoplasmic location. Only the proenzyme form of Kth-CL was present in Atlantic salmon muscle anti-mortem but this form became processed in vivo when infected muscle was stored at 4 degrees C. The proenzyme of Kth-CL showed uninhibited activity at pH 6.0, negligible activity at pH 6.5 and no measurable activity at pH 7.0 whilst the process...Continue Reading

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Citations

Oct 12, 2013·Diseases of Aquatic Organisms·Itziar EstensoroAriadna Sitjà-Bobadilla
Sep 3, 2013·Developmental and Comparative Immunology·Daniela GómezJ Oriol Sunyer
Sep 30, 2014·BMC Evolutionary Biology·Erez ShpirerDorothée Huchon
Feb 24, 2021·Trends in Parasitology·Gema Alama-Bermejo, Astrid S Holzer

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